|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-768 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 1373.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 179 ESGAGKTVNTKRVIQYFASIAAIGDrgKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSK--KKKESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd01377 159 IAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 339 VLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd01377 239 ILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 419 QQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd01377 319 EQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 499 QEEYKKEGIEWTFIDFGMDLQACIDLIEKP-MGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRnvKGKQEAH 577
Cdd:cd01377 399 QEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPK--PKKSEAH 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 578 FSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADTADsskgKGGKKKGSSFQTVSALHRENL 657
Cdd:cd01377 477 FILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGG----GKKKKKGGSFRTVSQLHKEQL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 658 NKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 737
Cdd:cd01377 553 NKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFD 632
|
650 660 670
....*....|....*....|....*....|.
gi 431907173 738 iDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01377 633 -DGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
99-768 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 1350.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 179 ESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 339 VLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 419 QQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 499 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 578
Cdd:cd14916 401 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 579 SLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADTADSSKGKGGKKKGSSFQTVSALHRENLN 658
Cdd:cd14916 481 SLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSSFQTVSALHRENLN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 659 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 738
Cdd:cd14916 561 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 640
|
650 660 670
....*....|....*....|....*....|
gi 431907173 739 DSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14916 641 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
99-768 |
0e+00 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 1318.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 179 ESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANAnKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKM-KGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 339 VLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14913 240 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 419 QQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14913 320 DQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 499 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 578
Cdd:cd14913 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 579 SLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADtADSSKGKGGKKKGSSFQTVSALHRENLN 658
Cdd:cd14913 480 SLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATAD-ADSGKKKVAKKKGSSFQTVSALFRENLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 659 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 738
Cdd:cd14913 559 KLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFI 638
|
650 660 670
....*....|....*....|....*....|
gi 431907173 739 DSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14913 639 DSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
99-768 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 1278.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 179 ESGAGKTVNTKRVIQYFASIAAIGDRGKKDNAnANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQT-PGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 339 VLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14917 240 VLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 419 QQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14917 320 QQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 499 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 578
Cdd:cd14917 400 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAHF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 579 SLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADtADSSKGKGGKKKGSSFQTVSALHRENLN 658
Cdd:cd14917 480 SLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGAD-APIEKGKGKAKKGSSFQTVSALHRENLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 659 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 738
Cdd:cd14917 559 KLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 638
|
650 660 670
....*....|....*....|....*....|
gi 431907173 739 DSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14917 639 DSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
100-768 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 1228.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 180 SGAGKTVNTKRVIQYFASIAAIGDR-GKKDNANANK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 256
Cdd:cd14927 82 SGAGKTVNTKRVIQYFAIVAALGDGpGKKAQFLATKtgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 257 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSA 336
Cdd:cd14927 162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 337 FDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 416
Cdd:cd14927 242 MDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 417 SVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14927 322 SVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 497 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPR-NVKGKQE 575
Cdd:cd14927 402 LEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRpDKKRKYE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 576 AHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADTAD--SSKGKGGKKKGSSFQTVSALH 653
Cdd:cd14927 482 AHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDSTEdpKSGVKEKRKKAASFQTVSQLH 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 654 RENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 733
Cdd:cd14927 562 KENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIP 641
|
650 660 670
....*....|....*....|....*....|....*
gi 431907173 734 EGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14927 642 DDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
99-768 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 1180.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 179 ESGAGKTVNTKRVIQYFASIAAIGDRgKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEK-KKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14918 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 339 VLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14918 240 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 419 QQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14918 320 QQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 499 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 578
Cdd:cd14918 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 579 SLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADtADSSKGKGGKKKGSSFQTVSALHRENLN 658
Cdd:cd14918 480 SLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAE-ADSGAKKGAKKKGSSFQTVSALFRENLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 659 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 738
Cdd:cd14918 559 KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFI 638
|
650 660 670
....*....|....*....|....*....|
gi 431907173 739 DSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14918 639 DSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
99-768 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 1175.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 179 ESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 339 VLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 419 QQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14923 321 QQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 499 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 578
Cdd:cd14923 401 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 579 SLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADTADS-SKGKGGKKKGSSFQTVSALHRENL 657
Cdd:cd14923 481 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSgGSKKGGKKKGSSFQTVSAVFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 658 NKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 737
Cdd:cd14923 561 NKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 431907173 738 IDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14923 641 IDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-768 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 1163.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 179 ESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANAN-KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAF 337
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 338 DVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 418 VQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 498 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAH 577
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 578 FSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADTADSSKGKGGKKKGSSFQTVSALHRENL 657
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 658 NKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 737
Cdd:cd14910 561 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 431907173 738 IDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14910 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
99-768 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 1159.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 179 ESGAGKTVNTKRVIQYFASIAAIGDRgKKDNANANK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 256
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEK-KKEEAASGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 257 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSA 336
Cdd:cd14915 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 337 FDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 416
Cdd:cd14915 240 VDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 417 SVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 497 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEA 576
Cdd:cd14915 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 577 HFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADTADSSKGKGGKKKGSSFQTVSALHREN 656
Cdd:cd14915 480 HFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGGGKKGGKKKGSSFQTVSALFREN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 657 LNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQ 736
Cdd:cd14915 560 LNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 639
|
650 660 670
....*....|....*....|....*....|..
gi 431907173 737 FIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14915 640 FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-768 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 1146.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 179 ESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANAN-KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAF 337
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 338 DVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 418 VQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 498 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAH 577
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 578 FSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASA--DTADSSKGKGGKKKGSSFQTVSALHRE 655
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAegASAGGGAKKGGKKKGSSFQTVSALFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 656 NLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEG 735
Cdd:cd14912 561 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 640
|
650 660 670
....*....|....*....|....*....|...
gi 431907173 736 QFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14912 641 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-768 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1119.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 87 IEDMAMLTFLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 167 TDRENQSILITGESGAGKTVNTKRVIQYFASIAAIGDRGkkdnanaNKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFG 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAG-------NVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 247 KFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTnNPYDYAFVSQ-GEVSVASID 325
Cdd:pfam00063 154 KYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT-NPKDYHYLSQsGCYTIDGID 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 326 DSEELMATDSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRV 405
Cdd:pfam00063 233 DSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 406 KVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQ-PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNE 484
Cdd:pfam00063 313 KTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYVNE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 485 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLYDNHlGKSNN 563
Cdd:pfam00063 393 KLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 564 FQKPRNvkgKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADTADSSKGKGG---K 640
Cdd:pfam00063 471 FQKPRL---QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKStpkR 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 641 KKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 720
Cdd:pfam00063 548 TKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEF 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 431907173 721 RQRYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:pfam00063 628 VQRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
99-768 |
0e+00 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 1090.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 179 ESGAGKTVNTKRVIQYFASIAAIGDRGKKdnananKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKK------LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKpDLLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14929 155 LSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 339 VLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14929 234 ILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 419 QQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14929 314 EQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 499 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 578
Cdd:cd14929 394 QEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHF 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 579 SLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADTAdSSKGKGGKKKGSSFQTVSALHRENLN 658
Cdd:cd14929 474 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSA-IQFGEKKRKKGASFQTVASLHKENLN 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 659 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 738
Cdd:cd14929 553 KLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFV 632
|
650 660 670
....*....|....*....|....*....|
gi 431907173 739 DSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14929 633 SSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-780 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 1053.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 80 NPPKFDKIEDMAMLTFLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISD 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 160 NAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFASIAAigdrgkkdnANANKGTLEDQIIQANPALEAFGNAKTVRN 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG---------SNTEVGSVEDQILESNPILEAFGNAKTLRN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 240 DNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNnPYDYAFVSQG-E 318
Cdd:smart00242 152 NNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQGgC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 319 VSVASIDDSEELMATDSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQA-EPDGTEDADKSAYLMGLNSADLL 397
Cdd:smart00242 231 LTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEELE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 398 KGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQL 477
Cdd:smart00242 311 KALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 478 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLYdN 556
Cdd:smart00242 391 CINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLN-Q 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 557 HLGKSNNFQKPRNvkgKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADTADsskg 636
Cdd:smart00242 469 HHKKHPHFSKPKK---KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAGSK---- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 637 kggkkkgSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRIL 716
Cdd:smart00242 542 -------KRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLP 614
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 431907173 717 YGDFRQRYRILNPAAIPEGQFiDSRKGAEKLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRD 780
Cdd:smart00242 615 FDEFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
100-768 |
0e+00 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 1029.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14934 2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 180 SGAGKTVNTKRVIQYFASIAAIGDRgkkdnANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd14934 82 SGAGKTENTKKVIQYFANIGGTGKQ-----SSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFDV 339
Cdd:cd14934 157 AGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 340 LGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQ 419
Cdd:cd14934 237 LGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNME 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 420 QVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 499
Cdd:cd14934 317 QCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 500 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNVKGK-QEAHF 578
Cdd:cd14934 397 EEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAHF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 579 SLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADTAdsskgkGGKKKGSSFQTVSALHRENLN 658
Cdd:cd14934 477 ELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAGS------KKQKRGSSFMTVSNFYREQLN 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 659 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFI 738
Cdd:cd14934 551 KLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FV 629
|
650 660 670
....*....|....*....|....*....|
gi 431907173 739 DSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14934 630 DNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-768 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 1018.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 179 ESGAGKTVNTKRVIQYFASIAAigdRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGA---SKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14909 158 LAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 339 VLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14909 238 ILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 419 QQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14909 318 QQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 499 QEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNVK-GKQEAH 577
Cdd:cd14909 398 QEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQAAH 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 578 FSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADTADSSKGKGGKKKGSSFQTVSALHRENL 657
Cdd:cd14909 478 FAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 658 NKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQf 737
Cdd:cd14909 558 NSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE- 636
|
650 660 670
....*....|....*....|....*....|.
gi 431907173 738 iDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14909 637 -DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
31-1428 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 897.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 31 FDIRTECFVPDDKEEFVKAKIVSRE--GGKVTAE--TENGKTVTLKEDQVLQ--QNPPKFDKIEDMAMLTFLHEPAVLYN 104
Cdd:COG5022 6 AEVGSGCWIPDEEKGWIWAEIIKEAfnKGKVTEEgkKEDGESVSVKKKVLGNdrIKLPKFDGVDDLTELSYLNEPAVLHN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 105 LKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGK 184
Cdd:COG5022 86 LEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 185 TVNTKRVIQYFASIAAigdrgkkdNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADI 264
Cdd:COG5022 166 TENAKRIMQYLASVTS--------SSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 265 ETYLLEKSRVIFQLKAERNYHIFYQILSNKkPDLLDMLLVTNNPYDYAFVSQGEV-SVASIDDSEELMATDSAFDVLGFT 343
Cdd:COG5022 238 ETYLLEKSRVVHQNKNERNYHIFYQLLAGD-PEELKKLLLLQNPKDYIYLSQGGCdKIDGIDDAKEFKITLDALKTIGID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 344 PEEKAGVYKLTGAIMHYGNMKFKqKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYY 423
Cdd:COG5022 317 EEEQDQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 424 SIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYK 503
Cdd:COG5022 396 IRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 504 KEGIEWTFIDFgMDLQACIDLIEK--PMGIMSILEEECMFPKATDMTFKAKLYDN-HLGKSNNFQKPRNVKGKqeahFSL 580
Cdd:COG5022 476 KEGIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNK----FVV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 581 IHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADTadsskgkggkkkGSSFQTVSALHRENLNKL 660
Cdd:COG5022 551 KHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIES------------KGRFPTLGSRFKESLNSL 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 661 MTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI-- 738
Cdd:COG5022 619 MSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwk 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 739 -DSRKGAEKLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERLSRIITRIQAQARGQLMRIEFKKMVERRDALLVIQ 817
Cdd:COG5022 699 eDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQ 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 818 WNIRAFMGVKNWPWMKLYFKIKPLLKSAETEKEM---------------------ANMKEEFGR----LKETLEKSEARR 872
Cdd:COG5022 779 HGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYrsylaciiklqktikrekklrETEEVEFSLkaevLIQKFGRSLKAK 858
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 873 K--ELEEKMVSLLQEKNDLQL---QVQAEQD-----------NLNDAEE----RCDQ----LIKNKIQLE--AKVKEMNE 926
Cdd:COG5022 859 KrfSLLKKETIYLQSAQRVELaerQLQELKIdvksisslklvNLELESEiielKKSLssdlIENLEFKTEliARLKKLLN 938
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 927 --RLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLakveKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEA 1004
Cdd:COG5022 939 niDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLL----KKSTILVREGNKANSELKNFKKELAELSKQYGALQES 1014
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1005 HQQ------ALDDLQAEEDKVNTLTKSKvKLEQQVDDLEGSLEQEKK------VRMDLERAKRKLEGDLKLTQES----- 1067
Cdd:COG5022 1015 TKQlkelpvEVAELQSASKIISSESTEL-SILKPLQKLKGLLLLENNqlqaryKALKLRRENSLLDDKQLYQLEStenll 1093
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1068 ----IMDLENDKLQLEEKLKKKEFDISQQ-NSKIEDE-QALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDL 1141
Cdd:COG5022 1094 ktinVKDLEVTNRNLVKPANVLQFIVAQMiKLNLLQEiSKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPP 1173
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1142 SRELEEISER----LEEAGGATSVQIEMNK-KREAEFQKMRRDLEEatlqheataaalrkkhADSVAELGEQIDNLQRVK 1216
Cdd:COG5022 1174 FAALSEKRLYqsalYDEKSKLSSSEVNDLKnELIALFSKIFSGWPR----------------GDKLKKLISEGWVPTEYS 1237
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1217 QKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLND--FTTQQAKLQTENGELARQLE 1294
Cdd:COG5022 1238 TSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINVglFNALRTKASSLRWKSATEVN 1317
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1295 EKEALISQLTRgklsyTQQTEDLKRQLEEEGKA-------KNALAHaLQSARhdcDLLREQYEEETEA-KAELQRVLSKA 1366
Cdd:COG5022 1318 YNSEELDDWCR-----EFEISDVDEELEELIQAvkvlqllKDDLNK-LDELL---DACYSLNPAEIQNlKSRYDPADKEN 1388
|
1450 1460 1470 1480 1490 1500 1510
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1367 NSEvAQWRTKYETDAIQRTEELEEAKLQDAEEAVEAVNA--------KCSSLEKTKhRLQNEIEDLMVDV 1428
Cdd:COG5022 1389 NLP-KEILKKIEALLIKQELQLSLEGKDETEVHLSEIFSeekslislDRNSIYKEE-VLSSLSALLTKEK 1456
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-768 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 863.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKR-SEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 178 GESGAGKTVNTKRVIQYFASIAAigdrGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSG----SGSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDML----LVTNNPYDYAFVSQGEVSVASIDDSEELMAT 333
Cdd:cd00124 157 RLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELklelLLSYYYLNDYLNSSGCDRIDGVDDAEEFQEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 334 DSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREE--QAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEY 411
Cdd:cd00124 237 LDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGET 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 412 VTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATL--ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 489
Cdd:cd00124 317 ITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALspTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 490 FNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPR 568
Cdd:cd00124 397 FNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 569 NVKGkqeaHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSlklmatlfssyasadtadsskgkggkkkgssfqt 648
Cdd:cd00124 476 KAKL----EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS---------------------------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 649 vsaLHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 728
Cdd:cd00124 518 ---QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILA 594
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 431907173 729 PAAiPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd00124 595 PGA-TEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-768 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 815.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 180 SGAGKTVNTKRVIQYFASIAAIGDRG------KKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHF 253
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVAASKPKGsgavphPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 254 GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVtNNPYDYAFVSQGEVSVASIDDSEELMAT 333
Cdd:cd14911 162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFIL-DDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 334 DSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 412
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNTV-AQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 413 TKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFN 491
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 492 HHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLgksnnfQKPRNVK 571
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS------MHPKFMK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 572 G--KQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLF---SSYASADTADSSKGKGGKKKGSSF 646
Cdd:cd14911 474 TdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWkdaEIVGMAQQALTDTQFGARTRKGMF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 647 QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 726
Cdd:cd14911 554 RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 431907173 727 LNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14911 634 LTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
100-768 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 781.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 180 SGAGKTVNTKRVIQYFASIAAiGDRGKKDnaNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd14920 82 SGAGKTENTKKVIQYLAHVAS-SHKGRKD--HNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDL-LDMLLVTNNpyDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14920 159 VGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 339 VLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd14920 237 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENTV-AQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 418 VQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQpRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14920 316 KEQADFAVEALAKATYERLFRWLVHRINKALDRTK-RQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 496 VLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLyDNHLGKSNNFQKPRNVKG 572
Cdd:cd14920 395 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKL-VQEQGSHSKFQKPRQLKD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 573 kqEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFS-------SYASADTADSSKGKGGKKKGSS 645
Cdd:cd14920 474 --KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKdvdrivgLDQVTGMTETAFGSAYKTKKGM 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 646 FQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 725
Cdd:cd14920 552 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 431907173 726 ILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14920 632 ILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
100-768 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 732.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14932 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 180 SGAGKTVNTKRVIQYFASIAAiGDRGKKDNANA--NKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd14932 82 SGAGKTENTKKVIQYLAYVAS-SFKTKKDQSSIalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKpDLLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAF 337
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAG-DKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 338 DVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 416
Cdd:cd14932 240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDTA-AQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 417 SVQQVYYSIGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14932 319 TQEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 496 VLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLYdNHLGKSNNFQKPRnvKG 572
Cdd:cd14932 399 ILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPK--KL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 573 KQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADTADSSKGKGGKKK------GSSF 646
Cdd:cd14932 476 KDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHgafktrKGMF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 647 QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 726
Cdd:cd14932 556 RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 431907173 727 LNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14932 636 LTPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
99-768 |
0e+00 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 713.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 178 GESGAGKTVNTKRVIQYFASIAAigdrgkkdnANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATVGG---------SSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAF 337
Cdd:cd01380 152 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 338 DVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd01380 232 TLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 418 VQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQP--RQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd01380 312 LQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 496 VLEQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNN-FQKPRNVKGKq 574
Cdd:cd01380 392 KLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNKhFKKPRFSNTA- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 575 eahFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMatlfssyasadtadsskgkggkkkgssfqTVSALHR 654
Cdd:cd01380 470 ---FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNRKK-----------------------------TVGSQFR 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 655 ENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAipE 734
Cdd:cd01380 518 DSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK--E 595
|
650 660 670
....*....|....*....|....*....|....
gi 431907173 735 GQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01380 596 WLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
100-768 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 709.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14921 2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 180 SGAGKTVNTKRVIQYFASIAAiGDRGKKDNANAnkGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd14921 82 SGAGKTENTKKVIQYLAVVAS-SHKGKKDTSIT--GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLL-DMLLVTNNpyDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14921 159 VGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRsDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETLEAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 339 VLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd14921 237 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNTA-AQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 418 VQQVYYSIGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14921 316 KEQADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 497 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLYDNHlGKSNNFQKPRNVKGK 573
Cdd:cd14921 396 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKPKQLKDK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 574 QEahFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSY-------ASADTADSSKGKGGKKKGSSF 646
Cdd:cd14921 475 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldQMAKMTESSLPSASKTKKGMF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 647 QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 726
Cdd:cd14921 553 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 431907173 727 LNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14921 633 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
100-768 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 695.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14919 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 180 SGAGKTVNTKRVIQYFASIAAiGDRGKKDnananKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd14919 82 SGAGKTENTKKVIQYLAHVAS-SHKSKKD-----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVtnNPYD-YAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14919 156 VGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 339 VLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd14919 234 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNTA-AQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 418 VQQVYYSIGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14919 313 KEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 497 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLYDNHlGKSNNFQKPRNVKGK 573
Cdd:cd14919 393 LEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 574 qeAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSY-------ASADTADSSKGKGGKKKGSSF 646
Cdd:cd14919 472 --ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldQVAGMSETALPGAFKTRKGMF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 647 QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 726
Cdd:cd14919 550 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 431907173 727 LNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14919 630 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
100-768 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 692.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd15896 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 180 SGAGKTVNTKRVIQYFASIAAiGDRGKKDNAN--ANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd15896 82 SGAGKTENTKKVIQYLAHVAS-SHKTKKDQNSlaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNPyDYAFVSQGEVSVASIDDSEELMATDSAF 337
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYN-NYRFLSNGNVTIPGQQDKDLFTETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 338 DVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 416
Cdd:cd15896 240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASmPDNTA-AQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 417 SVQQVYYSIGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd15896 319 TQEQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 496 VLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLYDNHlGKSNNFQKPRnvKG 572
Cdd:cd15896 399 ILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKPK--KL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 573 KQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADTADSSKGKGG-----KKKGSSFQ 647
Cdd:cd15896 476 KDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSEmpgafKTRKGMFR 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 648 TVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 727
Cdd:cd15896 556 TVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 635
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 431907173 728 NPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd15896 636 TPNAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
100-768 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 669.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14930 2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 180 SGAGKTVNTKRVIQYFASIAAiGDRGKKDNANAnkGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd14930 82 SGAGKTENTKKVIQYLAHVAS-SPKGRKEPGVP--GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNPYdYAFVSQGEVSVASiDDSEELMATDSAFDV 339
Cdd:cd14930 159 VGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 340 LGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd14930 237 LGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNTA-AQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 419 QQVYYSIGALAKAVYEKMFNWMVTRINATLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14930 316 EQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 497 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLYDNHlGKSNNFQKPRNVkgK 573
Cdd:cd14930 395 LEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRHL--R 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 574 QEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADTADSSKGKGG-----KKKGSSFQT 648
Cdd:cd14930 472 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDgppggRPRRGMFRT 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 649 VSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 728
Cdd:cd14930 552 VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 631
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 431907173 729 PAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14930 632 PNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-768 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 659.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 180 SGAGKTVNTKRVIQYFASIAAigdrgkkdNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSG--------GSESEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFDV 339
Cdd:cd01378 154 VGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 340 LGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEY---VTKGQ 416
Cdd:cd01378 234 IGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISDTSV-LDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 417 SVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQ-YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHhmF 495
Cdd:cd01378 313 NVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE--L 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 496 VL--EQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFP-KATDMTFKAKLyDNHLGKSNNFQKPRNVK 571
Cdd:cd01378 391 TLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGHF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 572 GKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSsyasaDTADSSKGKGGKkkgssfqTVSA 651
Cdd:cd01378 469 ELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFP-----EGVDLDSKKRPP-------TAGT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 652 LHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAA 731
Cdd:cd01378 537 KFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKT 616
|
650 660 670
....*....|....*....|....*....|....*..
gi 431907173 732 IPEGQFIDsRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01378 617 WPAWDGTW-QGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
100-768 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 653.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 180 SGAGKTVNTKRVIQYFASIAaigdrGKKDnanankgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd01381 82 SGAGKTESTKLILQYLAAIS-----GQHS-------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTnNPYDYAFVSQGE-VSVASIDDSEELMATDSAFD 338
Cdd:cd01381 150 EGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELG-DASDYYYLTQGNcLTCEGRDDAAEFADIRSAMK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 339 VLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQRE--EQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 416
Cdd:cd01381 229 VLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 417 SVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYF---IGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 493
Cdd:cd01381 309 SAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRH 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 494 MFVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLYDNHlGKSNNFQKPRNvkg 572
Cdd:cd01381 389 IFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKPKS--- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 573 KQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSY--ASADTADSSkgkggkkkgssfQTVS 650
Cdd:cd01381 464 DLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDisMGSETRKKS------------PTLS 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 651 ALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPa 730
Cdd:cd01381 532 SQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP- 610
|
650 660 670
....*....|....*....|....*....|....*...
gi 431907173 731 AIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01381 611 GIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
99-768 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 648.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRgkKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 179 ESGAGKTVNTKRVIQYFASIAAiGDRGkkdnanankgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd01383 79 ESGAGKTETAKIAMQYLAALGG-GSSG-----------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTnNPYDYAFVSQGE-VSVASIDDSEELMATDSAF 337
Cdd:cd01383 147 ICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLK-SASEYKYLNQSNcLTIDGVDDAKKFHELKEAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 338 DVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 417
Cdd:cd01383 226 DTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 418 VQQVYYSIGALAKAVYEKMFNWMVTRINATLET-KQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd01383 306 LQQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 497 LEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLyDNHLgKSNnfqkpRNVKGKQE 575
Cdd:cd01383 386 LEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHL-KSN-----SCFKGERG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 576 AHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLmATLFSSYASADTADSSKGKGGKKKGSSFQTVSALHRE 655
Cdd:cd01383 458 GAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQL-PQLFASKMLDASRKALPLTKASGSDSQKQSVATKFKG 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 656 NLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEG 735
Cdd:cd01383 537 QLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSAS 616
|
650 660 670
....*....|....*....|....*....|...
gi 431907173 736 QFIDSRKGAekLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01383 617 QDPLSTSVA--ILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-768 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 630.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 180 SGAGKTVNTKRVIQYFASiaaigdrgkkdnANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCA------------VTNNHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSN-KKPDLLDMLLVTNNPYDYAFVSQ-GEVSVASIDDSEELMATDSAF 337
Cdd:cd14883 150 KGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGaKHSKELKEKLKLGEPEDYHYLNQsGCIRIDNINDKKDFDHLRLAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 338 DVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 416
Cdd:cd14883 230 NVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 417 SVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14883 310 KVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 497 LEQEEYKKEGIEWTFIDFgMDLQACIDLIEK-PMGIMSILEEECMFPKATDMTFKAKLYDNHlGKSNNFQKPRNVKGKQE 575
Cdd:cd14883 390 LEQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPDRRRWKTE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 576 ahFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFS----SYASADTADSSKGKGGKKKGSSFQTVSA 651
Cdd:cd14883 468 --FGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTypdlLALTGLSISLGGDTTSRGTSKGKPTVGD 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 652 LHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAA 731
Cdd:cd14883 546 TFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRA 625
|
650 660 670
....*....|....*....|....*....|....*...
gi 431907173 732 IPEGQfiDSRKGAEK-LLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14883 626 RSADH--KETCGAVRaLMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-768 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 593.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 178 GESGAGKTVNTKRVIQYFAsiaaigDRGKKDNANANkgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd01384 81 GESGAGKTETTKMLMQYLA------YMGGRAVTEGR--SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVtNNPYDYAFVSQGE-VSVASIDDSEELMATDSA 336
Cdd:cd01384 153 RISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKL-KDPKQFHYLNQSKcFELDGVDDAEEYRATRRA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 337 FDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEP--DGTEDADK-SAYLMGLNSADLLKGLCHPRVKVGNEYVT 413
Cdd:cd01384 232 MDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPkdEKSEFHLKaAAELLMCDEKALEDALCKRVIVTPDGIIT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 414 KGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 493
Cdd:cd01384 312 KPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 494 MFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLYDNhLGKSNNFQKPrnvKG 572
Cdd:cd01384 392 VFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKP---KL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 573 KQEAhFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADTadsskgkggkKKGSSFQTVSAL 652
Cdd:cd01384 467 SRTD-FTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGT----------SSSSKFSSIGSR 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 653 HRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAI 732
Cdd:cd01384 536 FKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVL 615
|
650 660 670
....*....|....*....|....*....|....*.
gi 431907173 733 peGQFIDSRKGAEKLLSSLDIdhNQYKFGHTKVFFK 768
Cdd:cd01384 616 --KGSDDEKAACKKILEKAGL--KGYQIGKTKVFLR 647
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
848-1919 |
8.85e-175 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 567.88 E-value: 8.85e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 848 EKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNER 927
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 928 LEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQ 1007
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1008 ALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEF 1087
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1088 DISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNK 1167
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1168 KREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANL 1247
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1248 EKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLTRGKLSYTQQTEDLKRQLEEEGKA 1327
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1328 KNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAiQRTEELEEAK------LQDAEEAVE 1401
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKkrlqreLEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1402 AVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLK 1481
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1482 NAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEF 1561
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1562 NQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRTASEAQKHLKI 1641
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1642 AQAHLKDTQLQMDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLIN 1721
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1722 QKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAL 1801
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1802 KGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEA 1881
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 431907173 1882 EEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAK 1919
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-768 |
1.92e-173 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 548.61 E-value: 1.92e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 178 GESGAGKTVNTKRVIQYFASIAAigdrgkkdnaNANKGTLEdQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG----------GLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDmLLVTNNPYDYafvsQGEVSVASID---DSEELMATD 334
Cdd:cd14903 150 TLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERL-FLDSANECAY----TGANKTIKIEgmsDRKHFARTK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 335 SAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE--PDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 412
Cdd:cd14903 225 EALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 413 TKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNH 492
Cdd:cd14903 305 TVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 493 HMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNVKg 572
Cdd:cd14903 385 DVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 573 kqeAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLF----SSYASADTADSSKGKGGKKKGSSFQT 648
Cdd:cd14903 463 ---TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFkekvESPAAASTSLARGARRRRGGALTTTT 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 649 VSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 728
Cdd:cd14903 540 VGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFL 619
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 431907173 729 PAAipEGQFIDSRKGAEKLLSSLDIDH-NQYKFGHTKVFFK 768
Cdd:cd14903 620 PEG--RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-768 |
1.69e-172 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 545.53 E-value: 1.69e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 179 ESGAGKTVNTKRVIQYFASIAAigdrgkkdnanaNKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAG------------STNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSnkKPDLLDMLLVTNNPyDYAFVSQGE-VSVASIDDSEELMATDSAF 337
Cdd:cd14872 149 ICGASTENYLLEKSRVVYQIKGERNFHIFYQLLA--SPDPASRGGWGSSA-AYGYLSLSGcIEVEGVDDVADFEEVVLAM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 338 DVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKS---AYLMGLNSADLLKGLCHPRVKVgneyvtK 414
Cdd:cd14872 226 EQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLkevATLLGVDAATLEEALTSRLMEI------K 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 415 GQ-------SVQQVYYSIGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKL 486
Cdd:cd14872 300 GCdptriplTPAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 487 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEK-PMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSnnFQ 565
Cdd:cd14872 380 QQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS--TF 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 566 KPRNVKGKqEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFS-SYASADTADSskgkggkkkgs 644
Cdd:cd14872 457 VYAEVRTS-RTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPpSEGDQKTSKV----------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 645 sfqTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRY 724
Cdd:cd14872 525 ---TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRY 601
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 431907173 725 RILnPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14872 602 RFL-VKTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
94-768 |
2.15e-171 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 542.61 E-value: 2.15e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 94 TFLHepavlyNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQ 172
Cdd:cd01382 2 TLLN------NIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 173 SILITGESGAGKTVNTKRVIQYFAsiaaigdrgkkDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIH 252
Cdd:cd01382 76 SIIVSGESGAGKTESTKYILRYLT-----------ESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 253 FGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLvtnnpydyafvsqgevSVASIDDSEELMA 332
Cdd:cd01382 145 FNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 333 TDSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFkqkqrEEQAEPDG-----TEDADKS----AYLMGLNSADLLKGLCHp 403
Cdd:cd01382 209 MDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEF-----EENGSDSGggcnvKPKSEQSleyaAELLGLDQDELRVSLTT- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 404 RVKVGNEYVTKGQS------VQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQpRQYFIGVLDIAGFEIFDFNSFEQL 477
Cdd:cd01382 283 RVMQTTRGGAKGTVikvplkVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET-SSYFIGVLDIAGFEYFEVNSFEQF 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 478 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLYDN 556
Cdd:cd01382 362 CINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQK 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 557 HLgksNNF--QKPRnvKGKQEAH--------FSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYA 626
Cdd:cd01382 441 HK---NHFrlSIPR--KSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESST 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 627 SADTadsskGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRI 706
Cdd:cd01382 516 NNNK-----DSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDL 590
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 431907173 707 CRKGFPNRILYGDFRQRYRILNPAAIPEgqfIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01382 591 MQGGFPSRTSFHDLYNMYKKYLPPKLAR---LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
99-768 |
3.56e-171 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 541.48 E-value: 3.56e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd01379 1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 179 ESGAGKTVNTKRVIQYFASIaaigdrGKkdnanANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd01379 81 ESGAGKTESANLLVQQLTVL------GK-----ANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQI---LSNKKpDLLDMLLVTNNPYDYAFVSQGEVSVASIDDS--EELMAT 333
Cdd:cd01379 150 VTGARISEYLLEKSRVVHQAIGERNFHIFYYIyagLAEDK-KLAKYKLPENKPPRYLQNDGLTVQDIVNNSGnrEKFEEI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 334 DSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQ----AEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGN 409
Cdd:cd01379 229 EQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 410 EYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATL---ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKL 486
Cdd:cd01379 309 ETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpdRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 487 QQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACID-LIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHlgKSNNFQ 565
Cdd:cd01379 389 QYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--KSKYYW 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 566 KPRNVkgkqEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMAtlfssyasadtadsskgkggkkkgss 645
Cdd:cd01379 466 RPKSN----ALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR-------------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 646 fQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 725
Cdd:cd01379 516 -QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYY 594
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 431907173 726 IL--NPAAIPEGqfidSRKGAEKLLSSLDIDHnqYKFGHTKVFFK 768
Cdd:cd01379 595 FLafKWNEEVVA----NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
100-768 |
1.13e-170 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 541.29 E-value: 1.13e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYML----TDRENQSI 174
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIqsgvLDPSNQSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 175 LITGESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANANK-------GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGK 247
Cdd:cd14890 82 IISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASeaieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 248 FIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNnPYDYAFVSQGEVSVASIDDS 327
Cdd:cd14890 162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQT-PVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 328 EELMATDSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGT-EDADKSAYLMGLNSADLLKGLCHPRVK 406
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQLF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 407 VGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKL 486
Cdd:cd14890 321 VGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 487 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILE--EEC--MFPKATDMTFKAKLYDNHLGKS 561
Cdd:cd14890 401 QRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgKVNGKPGIFItlDDCwrFKGEEANKKFVSQLHASFGRKS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 562 NNFQKPRNVKGKQ---------EAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATlfssyasadtad 632
Cdd:cd14890 480 GSGGTRRGSSQHPhfvhpkfdaDKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSIREV------------ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 633 sskgkggkkkgssfqTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFP 712
Cdd:cd14890 548 ---------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFA 612
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 713 NRILYGDFRQRYRILNPAAipegqfiDSRKGAEKLLSS-LDIDHNQYKFGHTKVFFK 768
Cdd:cd14890 613 LREEHDSFFYDFQVLLPTA-------ENIEQLVAVLSKmLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-768 |
6.17e-169 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 536.58 E-value: 6.17e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRgKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 178 GESGAGKTVNTKRVIQYFASiAAIGDRGKKDnanankgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHF---- 253
Cdd:cd14888 80 GESGAGKTESTKYVMKFLAC-AGSEDIKKRS-------LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFsklk 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 254 -----GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILS-----------------------NKKPDLLDMLL-V 304
Cdd:cd14888 152 skrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMSSfE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 305 TNNPYDYAFVSqGEVSVASIDDSEELMATDSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQA---EPDGTED 381
Cdd:cd14888 232 PHLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASCTDD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 382 ADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGV 460
Cdd:cd14888 311 LEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCGV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 461 LDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLI-EKPMGIMSILEEEC 539
Cdd:cd14888 391 LDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEEC 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 540 MFPKATDMTFKAKLYDNHLGkSNNFQKprnVKGKQEAhFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMA 619
Cdd:cd14888 470 FVPGGKDQGLCNKLCQKHKG-HKRFDV---VKTDPNS-FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFIS 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 620 TLFSSYASADTadsskgkGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNG 699
Cdd:cd14888 545 NLFSAYLRRGT-------DGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGG 617
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 431907173 700 VLEGIRICRKGFPNRILYGDFRQRYRILNPaaiPEGQfidsrkgaekllssldIDHNQYKFGHTKVFFK 768
Cdd:cd14888 618 VLQAVQVSRAGYPVRLSHAEFYNDYRILLN---GEGK----------------KQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
100-768 |
2.38e-165 |
|
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 525.86 E-value: 2.38e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 180 SGAGKTVNTKRVIQYFASIAaigdrgKKDNAnankgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgATGKL 259
Cdd:cd01387 82 SGSGKTEATKLIMQYLAAVN------QRRNN-----LVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDML-LVTNNPYDYafVSQG-EVSVASIDDSEELMATDSAF 337
Cdd:cd01387 150 VGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYgLQEAEKYFY--LNQGgNCEIAGKSDADDFRRLLAAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 338 DVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQRE---EQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTK 414
Cdd:cd01387 228 QVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 415 GQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 494
Cdd:cd01387 308 PLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 495 FVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLYDNHlGKSNNFQKPRnvKGK 573
Cdd:cd01387 388 FKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPR--MPL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 574 QEahFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYAS--ADTADSSKGKGGKKKGSSFQTVSA 651
Cdd:cd01387 464 PE--FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAqtDKAPPRLGKGRFVTMKPRTPTVAA 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 652 LHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAA 731
Cdd:cd01387 542 RFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALK 621
|
650 660 670
....*....|....*....|....*....|....*....
gi 431907173 732 IPEGQFIDSRkgaEKLLSSLD--IDHNQYKFGHTKVFFK 768
Cdd:cd01387 622 LPRPAPGDMC---VSLLSRLCtvTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-766 |
5.38e-165 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 525.12 E-value: 5.38e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAY------RGKKRSEAPPHIFSISDNAYQYMLTDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 171 --NQSILITGESGAGKTVNTKRVIQYFASIAAigdRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKF 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSS---ATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 249 IRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNP-YDYAFVSQGEVSVASIDDS 327
Cdd:cd14901 158 IRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEeYKYLNSSQCYDRRDGVDDS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 328 EELMATDSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTE-DADKSAYLMGLNSADLLKGLCHPRVK 406
Cdd:cd14901 238 VQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLaNVRAACDLLGLDMDVLEKTLCTREIR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 407 VGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQP--RQYFIGVLDIAGFEIFDFNSFEQLCINFTNE 484
Cdd:cd14901 318 AGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFANE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 485 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLYDNhLGKSNN 563
Cdd:cd14901 398 KLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHAS 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 564 FQKPRNVKGKQEahFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATlfssyasadtadsskgkggkkkg 643
Cdd:cd14901 476 FSVSKLQQGKRQ--FVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS----------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 644 ssfqTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQR 723
Cdd:cd14901 531 ----TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHT 606
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 431907173 724 YRILNPAAIPEGQFIdsRKGAEKLLSSLDI------DHNQYKFGHTKVF 766
Cdd:cd14901 607 YSCLAPDGASDTWKV--NELAERLMSQLQHselnieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
105-768 |
3.53e-161 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 514.31 E-value: 3.53e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 105 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRG--KKRSEAPPHIFSISDNAYQYMLTDR----ENQSILIT 177
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYDVPGFDSQRKeeATASSPPPHVFSIAERAYRAMKGVGkgqgTPQSIVVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 178 GESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANANKGT-LEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 256
Cdd:cd14892 87 GESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHEsIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNSD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 257 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILS----NKKPDL-LDMLLvtnnpyDYAFVSQGE-VSVASIDDSEEL 330
Cdd:cd14892 167 GRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAgldaNENAALeLTPAE------SFLFLNQGNcVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 331 MATDSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQ--KQREEQAEPDGTEDADKSAYLMGLNSADLLKGLC-----HP 403
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaDDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVtqttsTA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 404 RVKVGNEYVTKGQSVQqvyySIGALAKAVYEKMFNWMVTRINAtlETKQ------------PRQYFIGVLDIAGFEIFDF 471
Cdd:cd14892 321 RGSVLEIKLTAREAKN----ALDALCKYLYGELFDWLISRINA--CHKQqtsgvtggaaspTFSPFIGILDIFGFEIMPT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 472 NSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEK-PMGIMSILEEECMFP-KATDMTF 549
Cdd:cd14892 395 NSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 550 KAKLYDNHLGKSNNFQKPRNvkgkQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSlklmatlfssyasad 629
Cdd:cd14892 474 LTIYHQTHLDKHPHYAKPRF----ECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS--------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 630 tadsskgkggkkkgsSFqtvsalhRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRK 709
Cdd:cd14892 535 ---------------KF-------RTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRRE 592
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 710 GFPNRILYGDFRQRYRIL-----NPAAIPEGQ--FIDSRKGAEKLLSSLdiDHNQYKFGHTKVFFK 768
Cdd:cd14892 593 GFPIRRQFEEFYEKFWPLarnkaGVAASPDACdaTTARKKCEEIVARAL--ERENFQLGRTKVFLR 656
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
102-768 |
5.22e-161 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 515.00 E-value: 5.22e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 102 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESG 181
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 182 AGKTVNTKRVIQYFASIAAIGdrgkkdnanANKGTlEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 261
Cdd:cd01385 84 SGKTESTNFLLHHLTALSQKG---------YGSGV-EQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 262 ADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTnNPYDYAFVSQGE-VSVASIDDSEELMATDSAFDVL 340
Cdd:cd01385 154 AVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLK-QPEDYHYLNQSDcYTLEGEDEKYEFERLKQAMEMV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 341 GFTPEEKAGVYKLTGAIMHYGNMKFKQK--QREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 418
Cdd:cd01385 233 GFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 419 QQVYYSIGALAKAVYEKMFNWMVTRINATLETKQ----PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 494
Cdd:cd01385 313 PEAIATRDAMAKCLYSALFDWIVLRINHALLNKKdleeAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 495 FVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKlYDNHLGKSNNFQKPRnvkgK 573
Cdd:cd01385 393 FKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQ----V 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 574 QEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLM------------------ATLFSSYASADTADSSK 635
Cdd:cd01385 467 MEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVreligidpvavfrwavlrAFFRAMAAFREAGRRRA 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 636 GKGGKKKGSSFQ----------------TVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNG 699
Cdd:cd01385 547 QRTAGHSLTLHDrttksllhlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTG 626
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 431907173 700 VLEGIRICRKGFPNRILYGDFRQRYRILnpaaIPEGQfIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd01385 627 MLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGL-ISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
100-768 |
4.08e-157 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 502.40 E-value: 4.08e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 179 ESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANANkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVISQQSLELSLKEKTSC---VEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTnNPYDYAFVSQ-GEVSVASIDDSEELMATDSAF 337
Cdd:cd14873 159 IQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENYHYLNQsGCVEDKTISDQESFREVITAM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 338 DVLGFTPEEKAGVYKLTGAIMHYGNMKFkqkqreeqAEPDGTEDADK-----SAYLMGLNSADLLKGLCHPRVKVGNEYV 412
Cdd:cd14873 238 EVMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKtalgrSAELLGLDPTQLTDALTQRSMFLRGEEI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 413 TKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQyFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNH 492
Cdd:cd14873 310 LTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK-SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 493 HMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHlgkSNN--FQKPRnv 570
Cdd:cd14873 389 HIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH---ANNhfYVKPR-- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 571 kgKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADTADSSKGKGGKKKgssfQTVS 650
Cdd:cd14873 463 --VAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRR----PTVS 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 651 ALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNP- 729
Cdd:cd14873 537 SQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRn 616
|
650 660 670
....*....|....*....|....*....|....*....
gi 431907173 730 AAIPEgqfiDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14873 617 LALPE----DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
101-768 |
3.93e-153 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 490.36 E-value: 3.93e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 101 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKK-RSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 180 SGAGKTVNTKRVIQYFASIAAigdrgkKDNANankgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd14897 83 SGAGKTESTKYMIKHLMKLSP------SDDSD-----LLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVtNNPYDYAFVSQGEVSVASIDDSEELMATDSAFDV 339
Cdd:cd14897 152 LGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELEYYRQMFHD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 340 L-------GFTPEEKAGVYKLTGAIMHYGNMKFkqkqrEEQAEPDGTEDADK-----SAYLMGLNSADLLKGLCHPRVKV 407
Cdd:cd14897 231 LtnimkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVNTI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 408 GNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYF-----IGVLDIAGFEIFDFNSFEQLCINFT 482
Cdd:cd14897 306 RGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCINLS 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 483 NEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLyDNHLGKS 561
Cdd:cd14897 386 NERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NKYCGES 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 562 NNFQKPrnvKGKQEAhFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYasadtadsskgkggkk 641
Cdd:cd14897 464 PRYVAS---PGNRVA-FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSY---------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 642 kgssfqtvsalHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFR 721
Cdd:cd14897 524 -----------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFV 592
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 431907173 722 QRYRILNPAAIPegqfidSRKGAE-KLLSSLDIDHNQ-YKFGHTKVFFK 768
Cdd:cd14897 593 KRYKEICDFSNK------VRSDDLgKCQKILKTAGIKgYQFGKTKVFLK 635
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-768 |
2.29e-148 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 477.51 E-value: 2.29e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 178 GESGAGKTVNTKRVIQYFASIAAigdrGKKDNAnankgtlEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG----GRKDKT-------IAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 258 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSN-KKPDLLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSA 336
Cdd:cd14904 150 KLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 337 FDVLGFTPEEKAGVYKLTGAIMHYGNMKFkQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 416
Cdd:cd14904 230 LSLIGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 417 SVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQY-FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14904 309 APVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 496 VLEQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNH--LGKSNNFQKPRnVKGK 573
Cdd:cd14904 389 KTVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPK-VKRT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 574 QeahFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSsyaSADTADSSKGKGGKKKGSSFQTVSALH 653
Cdd:cd14904 467 Q---FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFG---SSEAPSETKEGKSGKGTKAPKSLGSQF 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 654 RENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 733
Cdd:cd14904 541 KTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMH 620
|
650 660 670
....*....|....*....|....*....|....*.
gi 431907173 734 EGqfiDSRKGAEKLLSSLDIDHN-QYKFGHTKVFFK 768
Cdd:cd14904 621 SK---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
101-768 |
3.17e-148 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 477.99 E-value: 3.17e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 101 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAY------RGKK--RSEAPPHIFSISDNAYQYMLTDREN 171
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYkeqiiqNGEYfdIKKEPPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 172 QSILITGESGAGKTVNTKRVIQYFASIAA--------IGDRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSS 243
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevLTLTSSIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 244 RFGKFIRIHFG-ATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNP--YDYAFVSQGE-V 319
Cdd:cd14907 163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLsgDRYDYLKKSNcY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 320 SVASIDDSEELMATDSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQ--REEQAEPDGTEDADKSAYLMGLNSADLL 397
Cdd:cd14907 243 EVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEELK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 398 KGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATL--------ETKQPRQYFIGVLDIAGFEIF 469
Cdd:cd14907 323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 470 DFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF--IDFgMDLQACIDLIEK-PMGIMSILEEECMFPKATD 546
Cdd:cd14907 403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 547 MTFKAKLYDNHlgksNNFQKPRNVKGKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSsya 626
Cdd:cd14907 482 EKLLNKIKKQH----KNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFS--- 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 627 SADTADSSKGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRI 706
Cdd:cd14907 555 GEDGSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRV 634
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 431907173 707 CRKGFPNRILYGDFRQRYRILNpaaipegqfidsrkgaekllssldidhNQYKFGHTKVFFK 768
Cdd:cd14907 635 RKQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
101-733 |
3.56e-145 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 467.48 E-value: 3.56e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 101 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAY-----------RGKKRSEAPPHIFSISDNAYQYM--- 165
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 166 -LTDRENQSILITGESGAGKTVNTKRVIQYFASIAAIGDRGKKdNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSR 244
Cdd:cd14900 83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASV-SMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 245 FGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILsnkkpdlldmllvtnnpydyafVSQGEVSVASi 324
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMA----------------------IGASEAARKR- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 325 DDSEELMAtdsAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDA-------DKSAYLMGLNSADLL 397
Cdd:cd14900 219 DMYRRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATKLE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 398 KGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATL-----ETKQPRQYFIGVLDIAGFEIFDFN 472
Cdd:cd14900 296 KALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEVFPKN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 473 SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKA 551
Cdd:cd14900 376 SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLAS 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 552 KLYdNHLGKSNNFQKPRNVKGKqeAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSslklmatlfssyasadta 631
Cdd:cd14900 455 KLY-RACGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVYG------------------ 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 632 dsskgkggkkkgSSFqtvsalhRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGF 711
Cdd:cd14900 514 ------------LQF-------KEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGF 574
|
650 660
....*....|....*....|..
gi 431907173 712 PNRILYGDFRQRYRILNPAAIP 733
Cdd:cd14900 575 PIRLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-768 |
1.82e-140 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 455.14 E-value: 1.82e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 101 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYML----TDRENQSILI 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 177 TGESGAGKTVNTKRVIQYFASIAaigdRGKKDnanankgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgAT 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC----RGNSQ--------LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 257 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILS------NKKPDLLDmllvtnnPYDYAFVSQG-----EVSVASID 325
Cdd:cd14889 150 GHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAgisaedRENYGLLD-------PGKYRYLNNGagckrEVQYWKKK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 326 DSEELmatdSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREE-QAEPDGTEDADKSAYLMGLNSADLLKGLchpr 404
Cdd:cd14889 223 YDEVC----NAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTL---- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 405 vkVGNEYVTKGQSVQQVYYSIGA------LAKAVYEKMFNWMVTRINATLetkQPRQYF------IGVLDIAGFEIFDFN 472
Cdd:cd14889 295 --TCTVTFTRGEQIQRHHTKQQAedardsIAKVAYGRVFGWIVSKINQLL---APKDDSsvelreIGILDIFGFENFAVN 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 473 SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDL-IEKPMGIMSILEEECMFPKATDMTFKA 551
Cdd:cd14889 370 RFEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVD 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 552 KLyDNHLGKSNNFQKPRNVKGKqeahFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADTA 631
Cdd:cd14889 449 KL-NIHFKGNSYYGKSRSKSPK----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGT 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 632 DSSKGKGGKKKGSSF-----QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRI 706
Cdd:cd14889 524 LMPRAKLPQAGSDNFnstrkQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRI 603
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 431907173 707 CRKGFPNRILYGDFRQRYRIL-NPAAIPegqfiDSRKGAEKLLSSLDIdhNQYKFGHTKVFFK 768
Cdd:cd14889 604 RREGFSWRPSFAEFAERYKILlCEPALP-----GTKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-734 |
1.03e-137 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 448.20 E-value: 1.03e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYR--GKKRS---EAP----PHIFSISDNAYQYMLTD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 169 RENQSILITGESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKF 248
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 249 IRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQIL------SNKKPDLLDMLLVTNN-PYDYAFVSQGEV-S 320
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrggdeeEHEKYEFHDGITGGLQlPNEFHYTGQGGApD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 321 VASIDDSEELMATDSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAY---LMGLNSADLL 397
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARvakLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 398 KGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATL--ETKQPRQYFIGVLDIAGFEIFDFNSFE 475
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 476 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLIE-KPMGIMSILEEECMFP-KATDMTFKAKL 553
Cdd:cd14908 401 QLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 554 YDNHLGKSNN-------FQKPRNVKGKqeAHFSLIHYAGTVDYNI-LGWLEKNKDPLNETVVGLYQKSslklmaTLFssy 625
Cdd:cd14908 480 YETYLPEKNQthsentrFEATSIQKTK--LIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFESG------QQF--- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 626 asadtadsskgkggkkkgssfqtvsalhRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIR 705
Cdd:cd14908 549 ----------------------------KAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVR 600
|
650 660
....*....|....*....|....*....
gi 431907173 706 ICRKGFPNRILYGDFRQRYRILNPaAIPE 734
Cdd:cd14908 601 VARSGYPVRLPHKDFFKRYRMLLP-LIPE 628
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-768 |
2.24e-136 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 442.95 E-value: 2.24e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAA--WMIYTYSGLFCVTVNPYKWLPvyNAEVvAAYRGKKRSEAPPHIFSISDNAYQYMLTDRE---NQS 173
Cdd:cd14891 1 AGILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLP--EPDK-SDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 174 ILITGESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANANKG-------TLEDQIIQANPALEAFGNAKTVRNDNSSRFG 246
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKkrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 247 KFIRIHFGATG-KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTnNPYDYAFVSQ-GEVSVASI 324
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLL-SPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 325 DDSEELMATDSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREE----QAEPDGTEDADKSAYLMGLNSADLLKGL 400
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 401 CHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFD-FNSFEQLCI 479
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 480 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLYDNHl 558
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 559 GKSNNFQKPRNvKGKQEAhFSLIHYAGTVDYNILGWLEKNKDPLNEtvvglyQKSSLKLMATLFSsyasadtadsskgkg 638
Cdd:cd14891 475 KRHPCFPRPHP-KDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPE------DFEDLLASSAKFS--------------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 639 gkkkgssfqtvsalhrENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 718
Cdd:cd14891 532 ----------------DQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYA 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 719 DFRQRYRILNPAAI------PEGQFIdsrkgaEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14891 596 ELVDVYKPVLPPSVtrlfaeNDRTLT------QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-729 |
6.17e-135 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 441.25 E-value: 6.17e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYR--------GKKRSEAPPHIFSISDNAYQYML-TD 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 169 RENQSILITGESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANANKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKF 248
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAVE--IGKRILQTNPILESFGNAQTIRNDNSSRFGKF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 249 IRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDmLLVTNNPYDYAFVSQGEVSVA-----S 323
Cdd:cd14902 159 IKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLD-LLGLQKGGKYELLNSYGPSFArkravA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 324 IDDSEELMATDSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDA---DKSAYLMGLNSADLLKGL 400
Cdd:cd14902 238 DKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDKLETLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 401 CHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRIN-------ATLETKQPRQYF--IGVLDIAGFEIFDF 471
Cdd:cd14902 318 SSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSdeinyfdSAVSISDEDEELatIGILDIFGFESLNR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 472 NSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLqACIDLIE-KPMGIMSILEEECMFPKATDMTFK 550
Cdd:cd14902 398 NGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNA-ACLALFDdKSNGLFSLLDQECLMPKGSNQALS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 551 AKLYDNHLGksnnfqkprnvkgkqEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLK-LMATLFSSYASAD 629
Cdd:cd14902 477 TKFYRYHGG---------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEvVVAIGADENRDSP 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 630 TADSSKGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRK 709
Cdd:cd14902 542 GADNGAAGRRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARH 621
|
650 660
....*....|....*....|
gi 431907173 710 GFPNRILYGDFRQRYRILNP 729
Cdd:cd14902 622 GYSVRLAHASFIELFSGFKC 641
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
62-821 |
4.78e-128 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 425.21 E-value: 4.78e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 62 ETENGKTVTLKEDQVLQQNPP-KFDKIEDMAMLTFLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVA 140
Cdd:PTZ00014 72 DPPTNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIR 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 141 AYR-GKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFASiaaigdrGKKDNanaNKGTLED 219
Cdd:PTZ00014 152 RYRdAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAS-------SKSGN---MDLKIQN 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 220 QIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDL- 298
Cdd:PTZ00014 222 AIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMk 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 299 --LDMLLVTnnpyDYAFVSQGEVSVASIDDSEELMATDSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKqrEEQAEP 376
Cdd:PTZ00014 302 ekYKLKSLE----EYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGK--EEGGLT 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 377 DGTEDADKS-------AYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLE 449
Cdd:PTZ00014 376 DAAAISDESlevfneaCELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIE 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 450 TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGI-----EWTfidfgmDLQACIDL 524
Cdd:PTZ00014 456 PPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGIsteelEYT------SNESVIDL 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 525 I-EKPMGIMSILEEECMFPKATDMTFKAKLYDNHlgKSNNFQKPrnVKGKQEAHFSLIHYAGTVDYNILGWLEKNKDPLN 603
Cdd:PTZ00014 530 LcGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNL--KNNPKYKP--AKVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLR 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 604 ETVVGLYQKSSLKLMATLFssyasadtadsSKGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAP 683
Cdd:PTZ00014 606 PELVEVVKASPNPLVRDLF-----------EGVEVEKGKLAKGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKP 674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 684 GVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNpAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHT 763
Cdd:PTZ00014 675 LDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLD-LAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKT 753
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 431907173 764 KVFFKAGLLGLLEEMRDERLSR---IITRIQAQARGQLMRIEFKKMVErrdALLVIQWNIR 821
Cdd:PTZ00014 754 MVFLKKDAAKELTQIQREKLAAwepLVSVLEALILKIKKKRKVRKNIK---SLVRIQAHLR 811
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-768 |
6.46e-125 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 409.94 E-value: 6.46e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 179 ESGAGKTVNTKRVIQYFASIaaigdrgKKDNANANKGTLEDQIiqanPALEAFGNAKTVRNDNSSRFGKFIRIHFgATGK 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL-------YQDQTEDRLRQPEDVL----PILESFGHAKTILNANASRFGQVLRLHL-QHGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVtNNPYDYAFVSQGEV-SVASIDDSEELMATDSAF 337
Cdd:cd14896 149 IVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYLNQGGAcRLQGKEDAQDFEGLLKAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 338 DVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDAD--KSAYLMGLnSADLLKGLCHPRVKVGN-EYVTK 414
Cdd:cd14896 228 QGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEihTAARLLQV-PPERLEGAVTHRVTETPyGRVSR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 415 GQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYF--IGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNH 492
Cdd:cd14896 307 PLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 493 HMFVLEQEEYKKEGIEWTFIDfGMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLYDNHlGKSNNFQKPRNvk 571
Cdd:cd14896 387 TLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQL-- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 572 gkQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASAdtadsskgkggKKKGSSFQTVSA 651
Cdd:cd14896 463 --PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQ-----------YGLGQGKPTLAS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 652 LHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILnpAA 731
Cdd:cd14896 530 RFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGAL--GS 607
|
650 660 670
....*....|....*....|....*....|....*..
gi 431907173 732 IPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14896 608 ERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
99-768 |
2.45e-124 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 410.11 E-value: 2.45e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNaevVAAYRGK--KRSEAPPHIFSISDNAYQYMLT-------D 168
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 169 RENQSILITGESGAGKTVNTKRVIQYFASIAAigDRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKF 248
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNYLAESSK--HTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 249 IRIHFG-----ATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDML-LVTNNPYDYAFVSQGEVSVA 322
Cdd:cd14895 156 VRMFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELqLELLSAQEFQYISGGQCYQR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 323 S--IDDSEELMATDSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDA------------------ 382
Cdd:cd14895 236 NdgVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqqhl 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 383 DKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQY------ 456
Cdd:cd14895 316 DIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNpnkaan 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 457 -----FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLIE-KPMG 530
Cdd:cd14895 396 kdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLEqRPSG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 531 IMSILEEECMFPKATDMTFKAKLYdNHLGKSNNFQKPRnvKGKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLY 610
Cdd:cd14895 475 IFSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 611 QKSSLKLMATLFSSYASADTADSSKGKGGKKKGSSFQT---VSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMD 687
Cdd:cd14895 552 GKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSsvgIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFD 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 688 NPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPegqfidSRKGAEKLLSSLDIDHNQykFGHTKVFF 767
Cdd:cd14895 632 MAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNA------SDATASALIETLKVDHAE--LGKTRVFL 703
|
.
gi 431907173 768 K 768
Cdd:cd14895 704 R 704
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-768 |
1.30e-122 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 403.21 E-value: 1.30e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRG-KKRSEAPPHIFSIS----DNAYQYmltdRENQS 173
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTArralENLHGV----NKSQT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 174 ILITGESGAGKTVNTKRVIQYFASiaaigdrGKKDNANankGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHF 253
Cdd:cd14876 77 IIVSGESGAGKTEATKQIMRYFAS-------AKSGNMD---LRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 254 GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLD--MLLVTNnpyDYAFVSQGEVSVASIDDSEELM 331
Cdd:cd14876 147 ASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSkyHLLGLK---EYKFLNPKCLDVPGIDDVADFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 332 ATDSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQReeqaepDGTEDA-----------DKSAYLMGLNSADLLKGL 400
Cdd:cd14876 224 EVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTE------QGVDDAaaisneslevfKEACSLLFLDPEALKREL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 401 CHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCIN 480
Cdd:cd14876 298 TVKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFIN 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 481 FTNEKLQQFFNHHMFVLEQEEYKKEGI-----EWTfidfgmDLQACID-LIEKPMGIMSILEEECMFPKATDMTFKAKLY 554
Cdd:cd14876 378 ITNEMLQKNFIDIVFERESKLYKDEGIptaelEYT------SNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACV 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 555 DNHlgKSNNFQKPrnVKGKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSyasadtadss 634
Cdd:cd14876 452 SKL--KSNGKFKP--AKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEG---------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 635 kGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNR 714
Cdd:cd14876 518 -VVVEKGKIAKGSLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYR 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 431907173 715 ILYGDFRQRYRILNPaAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14876 597 RPFEEFLYQFKFLDL-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
101-728 |
1.78e-113 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 378.94 E-value: 1.78e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 101 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKR-SEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 179 ESGAGKTVNTKRVIQYFASIAAiGDRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT-G 257
Cdd:cd14906 83 ESGSGKTEASKTILQYLINTSS-SNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 258 KLASADIETYLLEKSRVIFQL-KAERNYHIFYQILSNKKPDLLDMLLVTNNPYDYAFVSQGEVSVASI------------ 324
Cdd:cd14906 162 KIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFksqssnknsnhn 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 325 ---DDSEELMATDSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQ---REEQAEPDGTEDADKSAYLMGLNSADLLK 398
Cdd:cd14906 242 nktESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFKQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 399 GLCHPRVKVGNE--YVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINAT-LETKQPRQ----------YFIGVLDIAG 465
Cdd:cd14906 322 ALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKfNQNTQSNDlaggsnkknnLFIGVLDIFG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 466 FEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKA 544
Cdd:cd14906 402 FENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPKG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 545 TDMTFKAKlYDNHLGKSNNFQKPRNVKGKqeahFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSS 624
Cdd:cd14906 481 SEQSLLEK-YNKQYHNTNQYYQRTLAKGT----LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQ 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 625 YASADTADSSKGKGGKkkgssfqTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGI 704
Cdd:cd14906 556 QITSTTNTTKKQTQSN-------TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTI 628
|
650 660
....*....|....*....|....
gi 431907173 705 RICRKGFPNRILYGDFRQRYRILN 728
Cdd:cd14906 629 KVRKMGYSYRRDFNQFFSRYKCIV 652
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
101-766 |
7.68e-110 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 366.48 E-value: 7.68e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 101 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEA-PPHIFSISDNAYQYMLTDRE--NQSILI 176
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQKlKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 177 TGESGAGKTVNTKRVIQYFASIAAiGDRGKKDNANANKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 256
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAA-SPTSWESHKIAER--IEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 257 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILsnkKPDLLDMLLVTNNP--YDYAFVSQGEVSVasidDSEELMATD 334
Cdd:cd14880 160 QQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQIC---KGASADERLQWHLPegAAFSWLPNPERNL----EEDCFEVTR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 335 SAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQA---EPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEY 411
Cdd:cd14880 233 EAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 412 VT--KGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPR-QYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQ 488
Cdd:cd14880 313 QVfkKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 489 FFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDmtfkAKLYDNHLGK--SNNFQ 565
Cdd:cd14880 393 HFVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSS----AAQLQTRIESalAGNPC 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 566 KPRNvKGKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFssyaSADTADSSKGKGGKKKGSS 645
Cdd:cd14880 468 LGHN-KLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLF----PANPEEKTQEEPSGQSRAP 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 646 FQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 725
Cdd:cd14880 543 VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYK 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 431907173 726 IL---NPAAIPEGQFIDSRKGAEKLLSSldidhnqykfGHTKVF 766
Cdd:cd14880 623 LLrrlRPHTSSGPHSPYPAKGLSEPVHC----------GRTKVF 656
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
101-768 |
3.09e-108 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 362.21 E-value: 3.09e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 101 VLYNLKERYAAWMI-YTYSGLFCVTVNPYKWLPvYNAEVvaaYRGKKRSEA-----PPHIFSISDNAY-QYMLTDRENQS 173
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMP-FNSEE---ERKKYLALPdprllPPHIWQVAHKAFnAIFVQGLGNQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 174 ILITGESGAGKTVNTKRVIQYfasiaaIGDRGKKDNANANKGTLEDQIIQ----ANPALEAFGNAKTVRNDNSSRFGKFI 249
Cdd:cd14875 79 VVISGESGSGKTENAKMLIAY------LGQLSYMHSSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 250 RIHF-GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNPYDY-------AFVSQGeVSV 321
Cdd:cd14875 153 KLYFdPTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYkclnggnTFVRRG-VDG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 322 ASIDDSEELMATDSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDAdKSAYLMGLNSADLLKGLC 401
Cdd:cd14875 232 KTLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFL-TACRLLQLDPAKLRECFL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 402 hprVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLetkQPRQ-----YFIGVLDIAGFEIFDFNSFEQ 476
Cdd:cd14875 311 ---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASI---TPQGdcsgcKYIGLLDIFGFENFTRNSFEQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 477 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLYD 555
Cdd:cd14875 385 LCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWD 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 556 NHLGKSNNFQKPRNVKGKQeahFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADTADssk 635
Cdd:cd14875 464 QWANKSPYFVLPKSTIPNQ---FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRK--- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 636 gkggkkkgssfQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRI 715
Cdd:cd14875 538 -----------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRR 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 716 LYGDF-RQRYRILNPAAIPEGQFIDSRKGAEKLLSSLDIDHN----QYKFGHTKVFFK 768
Cdd:cd14875 607 PIEQFcRYFYLIMPRSTASLFKQEKYSEAAKDFLAYYQRLYGwakpNYAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
100-725 |
6.55e-108 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 362.88 E-value: 6.55e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYR-------GKKRSEA---PPHIFSISDNAYQYMLTD 168
Cdd:cd14899 2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhnsqfGDRVTSTdprEPHLFAVARAAYIDIVQN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 169 RENQSILITGESGAGKTVNTKRVIQYFA------SIAAIGDRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNS 242
Cdd:cd14899 82 GRSQSILISGESGAGKTEATKIIMTYFAvhcgtgNNNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 243 SRFGKFIRIHF-GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNK----KPDLLDMLLVTNNPYDYAFVSQG 317
Cdd:cd14899 162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 318 EVSVA--SIDDSEELMATDSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQ--KQREEQAEPDGTEDA----------D 383
Cdd:cd14899 242 LCSKRrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhfT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 384 KSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQY------- 456
Cdd:cd14899 322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASAPWgadesdv 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 457 --------FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlQACIDLIE-K 527
Cdd:cd14899 402 ddeedatdFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 528 PMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVV 607
Cdd:cd14899 481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 608 GLYQKSSLKLMATLFSSYASADTADSSKGKGGKKKGSSFQ-------TVSALHRENLNKLMTNLKTTHPHFVRCIIPNER 680
Cdd:cd14899 561 QLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAksaiaavSVGTQFKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 431907173 681 KAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 725
Cdd:cd14899 641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
105-768 |
1.52e-107 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 359.59 E-value: 1.52e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 105 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRS-----EAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 179 ESGAGKTVNTKRVIQYFASiaaigdrGKKDNANankgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAY-------GHSTSST----DVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQI---LSNKKPDLLDMLLVTNnpydYAFVSQGEVSVA-SIDDSEELMATD 334
Cdd:cd14886 156 LKGGKITSYMLELSRIEFQSTNERNYHIFYQCikgLSPEEKKSLGFKSLES----YNFLNASKCYDApGIDDQKEFAPVR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 335 SAFDVLgFTPEEKAGVYKLTGAIMHYGNMKFKQKQR---EEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEY 411
Cdd:cd14886 232 SQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNET 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 412 VTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFN 491
Cdd:cd14886 311 IISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 492 HHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEKP-MGIMSILEEECMFPKATDMTFKAKLyDNHLgKSNNFQKPrnv 570
Cdd:cd14886 391 NQVFKSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSFIPG--- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 571 KGKQeAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADtadsskgkggkkKGSSFQTVS 650
Cdd:cd14886 465 KGSQ-CNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNED------------GNMKGKFLG 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 651 ALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL--- 727
Cdd:cd14886 532 STFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILish 611
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 431907173 728 NPAAIPEGQfiDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14886 612 NSSSQNAGE--DLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
101-768 |
5.34e-105 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 353.54 E-value: 5.34e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 101 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd01386 3 VLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 181 GAGKTVNTKRVIQYFASIA-AIGDRGKKDNANAnkgtledqiiqANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 259
Cdd:cd01386 83 GSGKTTNCRHILEYLVTAAgSVGGVLSVEKLNA-----------ALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNPYDYAFvsqGEVSVASIDD----SEELMATDS 335
Cdd:cd01386 152 ASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSF---GIVPLQKPEDkqkaAAAFSKLQA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 336 AFDVLGFTPEEKAGVYKLTGAIMHYGN---MKFKQKQREEQAEPdgtEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 412
Cdd:cd01386 229 AMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 413 T---------------KGQSVQQvyySIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN----- 472
Cdd:cd01386 306 TtssgqesparsssggPKLTGVE---ALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqrg 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 473 -SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEK---------------PMGIMSILE 536
Cdd:cd01386 383 aTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGLLWLLD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 537 EECMFPKATDMTFKAKLYdNHLGKSNNFQKPRNV-KGKQEAHFSLIHYAGT--VDYNILGWLEKNK-DPLNETVVGLYQK 612
Cdd:cd01386 463 EEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLrRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQE 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 613 SSLKLMATLFSSYASAdtadsskgkggkkkgSSFQtvsalhrenLNKLMTNLKTTHPHFVRCIIPN------ERKAPGV- 685
Cdd:cd01386 542 SQKETAAVKRKSPCLQ---------------IKFQ---------VDALIDTLRRTGLHFVHCLLPQhnagkdERSTSSPa 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 686 -----MDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA----AIPEGQFIDSRKGAEKLLSSLDIDHN 756
Cdd:cd01386 598 agdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPltkkLGLNSEVADERKAVEELLEELDLEKS 677
|
730
....*....|..
gi 431907173 757 QYKFGHTKVFFK 768
Cdd:cd01386 678 SYRIGLSQVFFR 689
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-743 |
1.45e-100 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 336.87 E-value: 1.45e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKwlPVYNAEVVAAYRgKKRSEAPPHIFSISDNAYQYMLTdRENQSILITGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 180 SGAGKTVNTKRVIQYFASiaaigdrgkkdnANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgaTGKL 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLVE------------RTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGKI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKpdlldmLLVTNNPYDYAFVSQGEVSVasIDDSEELMATDSAFDV 339
Cdd:cd14898 144 TGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESI--VQLSEKYKMTCSAMKS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 340 LGFTPEEKagVYKLTGAIMHYGNMKFKQkqrEEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQ 419
Cdd:cd14898 216 LGIANFKS--IEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 420 QVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQyfIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 499
Cdd:cd14898 291 QARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQ 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 500 EEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKAT--DMTFKAKLYDNHlgksnnfqkprNVKGKQEAH 577
Cdd:cd14898 369 GMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNvkNLLVKIKKYLNG-----------FINTKARDK 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 578 FSLIHYAGTVDYNILGWLEKNKdplnetvvglyQKSSLKLMATLFssyasadTADSSKGkggkkkgssfQTVSALHRENL 657
Cdd:cd14898 437 IKVSHYAGDVEYDLRDFLDKNR-----------EKGQLLIFKNLL-------INDEGSK----------EDLVKYFKDSM 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 658 NKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIpegQF 737
Cdd:cd14898 489 NKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITLF---EV 565
|
....*.
gi 431907173 738 IDSRKG 743
Cdd:cd14898 566 VDYRKG 571
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
100-727 |
4.43e-95 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 323.69 E-value: 4.43e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYR---GKKRSEAPPHIFSISDNAYQYMLTDRENQSILI 176
Cdd:cd14878 2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 177 TGESGAGKTVNTKRVIQYFASiaaigdrgkkdNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 256
Cdd:cd14878 82 SGERGSGKTEASKQIMKHLTC-----------RASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 257 GK-LASADIETYLLEKSRVIFQLKAERNYHIFYQI---LSNKKPDLLDMllvtNNPYDYAFVSQGE----VSVASIDDSE 328
Cdd:cd14878 151 KKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLmdgLSAEEKYGLHL----NNLCAHRYLNQTMredvSTAERSLNRE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 329 ELMATDSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVG 408
Cdd:cd14878 227 KLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 409 NEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATL----ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNE 484
Cdd:cd14878 307 GDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 485 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACID-LIEKPMGIMSILEEECMFPKATDMTFKAKLyDNHLGKSNN 563
Cdd:cd14878 387 KMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDfFFQKPSGFLSLLDEESQMIWSVEPNLPKKL-QSLLESSNT 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 564 FQKPRNVKG--------KQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSyasadtadssk 635
Cdd:cd14878 466 NAVYSPMKDgngnvalkDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQS----------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 636 gkggkkkgsSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRI 715
Cdd:cd14878 535 ---------KLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRL 605
|
650
....*....|..
gi 431907173 716 LYGDFRQRYRIL 727
Cdd:cd14878 606 SFSDFLSRYKPL 617
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
101-768 |
1.31e-91 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 312.72 E-value: 1.31e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 101 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEvvaaYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 181 GAGKTVNTKRVIQYFASIAaigdrgKKDNANANkgTLEDqiiqANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 260
Cdd:cd14937 79 GSGKTEASKLVIKYYLSGV------KEDNEISN--TLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 261 SADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNPyDYAFVSQGEVSVASIDDSEELMATDSAFDVL 340
Cdd:cd14937 147 SSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDFGNLMISFDKM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 341 GFTPEEKAGVYKLTGAIMhYGNMKFKQ-----KQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKG 415
Cdd:cd14937 226 NMHDMKDDLFLTLSGLLL-LGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 416 QSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14937 305 LSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 496 VLEQEEYKKEGIEWTFIDFGMDlQACIDLIEKPMGIMSILEEECMFPKATDMTFkAKLYDNHLGKSNNFQkprNVKGKQE 575
Cdd:cd14937 385 EKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESI-VSVYTNKFSKHEKYA---STKKDIN 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 576 AHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYASADTADSSkgkggkkkgssfQTVSALHRE 655
Cdd:cd14937 460 KNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRK------------NLITFKYLK 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 656 NLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRIcRKGFPNRILYGDFRQRYRILNPAAIPEG 735
Cdd:cd14937 528 NLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDS 606
|
650 660 670
....*....|....*....|....*....|...
gi 431907173 736 QFIDSRKGAEKLLSSLDIDhnQYKFGHTKVFFK 768
Cdd:cd14937 607 SLTDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-768 |
1.34e-91 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 315.43 E-value: 1.34e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAA--------WMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 171 NQSILITGESGAGKTVNTKRVIQYfasIAAIGDRGKkdnaNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIR 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTY---LAAVSDRRH----GADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 251 IHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKK-PDLLDMLLVTNNPYDYafvsqgevsvasiddseE 329
Cdd:cd14887 154 LHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVaAATQKSSAGEGDPEST-----------------D 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 330 LMATDSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEP-----------DGTEDADKSAYLMGLNS----- 393
Cdd:cd14887 217 LRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKrkltsvsvgceETAADRSHSSEVKCLSSglkvt 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 394 -------ADLLKGLCHPRVKVGNEYV------------TKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPR 454
Cdd:cd14887 297 easrkhlKTVARLLGLPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 455 QY--------------FIGVLDIAGFEIF---DFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEG--IEWTFIDFG 515
Cdd:cd14887 377 SEsdsdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGvfQNQDCSAFP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 516 MDLQACIDLIEKP------------------------MGIMSILEEE-CMFPKATDMTFKAKLYDNHLGK----SNNFQK 566
Cdd:cd14887 457 FSFPLASTLTSSPsstspfsptpsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniinSAKYKN 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 567 PRNVKGKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNEtvvglyqksSLKLMATLFSSYASADTADSSKGKGGKKKGSsf 646
Cdd:cd14887 537 ITPALSRENLEFTVSHFACDVTYDARDFCRANREATSD---------ELERLFLACSTYTRLVGSKKNSGVRAISSRR-- 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 647 QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 726
Cdd:cd14887 606 STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYET 685
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 431907173 727 LNPAAIPEgqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 768
Cdd:cd14887 686 KLPMALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
105-767 |
3.61e-86 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 297.15 E-value: 3.61e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 105 LKERYAAWMIYTY---SGLfcVTVNPYKWLPVYNAEVVAAYR-------GKKRSEAPPHIFSISDNAYQYMLTDRENQSI 174
Cdd:cd14879 10 LASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRRRSEDQAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 175 LITGESGAGKTVNTKRVIQYFASIAAIGDRGKKdnanankgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 254
Cdd:cd14879 88 VFLGETGSGKSESRRLLLRQLLRLSSHSKKGTK---------LSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 255 ATGKLASADIETYLLEKSRVIfQLKA-ERNYHIFYQILSNKKPDLLDmLLVTNNPYDYAFV----SQGEVSVASIDDSE- 328
Cdd:cd14879 159 ERGRLIGAKVLDYRLERSRVA-SVPTgERNFHVFYYLLAGASPEERQ-HLGLDDPSDYALLasygCHPLPLGPGSDDAEg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 329 --ELMAtdsAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQkqreeqaEPDGTEDA---------DKSAYLMGLNSADLL 397
Cdd:cd14879 237 fqELKT---ALKTLGFKRKHVAQICQLLAAILHLGNLEFTY-------DHEGGEESavvkntdvlDIVAAFLGVSPEDLE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 398 KGLCHPRVKVGNEYVT-----KGQSVQQvyysiGALAKAVYEKMFNWMVTRINATL-ETKQPRQYFIGVLDIAGFEIFD- 470
Cdd:cd14879 307 TSLTYKTKLVRKELCTvfldpEGAAAQR-----DELARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRSs 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 471 --FNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEEC-MFPKATD 546
Cdd:cd14879 382 tgGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKTD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 547 MTFKAKLyDNHLGKSNNFQKPRNVKGKQEAH-FSLIHYAGTVDYNILGWLEKNKDPLNETVVglyqksslklmaTLFSSy 625
Cdd:cd14879 461 EQMLEAL-RKRFGNHSSFIAVGNFATRSGSAsFTVNHYAGEVTYSVEGFLERNGDVLSPDFV------------NLLRG- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 626 asadtadsskgkggkkkgssfqtvSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIR 705
Cdd:cd14879 527 ------------------------ATQLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAA 582
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 431907173 706 ICRKGFPNRILYGDFRQRYrilnpaaIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFF 767
Cdd:cd14879 583 RLRVEYVVSLEHAEFCERY-------KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-716 |
1.66e-78 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 276.02 E-value: 1.66e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEA-------PPHIFSISDNAYQYMLTDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 171 NQSILITGESGAGKTVNTKRVIQYFASIaaigdrgkkdNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIR 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----------QTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 251 IHF---------GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNPYDYAFV------- 314
Cdd:cd14884 151 LIFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLnpdeshq 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 315 ---SQGEVSVAS--IDDSEELMATDSA-----FDVLGFTPEEKAGV---YKLTGAIMHYGNMKFKQkqreeqaepdgted 381
Cdd:cd14884 231 krsVKGTLRLGSdsLDPSEEEKAKDEKnfvalLHGLHYIKYDERQInefFDIIAGILHLGNRAYKA-------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 382 adkSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINAT----------LETK 451
Cdd:cd14884 297 ---AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNvlkckekdesDNED 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 452 QPR--QYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDF--GMDLQACIDLIEK 527
Cdd:cd14884 374 IYSinEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVApsYSDTLIFIAKIFR 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 528 PMGIMSILEEECMfpKATDMTFKAKLYDNH----------LGK-SNNFQKPRNVKGK-QEAHFSLIHYAGTVDYNILGWL 595
Cdd:cd14884 454 RLDDITKLKNQGQ--KKTDDHFFRYLLNNErqqqlegkvsYGFvLNHDADGTAKKQNiKKNIFFIRHYAGLVTYRINNWI 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 596 EKNKDPLNETVVGLYQKSSLKLMatlfssyasadtadssKGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCI 675
Cdd:cd14884 532 DKNSDKIETSIETLISCSSNRFL----------------REANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCF 595
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 431907173 676 IPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRIL 716
Cdd:cd14884 596 LPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| FAT-like_EFS_C |
cd11571 |
C-terminal FAT-like Four helix bundle domain, also called DUF3513, of CAS (Crk-Associated ... |
2339-2468 |
3.66e-74 |
|
C-terminal FAT-like Four helix bundle domain, also called DUF3513, of CAS (Crk-Associated Substrate) scaffolding protein, Embryonal Fyn-associated Substrate; a protein interaction module; EFS is also called HEFS, CASS3 (CAS scaffolding protein family member 3) or SIN (Src-interacting protein). It was identified based on interactions with the Src kinases, Fyn and Yes. It plays a role in thymocyte development and acts as a negative regulator of T cell proliferation. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure containing protein interaction modules that enable their scaffolding function, including an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain, which binds to the C-terminal domain of NSPs (novel SH2-containing proteins) to form multidomain signaling modules that mediate cell migration and invasion.
Pssm-ID: 211412 Cd Length: 130 Bit Score: 242.83 E-value: 3.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2339 GDLQLLHFYAGQCQSHYSALQAAVEALTSSTRANQPPRLFVPHSKRVVVAAHRLVFVGDTLSRLAASTPLRAQVGAAGTA 2418
Cdd:cd11571 1 EDSQLLHFYAGQCQSHYSTLLAAVAALLSSTQANQPPRVFVPHGKRLIVAAHKLVFVGDTLGRLASSAPLRARVATAGGA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 431907173 2419 LGQALRATVLAVKAAALGYPSSPATEEMAQCVAELAGRALQFTNLLTSLA 2468
Cdd:cd11571 81 LCQALKAVVLATKGAALGYPSPPAAQEMAQCVADLSGQALQFTTLLQSLA 130
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
100-768 |
1.88e-73 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 259.42 E-value: 1.88e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYrgkkrseappHIFSISDNAYQYMLTDREN-QSILITG 178
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 179 ESGAGKTVNTKRVIQYFASiaaigdrgkkdNANANKGTLEDQIIQAnpALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 258
Cdd:cd14874 72 ESGSGKSYNAFQVFKYLTS-----------QPKSKVTTKHSSAIES--VFKSFGCAKTLKNDEATRFGCSIDLLYKRNVL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 259 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKpDLLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14874 139 TGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLN-DEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALH 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 339 VLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQR---EEQAEPDGTEDADK-SAYLMGLNSADLLKGLChPRVKVGNEYvtk 414
Cdd:cd14874 218 VLGFSDDHCISIYKIISTILHIGNIYFRTKRNpnvEQDVVEIGNMSEVKwVAFLLEVDFDQLVNFLL-PKSEDGTTI--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 415 gqSVQQVYYSIGALAKAVYEKMFNWMVTRINatLETKQPRQY-FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 493
Cdd:cd14874 294 --DLNAALDNRDSFAMLIYEELFKWVLNRIG--LHLKCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKH 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 494 MFVLEQEEYKKEGIEwtfIDFGMdlQACID-------LIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNnFQK 566
Cdd:cd14874 370 SFHDQLVDYAKDGIS---VDYKV--PNSIEngktvelLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS-YGK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 567 PRNvkgKQEAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSYaSADTADSskgkggkkkgssF 646
Cdd:cd14874 444 ARN---KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESY-SSNTSDM------------I 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 647 QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 726
Cdd:cd14874 508 VSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRC 587
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 431907173 727 LNPAAIPEGQfiDSRKGAEKLLSSLDIDH-NQYKFGHTKVFFK 768
Cdd:cd14874 588 LLPGDIAMCQ--NEKEIIQDILQGQGVKYeNDFKIGTEYVFLR 628
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-748 |
3.48e-70 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 250.03 E-value: 3.48e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 100 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPvyNAEVVAAYRGKKRSeapPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 180 SGAGKTVNTKRVIQYFASIAaigdrGKKDNANANKgtledQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgATGKL 259
Cdd:cd14881 77 SGSGKTYASMLLLRQLFDVA-----GGGPETDAFK-----HLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDGAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 260 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDML-LVTNNPYDYAFVSQGEVSVASIDDSEELMATDSAFD 338
Cdd:cd14881 146 YRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLhLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKACLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 339 VLG--FTpeekaGVYKLTGAIMHYGNMKFKQKQrEEQAEPDGTEDADKSAYLMGLNSADLLKGL---CHprvkvgneyVT 413
Cdd:cd14881 226 ILGipFL-----DVVRVLAAVLLLGNVQFIDGG-GLEVDVKGETELKSVAALLGVSGAALFRGLttrTH---------NA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 414 KGQ---SVQQVYYSIG---ALAKAVYEKMFNWMVTRIN------ATLETKQpRQYFIGVLDIAGFEIFDFNSFEQLCINF 481
Cdd:cd14881 291 RGQlvkSVCDANMSNMtrdALAKALYCRTVATIVRRANslkrlgSTLGTHA-TDGFIGILDMFGFEDPKPSQLEHLCINL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 482 TNEKLQQFFNHHMFVLEQEEYKKEGIewtfidfGMDLQA-------CIDLIEK-PMGIMSILEEECMfPKATDMTFKAKL 553
Cdd:cd14881 370 CAETMQHFYNTHIFKSSIESCRDEGI-------QCEVEVdyvdnvpCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKI 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 554 YDNHlgKSNN-FQKPRNVKGKQeahFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMatlFSSYasadTAD 632
Cdd:cd14881 442 KVQH--RQNPrLFEAKPQDDRM---FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNFG---FATH----TQD 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 633 sskgkggkkkgssFQTvsalhreNLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFP 712
Cdd:cd14881 510 -------------FHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYP 569
|
650 660 670
....*....|....*....|....*....|....*.
gi 431907173 713 NRILYGDFRQRYRILNPAAiPEGQFIDSRKGAEKLL 748
Cdd:cd14881 570 HRMRFKAFNARYRLLAPFR-LLRRVEEKALEDCALI 604
|
|
| CAS_C |
pfam12026 |
Crk-Associated Substrate C-terminal domain; This is a C-terminal domain found in CAS family ... |
2279-2464 |
4.64e-66 |
|
Crk-Associated Substrate C-terminal domain; This is a C-terminal domain found in CAS family members. The CAS (Crk-Associated Substrate) protein family is a group of scaffolding proteins that play important modulatory roles in both normal and pathological cell growth regulation. They contain an N-terminal Src homology 3 (SH3) domain pfam00018 and a substrate domain (SD). The SD contains a large number of YxxP motifs, which when phosphorylated by Src-family kinases provide canonical binding sites for proteins containing SH2 domains such as Crk, Crk-L, CRKII presumed domain is functionally uncharacterized.
Pssm-ID: 463437 Cd Length: 202 Bit Score: 222.65 E-value: 4.64e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2279 EYEGIPMTEEYDYVHLKGMDKAQGSRPLDKAFPGDPELQERGPLEQQEAL----------------STGEPLVLPTGDLQ 2342
Cdd:pfam12026 1 ENEGKSWMEDYDYVHLQGKEEFERQQKELLEKLPAEEQFENLIKQSKSQLeqqqqevtqpvedpsnWTPPQSQLSPNDRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2343 LLHFYAGQCQSHYSALQAAVEALTSSTRANQPPRLFVPHSKRVVVAAHRLVFVGDTLSRLAASTPLRAQVGAAGTALGQA 2422
Cdd:pfam12026 81 LLLFYSEQCETHFGALLNAIDAFFSSLSNNQPPKIFVAHSKFVILSAHKLVFIGDTLCRQASAADVRNRVLHCSNALCEL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 431907173 2423 LRATVLAVKAAALGYPSSPATEEMAQCVAELAGRALQFTNLL 2464
Cdd:pfam12026 161 LKTLVLATKKAALQYPSPAAVQEMVDRVTELSHHAQQFKTVL 202
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
105-720 |
7.29e-66 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 238.07 E-value: 7.29e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 105 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYrgKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAG 183
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 184 KTVNTKRVIQYFASIAAigDRGKkdnanankgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASAD 263
Cdd:cd14905 85 KSENTKIIIQYLLTTDL--SRSK---------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 264 IETYLLEKSRVIFQLKAERNYHIFYQILSNKKpDLLDMLLVTNNPYDYAFVSQ-GEVSVASIDDSEELMATDSAFDVLGF 342
Cdd:cd14905 154 LYSYFLDENRVTYQNKGERNFHIFYQFLKGIT-DEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFFDF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 343 TPEEKAGVYKLTGAIMHYGNMKFKQKQREeqaepdgTEDADKSaylmglnsadLLKGLCH----PRVKVGNEYVT-KGQS 417
Cdd:cd14905 233 PSEKIDLIFKTLSFIIILGNVTFFQKNGK-------TEVKDRT----------LIESLSHnitfDSTKLENILISdRSMP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 418 VQQVYYSIGALAKAVYEKMFNWMVTRINATLetkQPRQY--FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14905 296 VNEAVENRDSLARSLYSALFHWIIDFLNSKL---KPTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 496 VLEQEEYKKEGIEW-TFIDFgMDLQACIDLIEKpmgIMSILEEECMFPKATDMTFKAKLydnhlgksNNFQKPRNVKGKQ 574
Cdd:cd14905 373 KQEQREYQTERIPWmTPISF-KDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL--------QNFLSRHHLFGKK 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 575 EAHFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMAT---LFSSYASADTADSSKGKGGKKKGSSFQTVSA 651
Cdd:cd14905 441 PNKFGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFSrdgVFNINATVAELNQMFDAKNTAKKSPLSIVKV 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 652 L------HRENLNKLMTN-------------------LKTTHP-------------HFVRCIIPNERKAPGVMDNPLVMH 693
Cdd:cd14905 521 LlscgsnNPNNVNNPNNNsgggggggnsgggsgsggsTYTTYSstnkainnsncdfHFIRCIKPNSKKTHLTFDVKSVNE 600
|
650 660 670
....*....|....*....|....*....|.
gi 431907173 694 QLRCNGVLEGIRICRKGFP----NRILYGDF 720
Cdd:cd14905 601 QIKSLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-767 |
9.90e-65 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 236.41 E-value: 9.90e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 102 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKR----------SEAPPHIFSISDNAYQYMLTDREN 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 172 QSILITGESGAGKTVNTKRVIQYFASIA-AIGDRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIR 250
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGdETEPRPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 251 IHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILS--NKKPDLLDMLLVTNNPYDYAFVSQG--EVSVASID- 325
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAgvQHDPTLRDSLEMNKCVNEFVMLKQAdpLATNFALDa 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 326 -DSEELMatdSAFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLN-------SADLL 397
Cdd:cd14893 244 rDYRDLM---SSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGANSTTVSDAQSCALKdpaqillAAKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 398 KglCHPRV------------KVGNEYVT--KGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPR--------- 454
Cdd:cd14893 321 E--VEPVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRyeksnivin 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 455 QYFIGVLDIAGFEIFD--FNSFEQLCINFTNEKLQQFFNHHMFV-----LEQEEYKKEG--IEWTFIDFGMDLQACIDLI 525
Cdd:cd14893 399 SQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 526 E-KPMGIMSILEEECMFPKATDMTFKAKLYDNH-----LGKSNNFQKPRNVKGKQEAHFSLI----HYAGTVDYNILGWL 595
Cdd:cd14893 479 EdKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNeavggLSRPNMGADTTNEYLAPSKDWRLLfivqHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 596 EKNKDPLNETVVGLYQKSSLKLMATLFSSYASADTADS--SKGKGGKKKGSSFQTVSALHRENLN--------------K 659
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKaaKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqadA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 660 LMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRilnpaaipegQFID 739
Cdd:cd14893 639 LLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK----------NVCG 708
|
730 740 750
....*....|....*....|....*....|..
gi 431907173 740 SRKGAEKLLSSLD----IDHNQYKFGHTKVFF 767
Cdd:cd14893 709 HRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
101-727 |
5.22e-63 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 228.86 E-value: 5.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 101 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 181 GAGKTVNTKRVIQYfasIAAIGDrgkkdnanANKGTLEdQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 260
Cdd:cd14882 83 YSGKTTNARLLIKH---LCYLGD--------GNRGATG-RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 261 SADIETYLLEKSRVIFQLKAERNYHIFYQILS--NKKPDLLDMLLVTNNPYDYAFVSQG-------------EVSVASID 325
Cdd:cd14882 151 GAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDfiEAQNRLKEYNLKAGRNYRYLRIPPEvppsklkyrrddpEGNVERYK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 326 DSEELmatdsaFDVLGFTPEEKAGVYKLTGAIMHYGNMKFKQKQREeqAEPDGTEDADKSAYLMGLNSADLLKGLCHPRV 405
Cdd:cd14882 231 EFEEI------LKDLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 406 KVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETkqPR-----QYFIGVLDIAGFEIFDFNSFEQLCIN 480
Cdd:cd14882 303 IKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSF--PRavfgdKYSISIHDMFGFECFHRNRLEQLMVN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 481 FTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEecmfpKATDMTFKAKLYDNHLGK 560
Cdd:cd14882 381 TLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD-----ASRSCQDQNYIMDRIKEK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 561 SNNFQKPRNvkgkqeAH-FSLIHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSSyasadtadsskgkgg 639
Cdd:cd14882 456 HSQFVKKHS------AHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN--------------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 640 kKKGSSFQTVSALHR----ENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRI 715
Cdd:cd14882 515 -SQVRNMRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRI 593
|
650
....*....|..
gi 431907173 716 LYGDFRQRYRIL 727
Cdd:cd14882 594 PFQEFLRRYQFL 605
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-251 |
1.44e-60 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 205.66 E-value: 1.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 121 FCVTVNPYKWLPVYNAEVV-AAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFASIA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 200 AIGDRGKKDNANAN----KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 251
Cdd:cd01363 81 FNGINKGETEGWVYlteiTVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| FAT-like_CAS_C |
cd11564 |
C-terminal FAT-like Four helix bundle domain, also called DUF3513, of CAS (Crk-Associated ... |
2340-2465 |
2.04e-53 |
|
C-terminal FAT-like Four helix bundle domain, also called DUF3513, of CAS (Crk-Associated Substrate) scaffolding proteins; a protein interaction module; CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes including migration, chemotaxis, apoptosis, differentiation, and progenitor cell function. They mediate the signaling of integrins at focal adhesions where they localize, and thus, regulate cell invasion and survival. Over-expression of these proteins is implicated in poor prognosis, increased metastasis, and resistance to chemotherapeutics in many cancers such as breast, lung, melanoma, and glioblastoma. CAS proteins have also been linked to the pathogenesis of inflammatory disorders, Alzheimer's, Parkinson's, and developmental defects. They share a common domain structure containing protein interaction modules that enable their scaffolding function, including an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. Vertebrates contain four CAS proteins: BCAR1 (or p130Cas), NEDD9 (or HEF1), EFS (or SIN), and CASS4 (or HEPL). The FAT-like C-terminal domain of CAS proteins binds to the C-terminal domain of NSPs (novel SH2-containing proteins) to form multidomain signaling modules that mediate cell migration and invasion.
Pssm-ID: 211408 Cd Length: 126 Bit Score: 183.20 E-value: 2.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2340 DLQLLHFYAGQCQSHYSALQAAVEALTSSTRANQPPRLFVPHSKRVVVAAHRLVFVGDTLSRLAASTPLRAQVGAAGTAL 2419
Cdd:cd11564 1 DRQLLLFYSEQCESHFGALQKAIDAFLSSVESNQPPKVFVAHSKFVILSAHKLVFIGDTLCRNVQSADVRNKVLRCSNQL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 431907173 2420 GQALRATVLAVKAAALGYPSSPATEEMAQCVAELAGRALQFTNLLT 2465
Cdd:cd11564 81 CEALKTVVLATKKAALQYPSVAAVQEMVDRVVELSHHAQQFKTSLG 126
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-766 |
2.92e-53 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 201.22 E-value: 2.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 99 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYrgkKRSEAPPHI----FSISDNAYQYMLTDRENQSI 174
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKY---KCIDCIEDLslneYHVVHNALKNLNELKRNQSI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 175 LITGESGAGKTVNTKRVIQYFA------------SIAAIGDRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNS 242
Cdd:cd14938 78 IISGESGSGKSEIAKNIINFIAyqvkgsrrlptnLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 243 SRFGKFIRIHFgATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPDLLDMLLVTNNPYdYAFVSQGEVSVA 322
Cdd:cd14938 158 SRFSKFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIEN-YSMLNNEKGFEK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 323 SIDDSEELMATDSAFDVLGFTPEEKAGVYKLTGAIMHYGN-------------MKFKQKQRE----------EQAEPDGT 379
Cdd:cd14938 236 FSDYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 380 EDADKSAYL----MGLNSADLLKGLCHPRVkVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVTRINATLETKQPRQ 455
Cdd:cd14938 316 DENVKNLLLacklLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNIN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 456 YF---IGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM--G 530
Cdd:cd14938 395 INtnyINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 531 IMSILEEECMfPKATDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAhFSLIHYAGTVDYNILGWLEKNKDPLNETVVGLY 610
Cdd:cd14938 475 LFSLLENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 611 QKSSLKLMATLFSSYASADTADSSKGKGGKKKGSSF-----------QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNE 679
Cdd:cd14938 553 KQSENEYMRQFCMFYNYDNSGNIVEEKRRYSIQSALklfkrrydtknQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNE 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 680 RKAP-GVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPaaipegqfiDSRKGAEKLLSSLDIDHNQY 758
Cdd:cd14938 633 SKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEW 703
|
....*...
gi 431907173 759 KFGHTKVF 766
Cdd:cd14938 704 MIGNNMIF 711
|
|
| SH3_EFS |
cd12003 |
Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding protein family member, ... |
1928-1990 |
1.63e-35 |
|
Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding protein family member, Embryonal Fyn-associated Substrate; EFS is also called HEFS, CASS3 (Cas scaffolding protein family member 3) or SIN (Src-interacting protein). It was identified based on interactions with the Src kinases, Fyn and Yes. It plays a role in thymocyte development and acts as a negative regulator of T cell proliferation. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure that includes an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. The SH3 domain of CAS proteins binds to diverse partners including FAK, FRNK, Pyk2, PTP-PEST, DOCK180, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212936 Cd Length: 62 Bit Score: 130.01 E-value: 1.63e-35
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1928 QLARALYDNTAESPQELSFRRGDVLRVLQREGaGGLDGWCLCSLHGQQGIVPANRVKLLPAGP 1990
Cdd:cd12003 1 QLAKALYDNAAESPEELSFRRGDVLMVLKREH-GSLPGWWLCSLHGQQGIAPANRLRLLPTAP 62
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1146-1926 |
2.63e-33 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 141.73 E-value: 2.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1146 EEISERLEEAGGATSVqiemnkkreaefqKMRRdlEEATLQHEATAAALrKKHADSVAELGEQIDNLQRVKQK------- 1218
Cdd:TIGR02168 155 EERRAIFEEAAGISKY-------------KERR--KETERKLERTRENL-DRLEDILNELERQLKSLERQAEKaerykel 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1219 ------------------LEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQA 1280
Cdd:TIGR02168 219 kaelrelelallvlrleeLREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1281 KLQtengelaRQLEEKEALISQLTRGKLSYTQQTEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQ 1360
Cdd:TIGR02168 299 RLE-------QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1361 RVLSKANSEVAQWRTKYetDAIQRTEELEEAKLQDAEEAVEavnakcsSLEKTKHRLQNEIEDLmvDVERSNAAAAALDK 1440
Cdd:TIGR02168 372 SRLEELEEQLETLRSKV--AQLELQIASLNNEIERLEARLE-------RLEDRRERLQQEIEEL--LKKLEEAELKELQA 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1441 KQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEES---LEHLETFKRENKNLQEEISDLT---EQLGE 1514
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLqarLDSLERLQENLEGFSEGVKALLknqSGLSG 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1515 GGKNVHELEKVRKQLEAEKLE-------------LQSALEEAEASLEHEEGK--------ILRAQLEFN--QIKAEIERK 1571
Cdd:TIGR02168 521 ILGVLSELISVDEGYEAAIEAalggrlqavvvenLNAAKKAIAFLKQNELGRvtflpldsIKGTEIQGNdrEILKNIEGF 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1572 LAEKDEEMEQAKR---------NHLRVVDSLQTSL-----------------------------DAETRS-----RNEAL 1608
Cdd:TIGR02168 601 LGVAKDLVKFDPKlrkalsyllGGVLVVDDLDNALelakklrpgyrivtldgdlvrpggvitggSAKTNSsilerRREIE 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1609 RVKKK---MEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKENIAIVERRNNLLQAELEELR 1685
Cdd:TIGR02168 681 ELEEKieeLEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1686 AVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKakkaitdaammaeeL 1765
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER--------------L 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1766 KKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEqialkggkKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKE 1845
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLA--------AEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1846 LTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFR-KVQHELDEAEERADIAESQVNKLRAKSRDIG 1924
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
..
gi 431907173 1925 AK 1926
Cdd:TIGR02168 979 NK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
978-1867 |
4.77e-33 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 140.96 E-value: 4.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 978 KNLTEEMAGldeiIAKLTKEKKalqEAHQQ---ALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVR------- 1047
Cdd:TIGR02168 158 RAIFEEAAG----ISKYKERRK---ETERKlerTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRelelall 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1048 -MDLERAKRKLEGdlklTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEA 1126
Cdd:TIGR02168 231 vLRLEELREELEE----LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQI 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1127 ERTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnkkrEAEFQKMRRDLEEATLQHEATAAALRKKHADsVAELG 1206
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDEL--------------AEELAELEEKLEELKEELESLEAELEELEAE-LEELE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1207 EQIDNLQrvkQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRslNDFTTQQAKLQTEN 1286
Cdd:TIGR02168 372 SRLEELE---EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELE 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1287 GELARQLEEKEALISQLTRGKLSYTQQTEDLkRQLEEEGKAKNALAHALQSarhdcdlLREQYEEETEAKAELQRVLSKA 1366
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQAL-DAAERELAQLQARLDSLER-------LQENLEGFSEGVKALLKNQSGL 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1367 N------SEVAQWRTKYETdAIqrtEELEEAKLQ-----DAEEAVEAVNA-------KCSSLEKTKHR---LQNEIEDLM 1425
Cdd:TIGR02168 519 SgilgvlSELISVDEGYEA-AI---EAALGGRLQavvveNLNAAKKAIAFlkqnelgRVTFLPLDSIKgteIQGNDREIL 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1426 VDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNL---- 1501
Cdd:TIGR02168 595 KNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSsile 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1502 -QEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERkLAEKDEEME 1580
Cdd:TIGR02168 675 rRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ-LEERIAQLS 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1581 QAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRTaseaqkhLKIAQAHLKDTQLQMDDAVRAN 1660
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA-------LDELRAELTLLNEEAANLRERL 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1661 DDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKlAEQELIETservqlLHSQNTSLINQKKKMESDLTQLQSEVEEA 1740
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE-ELEELIEE------LESELEALLNERASLEEALALLRSELEEL 899
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1741 VQECRNAEEKAKKAITDAAMMAEELKKEQdtsAHLERMKKNMEQTIKDL--QHRLDEAEQIALK-GGKKQLQKLEARVRE 1817
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLE---LRLEGLEVRIDNLQERLseEYSLTLEEAEALEnKIEDDEEEARRRLKR 976
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 431907173 1818 LENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKL 1867
Cdd:TIGR02168 977 LENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| FAT-like_BCAR1_C |
cd11569 |
C-terminal FAT-like Four helix bundle domain, also called DUF3513, of CAS (Crk-Associated ... |
2336-2467 |
9.61e-33 |
|
C-terminal FAT-like Four helix bundle domain, also called DUF3513, of CAS (Crk-Associated Substrate) scaffolding protein, Breast Cancer Anti-estrogen Resistance 1; a protein interaction module; BCAR1, also called p130cas or CASS1, is the founding member of the CAS family of scaffolding proteins and was originally identified through its ability to associate with Crk. The name BCAR1 was designated because the human gene was identified in a screen for genes that promote resistance to tamoxifen. It is widely expressed and its deletion is lethal in mice. It plays a role in regulating cell motility, survival, proliferation, transformation, cancer progression, and bacterial pathogenesis. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure containing protein interaction modules that enable their scaffolding function, including an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain, which binds to the C-terminal domain of NSPs (novel SH2-containing proteins) to form multidomain signaling modules that mediate cell migration and invasion.
Pssm-ID: 211410 Cd Length: 133 Bit Score: 124.72 E-value: 9.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2336 LPTGDLQLLHFYAGQCQSHYSALQAAVEALTSSTRANQPPRLFVPHSKRVVVAAHRLVFVGDTLSRLAASTPLRAQVGAA 2415
Cdd:cd11569 2 LGPSDRQLLLFYQEQCEANVTTLTNAIDAFFTSISSNQPPKIFVAHSKFVILSAHKLVFIGDTLSRQAKAADVRSKVTHY 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 431907173 2416 GTALGQALRATVLAVKAAALGYPSSPATEEMAQCVAELAGRALQFTNLLTSL 2467
Cdd:cd11569 82 SNLLCEKLKEIVLSTKTAALQYPSPAAAKDMVERVKELGGSTQQFRMVLGQL 133
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
837-1739 |
3.09e-31 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 134.80 E-value: 3.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 837 KIKPLLKSAETEKEMANMKEEFGRLKETLekSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLiknkiq 916
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL------ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 917 lEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTK 996
Cdd:TIGR02168 273 -RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 997 EKKALQEAHQQALDDLQAEEDKVNTLTKskvKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGdlklTQESIMDLENDKL 1076
Cdd:TIGR02168 352 ELESLEAELEELEAELEELESRLEELEE---QLETLRSKVAQLELQIASLNNEIERLEARLER----LEDRRERLQQEIE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1077 QLEEKLKKKEFDISQQNskIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAG 1156
Cdd:TIGR02168 425 ELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1157 GATS--VQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAelgeqIDNLQRVKQKLE--KEKSEFK---LE 1229
Cdd:TIGR02168 503 GFSEgvKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVV-----VENLNAAKKAIAflKQNELGRvtfLP 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1230 LDDVT------------SNMEQIIKAKANLEKVSRTLE----------------DQANEYRTKLEEAQRslndFTTQQAK 1281
Cdd:TIGR02168 578 LDSIKgteiqgndreilKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvddlDNALELAKKLRPGYR----IVTLDGD 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1282 LQTENGELARQLEEKEALIsqltrgkLSYTQQTEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQR 1361
Cdd:TIGR02168 654 LVRPGGVITGGSAKTNSSI-------LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1362 VLSKANSEVAQWRTKYETDAIQRTEELEEakLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKK 1441
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEERIAQLSKE--LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1442 QRNFdkilaewkqkyeesqselessQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLgeggknvhe 1521
Cdd:TIGR02168 805 LDEL---------------------RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI--------- 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1522 lekvrKQLEAEKLELQSALEEAEASLEHEEgkilraqlefnQIKAEIERKLAEKDEEMEQAkRNHLRVVDSLQTSLDAET 1601
Cdd:TIGR02168 855 -----ESLAAEIEELEELIEELESELEALL-----------NERASLEEALALLRSELEEL-SEELRELESKRSELRREL 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1602 RSRNEALrvkKKMEGDLNEMEIQLSQANRTASEAQkhlkiaqahlkdtQLQMDDAVRANDDLKENIAIVERRNNLLQAEL 1681
Cdd:TIGR02168 918 EELREKL---AQLELRLEGLEVRIDNLQERLSEEY-------------SLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1682 EELRAVVEqtersrkLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEE 1739
Cdd:TIGR02168 982 KELGPVNL-------AAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| FAT-like_NEDD9_C |
cd11570 |
C-terminal FAT-like Four helix bundle domain, also called DUF3513, of CAS (Crk-Associated ... |
2340-2460 |
2.86e-30 |
|
C-terminal FAT-like Four helix bundle domain, also called DUF3513, of CAS (Crk-Associated Substrate) scaffolding protein, Neural precursor cell Expressed, Developmentally Down-regulated 9; a protein interaction module; NEDD9 is also called human enhancer of filamentation 1 (HEF1) or CAS-L (Crk-associated substrate in lymphocyte). It was first described as a gene predominantly expressed in early embryonic brain, and was also isolated from a screen of human proteins that regulate filamentous budding in yeast, and as a tyrosine phosphorylated protein in lymphocytes. It promotes metastasis in different solid tumors. NEDD9 localizes in focal adhesions and associates with FAK and Abl kinase. It also interacts with SMAD3 and the proteasomal machinery which allows its rapid turnover; these interactions are not shared by other CAS proteins. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure containing protein interaction modules that enable their scaffolding function, including an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain, which binds to the C-terminal domain of NSPs (novel SH2-containing proteins) to form multidomain signaling modules that mediate cell migration and invasion.
Pssm-ID: 211411 Cd Length: 128 Bit Score: 117.32 E-value: 2.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2340 DLQLLHFYAGQCQSHYSALQAAVEALTSSTRANQPPRLFVPHSKRVVVAAHRLVFVGDTLSRLAASTPLRAQVGAAGTAL 2419
Cdd:cd11570 1 DRQLLGFYADQCETHFISLLNAIDAFFSCVSSGQPPRIFVAHSKFVILSAHKLVFIGDTLTRQVTVQDIRNRVMNSSNQL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 431907173 2420 GQALRATVLAVKAAALGYPSSPATEEMAQCVAELAGRALQF 2460
Cdd:cd11570 81 CELLKTIVMATKMAALHYPSTAALQEMVDRVTDLSHLAQLF 121
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1261-1939 |
1.66e-29 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 129.41 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1261 YRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLTRGKlsytqqteDLKRQLEEegKAKNALAHALQSARH 1340
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYK--------ELKAELRE--LELALLVLRLEELRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1341 DCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYEtdaiqrteELEEaKLQDAEEAVEAVNAKCSSLEKTKHRLQNE 1420
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS--------ELEE-EIEELQKELYALANEISRLEQQKQILRER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1421 IEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKN 1500
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1501 LQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLE--------FNQIKAEIERKL 1572
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEelqeelerLEEALEELREEL 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1573 AEKDEEMEQAKRNH------LRVVDSLQTSLDAETRSRNEALRVKKKMEGDL----------NEMEIQLSQA-------- 1628
Cdd:TIGR02168 471 EEAEQALDAAERELaqlqarLDSLERLQENLEGFSEGVKALLKNQSGLSGILgvlselisvdEGYEAAIEAAlggrlqav 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1629 ----NRTASEAQKHLK---------IAQAHLKDTQLQMDDAVRAN---------------------------------DD 1662
Cdd:TIGR02168 551 vvenLNAAKKAIAFLKqnelgrvtfLPLDSIKGTEIQGNDREILKniegflgvakdlvkfdpklrkalsyllggvlvvDD 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1663 LKENIAI----------------------------VERRNNLL--QAELEELRAVVEQTERSRKLAEQELIETSERVQLL 1712
Cdd:TIGR02168 631 LDNALELakklrpgyrivtldgdlvrpggvitggsAKTNSSILerRREIEELEEKIEELEEKIAELEKALAELRKELEEL 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1713 HSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEK---AKKAITDA----AMMAEELKKEQDTSAHLERMKKNMEQT 1785
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqLSKELTELeaeiEELEERLEEAEEELAEAEAEIEELEAQ 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1786 IKDLQHRLDEAEQiALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVD 1865
Cdd:TIGR02168 791 IEQLKEELKALRE-ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1866 KLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKAQLARALYDNTAE 1939
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1132-1905 |
3.52e-29 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 128.26 E-value: 3.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1132 AKVEKLRsdlsRELEEISERLEEaggatsVQIEMNKKREaEFQKMRRDLEEAtLQHEATAAALRK----KHADSVAELGE 1207
Cdd:TIGR02169 170 RKKEKAL----EELEEVEENIER------LDLIIDEKRQ-QLERLRREREKA-ERYQALLKEKREyegyELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1208 QIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANL-EKVSRTLEDQANEYRTKLEEaqrslndFTTQQAKLQTEN 1286
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnKKIKDLGEEEQLRVKEKIGE-------LEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1287 GELARQLEEKEALISQLTRGKLSYTQQTEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKA 1366
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1367 NSEVAQwrTKYETDAIQRTEELEEAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVErsnaaaaALDKKQRNFD 1446
Cdd:TIGR02169 391 REKLEK--LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK-------KQEWKLEQLA 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1447 KILAEWKQKYEESQSELESSQKEARSLSTELfklknayeeslEHLETFKRENKNLQEEISDLTEQLGEGGKNVH----EL 1522
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEKELSKLQREL-----------AEAEAQARASEERVRGGRAVEEVLKASIQGVHgtvaQL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1523 EKVRkqlEAEKLELQSAL------------EEAEASLEH-EEGKILRAQ-LEFNQIKAE--------------IERKLAE 1574
Cdd:TIGR02169 531 GSVG---ERYATAIEVAAgnrlnnvvveddAVAKEAIELlKRRKAGRATfLPLNKMRDErrdlsilsedgvigFAVDLVE 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1575 KDEEMEQAKRNHLR---VVDSLQT-----------SLDAE-----------TRSRNEALRVKKKMEGDLNEMEIQLSQAN 1629
Cdd:TIGR02169 608 FDPKYEPAFKYVFGdtlVVEDIEAarrlmgkyrmvTLEGElfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLK 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1630 RTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERV 1709
Cdd:TIGR02169 688 RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARI 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1710 QLLHSQntslINQKKKMESDLTQ--LQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIK 1787
Cdd:TIGR02169 768 EELEED----LHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1788 DLQHRLDE-AEQIALKGGKK-----QLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQ 1861
Cdd:TIGR02169 844 DLKEQIKSiEKEIENLNGKKeeleeELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 431907173 1862 DLVDKLQLKVKAYKRQAEEAEEQANTNLSkFRKVQHELDEAEER 1905
Cdd:TIGR02169 924 AKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEE 966
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
842-1574 |
1.78e-28 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 125.95 E-value: 1.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 842 LKSAETEKEMAnmkEEFGRLKEtlEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKV 921
Cdd:TIGR02169 200 LERLRREREKA---ERYQALLK--EKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 922 KEMNERLED--EEEMNA------ELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAK 993
Cdd:TIGR02169 275 EELNKKIKDlgEEEQLRvkekigELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 994 LTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLEN 1073
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1074 DKLQLEEKLKKKEFDISQQNSKIE---------DEQALAL-----QLQKKLKENQARIEELEEELEAERTA----RAKVE 1135
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEqlaadlskyEQELYDLkeeydRVEKELSKLQRELAEAEAQARASEERvrggRAVEE 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1136 KLRSDLS------RELEEISER----LEEAGG-----------ATSVQ-IEMNKKREA------EFQKMRRDLEEATLQH 1187
Cdd:TIGR02169 515 VLKASIQgvhgtvAQLGSVGERyataIEVAAGnrlnnvvveddAVAKEaIELLKRRKAgratflPLNKMRDERRDLSILS 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1188 EATAAALrkkhADSVAELGEQIDNLQR-------VKQKLEKEKS---EFKL-----ELDDVTSNMEQIIKAKANLEKVSR 1252
Cdd:TIGR02169 595 EDGVIGF----AVDLVEFDPKYEPAFKyvfgdtlVVEDIEAARRlmgKYRMvtlegELFEKSGAMTGGSRAPRGGILFSR 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1253 TLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLTRGKLSYTQQTEDLKRQLEEegkaknala 1332
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE--------- 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1333 halqsarhdcdlLREQYEEETEAKAELQRVLSKANSEVAQwrtkYETDAIQRTEELEEAKLQDAEEAVEAVNAKCSSLEK 1412
Cdd:TIGR02169 742 ------------LEEDLSSLEQEIENVKSELKELEARIEE----LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEE 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1413 TKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLE 1492
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1493 TFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEASLEHEEgKILRAQLEFNQIKAEIERKL 1572
Cdd:TIGR02169 886 DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE-EIPEEELSLEDVQAELQRVE 964
|
..
gi 431907173 1573 AE 1574
Cdd:TIGR02169 965 EE 966
|
|
| SH3_CAS |
cd11844 |
Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding proteins; CAS proteins ... |
1929-1985 |
2.16e-28 |
|
Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding proteins; CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes including migration, chemotaxis, apoptosis, differentiation, and progenitor cell function. They mediate the signaling of integrins at focal adhesions where they localize, and thus, regulate cell invasion and survival. Over-expression of these proteins is implicated in poor prognosis, increased metastasis, and resistance to chemotherapeutics in many cancers such as breast, lung, melanoma, and glioblastoma. CAS proteins have also been linked to the pathogenesis of inflammatory disorders, Alzheimer's, Parkinson's, and developmental defects. They share a common domain structure that includes an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. Vertebrates contain four CAS proteins: BCAR1 (or p130Cas), NEDD9 (or HEF1), EFS (or SIN), and CASS4 (or HEPL). The SH3 domain of CAS proteins binds to diverse partners including FAK, FRNK, Pyk2, PTP-PEST, DOCK180, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212778 Cd Length: 56 Bit Score: 109.36 E-value: 2.16e-28
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1929 LARALYDNTAESPQELSFRRGDVLRVLQREGAgGLDGWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd11844 1 LARALYDNVAESPDELAFRRGDILTVLEQNTA-GLEGWWLCSLRGRQGIAPGNRLKL 56
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
835-1404 |
3.13e-27 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 121.58 E-value: 3.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 835 YFKIKPLLKSAETE---KEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLI 911
Cdd:COG1196 215 YRELKEELKELEAElllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 912 KNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEII 991
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 992 AKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDL 1071
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1072 ENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAK---------VEKLRSDLS 1142
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLaglrglagaVAVLIGVEA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1143 RELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKE 1222
Cdd:COG1196 535 AYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAR 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1223 KSEFKLELDDVTSnmeqiikAKANLEKVSRTLEDQANEYRTKLEEAQRSLndftTQQAKLQTENGELARQLEEKEALISQ 1302
Cdd:COG1196 615 YYVLGDTLLGRTL-------VAARLEAALRRAVTLAGRLREVTLEGEGGS----AGGSLTGGSRRELLAALLEAEAELEE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1303 LTRGKLSYTQQTEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAqwrtKYETDAI 1382
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA----LEELPEP 759
|
570 580
....*....|....*....|....
gi 431907173 1383 QRTEELEE--AKLQDAEEAVEAVN 1404
Cdd:COG1196 760 PDLEELERelERLEREIEALGPVN 783
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
989-1797 |
7.69e-26 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 117.14 E-value: 7.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 989 EIIAKLTKE--KKALQEAHQQaLDDLQAEEDKVNTL-TKSKVKLEQQVDDLEGSLEQ---EKKVRMDLERAKRKLEGDLK 1062
Cdd:pfam15921 66 KIIAYPGKEhiERVLEEYSHQ-VKDLQRRLNESNELhEKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQEDLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1063 ltqesiMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAE------------RTA 1130
Cdd:pfam15921 145 ------NQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKiyehdsmstmhfRSL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1131 RAKVEKLRSDLSRELEEISERLEEAGGA-TSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQI 1209
Cdd:pfam15921 219 GSAISKILRELDTEISYLKGRIFPVEDQlEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1210 DNLQRVKQKLEKEKSEFKLELDDVTSNMEQIikaKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGEL 1289
Cdd:pfam15921 299 SQLEIIQEQARNQNSMYMRQLSDLESTVSQL---RSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1290 ARQLEEkeaLISQLTRGKLSYTQQTEDLKRQLEEEGKAKNALAHalqsarhdcdlLREQYEEETEAKAELQRVLSKANSE 1369
Cdd:pfam15921 376 DDQLQK---LLADLHKREKELSLEKEQNKRLWDRDTGNSITIDH-----------LRRELDDRNMEVQRLEALLKAMKSE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1370 VaqwrtkyetdaiQRTEELEEAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLmvdversNAAAAALDKKQRNFDKIL 1449
Cdd:pfam15921 442 C------------QGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTVSDLT 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1450 AEWKQKyeesqselessQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQ------------------------EEI 1505
Cdd:pfam15921 503 ASLQEK-----------ERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRnvqtecealklqmaekdkvieilrQQI 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1506 SDLTEQLGEGGKNVHELEKVRKQLEAE----KLELQS---ALEEAEASLEHEEGKIlrAQLEFNQIK---AEIERKLAEK 1575
Cdd:pfam15921 572 ENMTQLVGQHGRTAGAMQVEKAQLEKEindrRLELQEfkiLKDKKDAKIRELEARV--SDLELEKVKlvnAGSERLRAVK 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1576 DEEMEQAK-RNHLRVVDSLQTSLDAETRSRNEALRVK-KKMEGDLNEMEIQLSQanrtaseAQKHLKIAQAHLKDTQLQM 1653
Cdd:pfam15921 650 DIKQERDQlLNEVKTSRNELNSLSEDYEVLKRNFRNKsEEMETTTNKLKMQLKS-------AQSELEQTRNTLKSMEGSD 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1654 DDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVqllhsqnTSLINQKKKMESDLTQL 1733
Cdd:pfam15921 723 GHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQEL-------STVATEKNKMAGELEVL 795
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1734 QSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLErmkknmeqtikdLQHRLDEAE 1797
Cdd:pfam15921 796 RSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK------------LQHTLDVKE 847
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1075-1725 |
2.20e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 115.42 E-value: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1075 KLQLEEKLKKKE---FDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISER 1151
Cdd:COG1196 217 ELKEELKELEAElllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1152 LEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALrkkhadsvAELGEQIDNLQRVKQKLEKEKSEFKLELD 1231
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL--------EELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1232 DVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLTRGKLSYT 1311
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1312 QQTEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKyETDAIQRTEELEEA 1391
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA-LLLAGLRGLAGAVA 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1392 KLQDAEEAVEAVnakcsslektkhrLQNEIEDLMVDVERSNAAAAAldkKQRNFDKILAEWKQKYEESQSELESSQKEAR 1471
Cdd:COG1196 528 VLIGVEAAYEAA-------------LEAALAAALQNIVVEDDEVAA---AAIEYLKAAKAGRATFLPLDKIRARAALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1472 SLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEASLEHEE 1551
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1552 GKILRAQLEfnqiKAEIERKLAEKDEEMEQAKRnhlrvvdslqtsldAETRSRNEALRVKKKMEGDLNEMEIQLSQANRT 1631
Cdd:COG1196 672 AALLEAEAE----LEELAERLAEEELELEEALL--------------AEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1632 ASEAQkhlkiaqAHLKDTQLQMDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEqtersrkLAEQELIETSERVQL 1711
Cdd:COG1196 734 REELL-------EELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVNL-------LAIEEYEELEERYDF 799
|
650
....*....|....
gi 431907173 1712 LHSQNTSLINQKKK 1725
Cdd:COG1196 800 LSEQREDLEEARET 813
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
848-1849 |
2.42e-24 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 112.13 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 848 EKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQ-----------AEQDNLNDAEERCDQLIKNKIQ 916
Cdd:pfam15921 102 EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQntvheleaakcLKEDMLEDSNTQIEQLRKMMLS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 917 LEAKVKEMNERLEDEEE-------------------MNAELTAKKRKLEDECSELKRDIDDLEltlAKVEKEKHATENKV 977
Cdd:pfam15921 182 HEGVLQEIRSILVDFEEasgkkiyehdsmstmhfrsLGSAISKILRELDTEISYLKGRIFPVE---DQLEALKSESQNKI 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 978 KNLTEEMAG-LDEIIAKLTKEKKALQE----AHQQAlDDLQAEEDKVNTLTKSKVKL-EQQVDDLEGSLEQekkVRMDLE 1051
Cdd:pfam15921 259 ELLLQQHQDrIEQLISEHEVEITGLTEkassARSQA-NSIQSQLEIIQEQARNQNSMyMRQLSDLESTVSQ---LRSELR 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1052 RAKRKLEGDLKLTQESIMdLENDKLQlEEKLKKKEFdiSQQNSKIEDeqalalQLQKKLkenqarieeleeeleaertar 1131
Cdd:pfam15921 335 EAKRMYEDKIEELEKQLV-LANSELT-EARTERDQF--SQESGNLDD------QLQKLL--------------------- 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1132 AKVEKLRSDLSRELEEiSERLEEAGGATSVQIEmnkkreaefqKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDN 1211
Cdd:pfam15921 384 ADLHKREKELSLEKEQ-NKRLWDRDTGNSITID----------HLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1212 LQRVKQKLEKeksefklelddVTSNMEQIIKAKANLEKVSRTLEDQaneyRTKLEEAQRSLNDFTTqqaklqtengelar 1291
Cdd:pfam15921 453 IQGKNESLEK-----------VSSLTAQLESTKEMLRKVVEELTAK----KMTLESSERTVSDLTA-------------- 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1292 QLEEKEALIsQLTRGKLSYTQQTEDLKrqLEEEGKAKNALAHaLQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVA 1371
Cdd:pfam15921 504 SLQEKERAI-EATNAEITKLRSRVDLK--LQELQHLKNEGDH-LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVG 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1372 QW----------RTKYETDAIQRTEELEEAK-LQDAEEA-VEAVNAKCSSLEKTKHRLQNeiedlmvdvERSNAAAAALD 1439
Cdd:pfam15921 580 QHgrtagamqveKAQLEKEINDRRLELQEFKiLKDKKDAkIRELEARVSDLELEKVKLVN---------AGSERLRAVKD 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1440 KKQRNfDKILAEWKqkyeesqseleSSQKEARSLSTELFKLKNAYEESLEHLET----FKRENKNLQEEISDLTEQL--- 1512
Cdd:pfam15921 651 IKQER-DQLLNEVK-----------TSRNELNSLSEDYEVLKRNFRNKSEEMETttnkLKMQLKSAQSELEQTRNTLksm 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1513 -GEGGKNVHELEKVRKQLEAEKLE---LQSA---LEEA------EASLEHEEGKILRAQL-----EFNQIKAEI------ 1568
Cdd:pfam15921 719 eGSDGHAMKVAMGMQKQITAKRGQidaLQSKiqfLEEAmtnankEKHFLKEEKNKLSQELstvatEKNKMAGELevlrsq 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1569 ERKLAEKDEEMEQAKRNHlrvvdSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRTASEAQKHLK---IAQAH 1645
Cdd:pfam15921 799 ERRLKEKVANMEVALDKA-----SLQFAECQDIIQRQEQESVRLKLQHTLDVKELQGPGYTSNSSMKPRLLQpasFTRTH 873
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1646 LKDTQLQMDDAVRANDDLKENiAIVERRNNLLQAELEELRAVVEQTE-----------------RSRKLAEQELIETSER 1708
Cdd:pfam15921 874 SNVPSSQSTASFLSHHSRKTN-ALKEDPTRDLKQLLQELRSVINEEPtvqlskaedkgrapslgALDDRVRDCIIESSLR 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1709 VQLLHSQNTSLINQKKKMESDLTQlqseveEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKD 1788
Cdd:pfam15921 953 SDICHSSSNSLQTEGSKSSETCSR------EPVLLHAGELEDPSSCFTFPSTASPSVKNSASRSFHSSPKKSPVHSLLTS 1026
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1789 L---------QHR----------LDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQ 1849
Cdd:pfam15921 1027 SaegsigsssQYRsaktihspdsVKDSQSLPIETTGKTCRKLQNRLESLQTLVEDLQLKNQAMSSMIRNQEKRIQKVKDQ 1106
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
860-1569 |
3.13e-24 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 111.27 E-value: 3.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 860 RLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLiKNKIQ-LEAKVKEMNERLEDEEEMNAEL 938
Cdd:TIGR04523 23 GYKNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNS-NNKIKiLEQQIKDLNDKLKKNKDKINKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 939 TAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATE-------NKVKNLTEEMAGLDEIIAKLTKEKKALqeahqqaldd 1011
Cdd:TIGR04523 102 NSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKknidkflTEIKKKEKELEKLNNKYNDLKKQKEEL---------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1012 lqaeEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLErakrKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQ 1091
Cdd:TIGR04523 172 ----ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK----KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1092 QNSKIEDEQALALQLQKKLKENQARIEELEEELEaertaraKVEKLRSDLSRELEEISERLEeaggatsvqiEMNKKREA 1171
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELE-------QNNKKIKELEKQLNQLKSEIS----------DLNNQKEQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1172 EFQK-MRRDLEEATLQHEATAAALRKKHaDSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKV 1250
Cdd:TIGR04523 307 DWNKeLKSELKNQEKKLEEIQNQISQNN-KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1251 SRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLtrgklsyTQQTEDLKRQLEEEGKAKNA 1330
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN-------NSEIKDLTNQDSVKELIIKN 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1331 LAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQwrtkyetdAIQRTEELEEaKLQDAEEAVEAVNAKCSSL 1410
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK--------LNEEKKELEE-KVKDLTKKISSLKEKIEKL 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1411 EKTKHRLQNEIEDLMVDVER--SNAAAAALDKKQRNFDKILAEWKQKYEesqselessqkearslstelfKLKNAYEESL 1488
Cdd:TIGR04523 530 ESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQK---------------------SLKKKQEEKQ 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1489 EHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEI 1568
Cdd:TIGR04523 589 ELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKI 668
|
.
gi 431907173 1569 E 1569
Cdd:TIGR04523 669 K 669
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1260-1925 |
6.36e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 110.80 E-value: 6.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1260 EYRTKLEEAQRSLNDftTQQ--AKLQTENGELARQLE--EKEAlisqltrgklsytQQTE---DLKRQLEEegKAKNALA 1332
Cdd:COG1196 169 KYKERKEEAERKLEA--TEEnlERLEDILGELERQLEplERQA-------------EKAEryrELKEELKE--LEAELLL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1333 HALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQwrtkyetdaIQRTEELEEAKLQDAEEAVEAVNAKCSSLEK 1412
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEE---------LRLELEELELELEEAQAEEYELLAELARLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1413 TKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLE 1492
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1493 TFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKL 1572
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1573 AEKDEEMEQAKRnhlrvvdslqtsLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLkdtqlq 1652
Cdd:COG1196 463 ELLAELLEEAAL------------LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG------ 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1653 mDDAVRANDDLKENIAIVERRNNLLQaeleelRAVVEQTERSRKLAEQELIETSERVQLLHSqntSLINQKKKMESDLTQ 1732
Cdd:COG1196 525 -AVAVLIGVEAAYEAALEAALAAALQ------NIVVEDDEVAAAAIEYLKAAKAGRATFLPL---DKIRARAALAAALAR 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1733 LQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLE 1812
Cdd:COG1196 595 GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1813 ARVRELENELEAEQKRNAESVkgmRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSkf 1892
Cdd:COG1196 675 LEAEAELEELAERLAEEELEL---EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE-- 749
|
650 660 670
....*....|....*....|....*....|...
gi 431907173 1893 rKVQHELDEAEERADIAESQVNKLRAKSRDIGA 1925
Cdd:COG1196 750 -EEALEELPEPPDLEELERELERLEREIEALGP 781
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1142-1907 |
6.66e-24 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 111.39 E-value: 6.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1142 SRELEEISE---RLEEAGGATSVQIEMNKKREAEFQKMR--RDLEEATLQHEA-TAAALRKKHADSVAELGEQIDNLQRV 1215
Cdd:PTZ00121 1087 NRADEATEEafgKAEEAKKTETGKAEEARKAEEAKKKAEdaRKAEEARKAEDArKAEEARKAEDAKRVEIARKAEDARKA 1166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1216 KQKLEKEKSefklelddvtsnmeQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKlqteNGELARQLEE 1295
Cdd:PTZ00121 1167 EEARKAEDA--------------KKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEAR----KAEDAKKAEA 1228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1296 kealisqltrgklsyTQQTEDLKRQlEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRvlsKANsEVAQWRT 1375
Cdd:PTZ00121 1229 ---------------VKKAEEAKKD-AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR---KAD-ELKKAEE 1288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1376 KYETDAIQRTEE---LEEAKlQDAEEAVEAVNAKCSSLEKTKhrlqnEIEDLMVDVERSNAAAAALDKKQRNFDKILAEW 1452
Cdd:PTZ00121 1289 KKKADEAKKAEEkkkADEAK-KKAEEAKKADEAKKKAEEAKK-----KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1453 KQKYEESQSELESSQKEARSLSTELFKLKNAyeeslEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAE 1532
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKA-----DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK 1437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1533 KlELQSALEEAEASLEHEEGKilraqlefnqiKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAEtRSRNEALRVKK 1612
Cdd:PTZ00121 1438 K-KAEEAKKADEAKKKAEEAK-----------KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE-EAKKKADEAKK 1504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1613 KMEGDLNEMEIQLSQANRTASEAQKhlkiAQAHLKDTQLQMDDAVRANDDLKEniaiverrnnllqaeLEELRavveQTE 1692
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKADEAKK----AEEAKKADEAKKAEEKKKADELKK---------------AEELK----KAE 1561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1693 RSRKlAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAitdaammaEELKKEQDTS 1772
Cdd:PTZ00121 1562 EKKK-AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA--------EELKKAEEEK 1632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1773 AHLERMKKNMEQTIKDLQHRLDEAEQIALKggKKQLQKLEARVRELENEL---EAEQKRNAESVKGMRKSERRIKELTYQ 1849
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIK--AAEEAKKAEEDKKKAEEAkkaEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 431907173 1850 TEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAE---EQANTNLSKFRKVQHELDEAEERAD 1907
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKkkaEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| SH3_NEDD9 |
cd12002 |
Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding protein family member, ... |
1929-1986 |
3.64e-23 |
|
Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding protein family member, Neural precursor cell Expressed, Developmentally Down-regulated 9; NEDD9 is also called human enhancer of filamentation 1 (HEF1) or CAS-L (Crk-associated substrate in lymphocyte). It was first described as a gene predominantly expressed in early embryonic brain, and was also isolated from a screen of human proteins that regulate filamentous budding in yeast, and as a tyrosine phosphorylated protein in lymphocytes. It promotes metastasis in different solid tumors. NEDD9 localizes in focal adhesions and associates with FAK and Abl kinase. It also interacts with SMAD3 and the proteasomal machinery which allows its rapid turnover; these interactions are not shared by other CAS proteins. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure that includes an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. The SH3 domain of CAS proteins binds to diverse partners including FAK, FRNK, Pyk2, PTP-PEST, DOCK180, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212935 Cd Length: 57 Bit Score: 94.67 E-value: 3.64e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1929 LARALYDNTAESPQELSFRRGDVLRVLQrEGAGGLDGWCLCSLHGQQGIVPANRVKLL 1986
Cdd:cd12002 1 MARALYDNVPECAEELAFRKGDILTVIE-QNTGGLEGWWLCSLHGRQGIAPGNRLKLL 57
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
919-1768 |
9.58e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 107.08 E-value: 9.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 919 AKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRdIDDLELTLAKVE-----KEKHATENKVKNLTEEMAGLDEIIAK 993
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 994 LTKEKKALQEAHQQALDDLQAEEDKVNTLTKSK-VKLEQQVDDLEGSLEQekkvrmdlerakrkLEGDLKLTQESIMDLE 1072
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqLRVKEKIGELEAEIAS--------------LERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1073 NDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERL 1152
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1153 EEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKhADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDD 1232
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK-ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1233 VTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEE----------------- 1295
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVaagnrlnnvvveddava 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1296 -------KEALISQLTRGKLSYTQQTEDLKRQLEEEG-------------KAKNALAHALQSArhdcdLLREQYEEETEA 1355
Cdd:TIGR02169 561 keaiellKRRKAGRATFLPLNKMRDERRDLSILSEDGvigfavdlvefdpKYEPAFKYVFGDT-----LVVEDIEAARRL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1356 KAELQRV------LSKANSEVAQWRTKYETDAIQRTEELEEAKLQDAEEaveavnakcsSLEKTKHRLQNEIEDLMvdvE 1429
Cdd:TIGR02169 636 MGKYRMVtlegelFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLE----------GLKRELSSLQSELRRIE---N 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1430 RSNAAAAALDKKQRNFDKILAEWkqkyeesqselessqkearslstelfklknayEESLEHLETFKRENKNLQEEISDLT 1509
Cdd:TIGR02169 703 RLDELSQELSDASRKIGEIEKEI--------------------------------EQLEQEEEKLKERLEELEEDLSSLE 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1510 EQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEF--------NQIKAEIERKLAEKDEEMEQ 1581
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKleeevsriEARLREIEQKLNRLTLEKEY 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1582 A--KRNHLRVVDSLQTSLDAETRSRNEALRVK--------KKMEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQL 1651
Cdd:TIGR02169 831 LekEIQELQEQRIDLKEQIKSIEKEIENLNGKkeeleeelEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEA 910
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1652 QMDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLaEQELIETSERVQLLHSQNTSLINQKKKMESDLT 1731
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDV-QAELQRVEEEIRALEPVNMLAIQEYEEVLKRLD 989
|
890 900 910
....*....|....*....|....*....|....*..
gi 431907173 1732 QLQSEveeavqecRNAEEKAKKAITDAAMMAEELKKE 1768
Cdd:TIGR02169 990 ELKEK--------RAKLEEERKAILERIEEYEKKKRE 1018
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
944-1817 |
3.27e-22 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 105.44 E-value: 3.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 944 KLEDECSELKRDIDDLEltlaKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQAlddlQAEEDKVNTLT 1023
Cdd:pfam02463 157 EIEEEAAGSRLKRKKKE----ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKE----KLELEEEYLLY 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1024 KSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLEN----------DKLQLEEKLKKKEFDISQQN 1093
Cdd:pfam02463 229 LDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEkekklqeeelKLLAKEEEELKSELLKLERR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1094 SKIEDEQALALQ-----LQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKK 1168
Cdd:pfam02463 309 KVDDEEKLKESEkekkkAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1169 REAEFQKMR----RDLEEATLQHEA------TAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNME 1238
Cdd:pfam02463 389 AAKLKEEELelksEEEKEAQLLLELarqledLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELK 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1239 QIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSlndfttQQAKLQTENGELARQLEEKEALISQLTRGKLSYTQQTEDLK 1318
Cdd:pfam02463 469 KSEDLLKETQLVKLQEQLELLLSRQKLEERSQK------ESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1319 RQLEEEGKAKNALAHAlqsarhDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEEleeakLQDAEE 1398
Cdd:pfam02463 543 VAISTAVIVEVSATAD------EVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL-----AQLDKA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1399 AVEAVNAKCSSLEKTKHRlqnEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSlstELF 1478
Cdd:pfam02463 612 TLEADEDDKRAKVVEGIL---KDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQ---EKA 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1479 KLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSA---LEEAEASLEHEEGKIL 1555
Cdd:pfam02463 686 ESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDeeeEEEEKSRLKKEEKEEE 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1556 RAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLqtsldaetrsRNEALRVKKKMEGDLNEMEIQLSQANRTASEA 1635
Cdd:pfam02463 766 KSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL----------RALEEELKEEAELLEEEQLLIEQEEKIKEEEL 835
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1636 QKHLKIAQAHLKDTQLQMDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQ 1715
Cdd:pfam02463 836 EELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEK 915
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1716 NTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAItdaamMAEELKKEQDTSAHLERMKKN----MEQTIKDLQH 1791
Cdd:pfam02463 916 ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK-----EEEEERNKRLLLAKEELGKVNlmaiEEFEEKEERY 990
|
890 900
....*....|....*....|....*.
gi 431907173 1792 RLDEAEQIALKGGKKQLQKLEARVRE 1817
Cdd:pfam02463 991 NKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1079-1879 |
4.58e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 105.22 E-value: 4.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1079 EEKLKKKEFDISQQNSKIEDEQALalQLQKKLKENQARIEELEEELEAERT--ARAKVEKLRSDLSRELEEiSERLEEAG 1156
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKA--EEAKKKAEDARKAEEARKAEDARKAeeARKAEDAKRVEIARKAED-ARKAEEAR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1157 GATSVQIEMNKKREAEFQKmrrdleeatlqheatAAALRKKHADSVAELGEQIDNLQRVkQKLEKEKSEFKLElddvtsN 1236
Cdd:PTZ00121 1171 KAEDAKKAEAARKAEEVRK---------------AEELRKAEDARKAEAARKAEEERKA-EEARKAEDAKKAE------A 1228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1237 MEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQrsLNDFTTQQAKLQTENGELARQLEEKEALISQLTRGKLSYTQQTED 1316
Cdd:PTZ00121 1229 VKKAEEAKKDAEEAKKAEEERNNEEIRKFEEAR--MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADE 1306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1317 LKRQLEEEGKAKNALAHAlQSARHDCDLLREQYEEeteakaelqrvlSKANSEVAQWRTKYETDAIQRTEELEEA-KLQD 1395
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKA-EEAKKKADAAKKKAEE------------AKKAAEAAKAEAEAAADEAEAAEEKAEAaEKKK 1373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1396 AEEAVEAVNAKCSSLEKTKhrlqneIEDLMVDVERSNAAAAALDKKqrnfdkilaEWKQKYEESQSELESSQKEARSLST 1475
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKK------ADEAKKKAEEDKKKADELKKA---------AAAKKKADEAKKKAEEKKKADEAKK 1438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1476 ELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKIL 1555
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA 1518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1556 RAQLEFNQI-KAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSldAETRSRNEALRVKKKMEGDLNEMEIqLSQANRTASE 1634
Cdd:PTZ00121 1519 EEAKKADEAkKAEEAKKADEAKKAEEKKKADELKKAEELKKA--EEKKKAEEAKKAEEDKNMALRKAEE-AKKAEEARIE 1595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1635 AQKHLKIAQAHLKDTQLQMDDAVRAN-DDLKENIAIVERRNNLLQAELEELRavveQTERSRKLAEQELIETSErvqllh 1713
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKaEELKKAEEEKKKVEQLKKKEAEEKK----KAEELKKAEEENKIKAAE------ 1665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1714 sqntslinQKKKMESDltqlqsevEEAVQECRNAEEKAKKAitdaammAEELKKEQDTSAHLERMKKNMEQTIKdlqhrl 1793
Cdd:PTZ00121 1666 --------EAKKAEED--------KKKAEEAKKAEEDEKKA-------AEALKKEAEEAKKAEELKKKEAEEKK------ 1716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1794 dEAEQIalkggKKQLQKLEARVRELENELEaEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKA 1873
Cdd:PTZ00121 1717 -KAEEL-----KKAEEENKIKAEEAKKEAE-EDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789
|
....*.
gi 431907173 1874 YKRQAE 1879
Cdd:PTZ00121 1790 EKRRME 1795
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
941-1667 |
5.92e-22 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 103.95 E-value: 5.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 941 KKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLD----EIIAKLTKEKKALQEahqqaLD-DLQAE 1015
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEqqikDLNDKLKKNKDKINK-----LNsDLSKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1016 EDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSK 1095
Cdd:TIGR04523 109 NSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1096 IEDEQALALQLQKKLKENQARIEeleeeleaertaraKVEKLRSDLSrELEEISERLEEAggATSVQIEMNKKrEAEFQK 1175
Cdd:TIGR04523 189 IDKIKNKLLKLELLLSNLKKKIQ--------------KNKSLESQIS-ELKKQNNQLKDN--IEKKQQEINEK-TTEISN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1176 MRRDLEEATLQHEATAAALRKKHADsVAELGEQIDNLQRVKQKLEKEKSEFKLELD-DVTSNMEQIIKakaNLEKVSRTL 1254
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQLSEKQKE-LEQNNKKIKELEKQLNQLKSEISDLNNQKEqDWNKELKSELK---NQEKKLEEI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1255 EDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLTRGKLSYTQQTEDLKRQleeegkaKNALaha 1334
Cdd:TIGR04523 327 QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ-------INDL--- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1335 lqsarhdcdllreqyeeeteakaelqrvlskansevaqwrtkyetdaiqrteeleEAKLQDAEEAVEAVNAKCSSLEKTK 1414
Cdd:TIGR04523 397 -------------------------------------------------------ESKIQNQEKLNQQKDEQIKKLQQEK 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1415 HRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETF 1494
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1495 KRENKNLQEEISDLTeqlgeggKNVHELEKVRKQLEAEKLELQSALEEAEASLEheegkilraQLEFNQIKAEIERKLAE 1574
Cdd:TIGR04523 502 NEEKKELEEKVKDLT-------KKISSLKEKIEKLESEKKEKESKISDLEDELN---------KDDFELKKENLEKEIDE 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1575 KDEEMEQAKRNhlrvvdslQTSLDAETRSRNEALRVKKKMEGDLNEmeiQLSQANRTASEAQKHLKIAQAHLKDTQLQMD 1654
Cdd:TIGR04523 566 KNKEIEELKQT--------QKSLKKKQEEKQELIDQKEKEKKDLIK---EIEEKEKKISSLEKELEKAKKENEKLSSIIK 634
|
730
....*....|...
gi 431907173 1655 DAVRANDDLKENI 1667
Cdd:TIGR04523 635 NIKSKKNKLKQEV 647
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1204-1923 |
9.49e-22 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 103.72 E-value: 9.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1204 ELGEQIDNLQRVKQKLEKEKSEFKleldDVTSNMEQIIKAKANLEKVSRT---LEDQANEYRTKLEEAQRSLNDFTtqqa 1280
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKAESELK----ELEKKHQQLCEEKNALQEQLQAeteLCAEAEEMRARLAARKQELEEIL---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1281 klqtenGELARQLEEKEALISQLTRGKLSYTQQTEDLKRQLEEEGKAKnalaHALQSARHDCDLLREQYEEETEAKAELQ 1360
Cdd:pfam01576 78 ------HELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAAR----QKLQLEKVTTEAKIKKLEEDILLLEDQN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1361 RVLSKANSEVAQWRTKYETdaiQRTEELEEAKlqdaeeaveavnakcsSLEKTKHRLQNEIEDLMVDVERSNAAAAALDK 1440
Cdd:pfam01576 148 SKLSKERKLLEERISEFTS---NLAEEEEKAK----------------SLSKLKNKHEAMISDLEERLKKEEKGRQELEK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1441 KQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVH 1520
Cdd:pfam01576 209 AKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1521 ELEKVRK----QLEAEKLELQSALEEAEASLEheegkiLRAQ--LEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQ 1594
Cdd:pfam01576 289 KAEKQRRdlgeELEALKTELEDTLDTTAAQQE------LRSKreQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1595 TSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKEniaiverRN 1674
Cdd:pfam01576 363 EQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAE-------KL 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1675 NLLQAELEELRAVVEQTE-RSRKLA------EQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNA 1747
Cdd:pfam01576 436 SKLQSELESVSSLLNEAEgKNIKLSkdvsslESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNV 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1748 EekakKAITDAAMMAEELKK--EQDTSA--HLERMKKNMEQTIKDLQHRLDEAEQIALKggkkqLQKLEARVRELENELE 1823
Cdd:pfam01576 516 E----RQLSTLQAQLSDMKKklEEDAGTleALEEGKKRLQRELEALTQQLEEKAAAYDK-----LEKTKNRLQQELDDLL 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1824 AEQKRNAESVKGMRKSERRIKELTyqtEEDKKNLLRLQDLVDKlqlkvkaykrqaeeAEEQANTNLSKFRKVQHELDEAE 1903
Cdd:pfam01576 587 VDLDHQRQLVSNLEKKQKKFDQML---AEEKAISARYAEERDR--------------AEAEAREKETRALSLARALEEAL 649
|
730 740
....*....|....*....|
gi 431907173 1904 ERADIAESQVNKLRAKSRDI 1923
Cdd:pfam01576 650 EAKEELERTNKQLRAEMEDL 669
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1143-1824 |
1.35e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.09 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1143 RELEEISERLEEAggaTSVQIEMNK-----KREAE----FQKMRRDLEEatLQHEATAAALRKKHADsVAELGEQIDNLQ 1213
Cdd:COG1196 179 RKLEATEENLERL---EDILGELERqleplERQAEkaerYRELKEELKE--LEAELLLLKLRELEAE-LEELEAELEELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1214 RVKQKLEKEksefklelddvtsnMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQL 1293
Cdd:COG1196 253 AELEELEAE--------------LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1294 EEKEALISQLTRGKLSYTQQTEDLKRQLEEEGKAKNALAHALQSArhdcdllREQYEEETEAKAELQRVLSKANSEVAQw 1373
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA-------EEALLEAEAELAEAEEELEELAEELLE- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1374 rtkyetdaIQRTEELEEAKLQDAEEAVEAvnakcssLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWK 1453
Cdd:COG1196 391 --------ALRAAAELAAQLEELEEAEEA-------LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1454 QKYEESQSELESSQKEARSLSTELFKLKNAYEEslehletfKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKqLEAEK 1533
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAE--------AAARLLLLLEAEADYEGFLEGVKAALLLAGLRG-LAGAV 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1534 LELQSALEEAEASLEHEEGkilraqlefnqikAEIERKLAEKDEEMEQAkrnhlrvvdslqtsldAETRSRNEALRVKkk 1613
Cdd:COG1196 527 AVLIGVEAAYEAALEAALA-------------AALQNIVVEDDEVAAAA----------------IEYLKAAKAGRAT-- 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1614 megdlnemEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTER 1693
Cdd:COG1196 576 --------FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLR 647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1694 SRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSA 1773
Cdd:COG1196 648 EVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 431907173 1774 HLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEA 1824
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SH3_BCAR1 |
cd12001 |
Src homology 3 domain of the CAS (Crk-Associated Substrate) scaffolding protein family member, ... |
1929-1994 |
1.56e-21 |
|
Src homology 3 domain of the CAS (Crk-Associated Substrate) scaffolding protein family member, Breast Cancer Anti-estrogen Resistance 1; BCAR1, also called p130cas or CASS1, is the founding member of the CAS family of scaffolding proteins and was originally identified through its ability to associate with Crk. The name BCAR1 was designated because the human gene was identified in a screen for genes that promote resistance to tamoxifen. It is widely expressed and its deletion is lethal in mice. It plays a role in regulating cell motility, survival, proliferation, transformation, cancer progression, and bacterial pathogenesis. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure that includes an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. The SH3 domain of CAS proteins binds to diverse partners including FAK, FRNK, Pyk2, PTP-PEST, DOCK180, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212934 Cd Length: 68 Bit Score: 90.10 E-value: 1.56e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1929 LARALYDNTAESPQELSFRRGDVLRVLQREgAGGLDGWCLCSLHGQQGIVPANRVKLLPAGPTPKP 1994
Cdd:cd12001 4 LAKALYDNVAESPDELSFRKGDIMTVLERD-TQGLDGWWLCSLHGRQGIVPGNRLKILVGMYDKKQ 68
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
221-708 |
1.67e-21 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 102.51 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 221 IIQANPALEAFGNAKTVRNDNSSRFGKF--IRIHFGATG---KLASADIETYLLEKSRVIFQL------KAERNYHIFYQ 289
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 290 ILSNKKPDLLDMLLVTNNPYD------YAFVSQGEVSVASIDDSEELMATD--------SAFDVLGFTPEEKAGVYKLTG 355
Cdd:cd14894 329 MVAGVNAFPFMRLLAKELHLDgidcsaLTYLGRSDHKLAGFVSKEDTWKKDverwqqviDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 356 AIMHYGNMKFKQKQREEQAEPDGT---EDADKSAYLMGLNSADLLKGLCHPR---VKVGNEYVTKGQSVQQVYYSIGALA 429
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 430 KAVYEKMFNWMV------TRINATLETKQPRQY-----------FIGVLDIAGFEIFDFNSFEQLCINFTNEKLqqffnh 492
Cdd:cd14894 489 RLLYQLAFNYVVfvmneaTKMSALSTDGNKHQMdsnasapeavsLLKIVDVFGFEDLTHNSLDQLCINYLSEKL------ 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 493 hmFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMT----------FKAKLYDNHlgkSN 562
Cdd:cd14894 563 --YAREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENMNaqqeekrnklFVRNIYDRN---SS 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 563 NFQKPRNVKGKQEAH---------FSLIHYAGTVDYNILGWLEKNKDPLNETV-VGLYQKSSLKL--MATLFSSYASADT 630
Cdd:cd14894 638 RLPEPPRVLSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLlVGLKTSNSSHFcrMLNESSQLGWSPN 717
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 631 ADSSKGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICR 708
Cdd:cd14894 718 TNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1085-1915 |
2.19e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 102.91 E-value: 2.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1085 KEFDISQQNSKIEDEQALalQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIE 1164
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATE--EAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRV 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1165 MNKKREAEFQKMR--RDLEEATLQHEA-TAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEfKLELDDVTSNMEQII 1241
Cdd:PTZ00121 1155 EIARKAEDARKAEeaRKAEDAKKAEAArKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKKAEAVKKAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1242 KAKANLEKVSRTLEDQANEYRTKLEEAQrsLNDFTTQQAKLQTENGELARQLEEKEALISQLTRGKLSYTQQTEDLKRQL 1321
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEAR--MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1322 EEEGKAKNALAHAlQSARHDCDLLREQYEEeteakaelqrvlSKANSEVAQWRTKYETDAIQRTEELEEA-KLQDAEEAV 1400
Cdd:PTZ00121 1312 EEAKKADEAKKKA-EEAKKKADAAKKKAEE------------AKKAAEAAKAEAEAAADEAEAAEEKAEAaEKKKEEAKK 1378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1401 EAVNAKCSSLEKTK-HRLQNEIEDLMVDVERSNAAAAAldKKQRNFDKILAEWKQKYEESQSELESSQK--EARSLSTEL 1477
Cdd:PTZ00121 1379 KADAAKKKAEEKKKaDEAKKKAEEDKKKADELKKAAAA--KKKADEAKKKAEEKKKADEAKKKAEEAKKadEAKKKAEEA 1456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1478 FKLKNAY---EESLEHLETFKR--------ENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLElqsALEEAEAS 1546
Cdd:PTZ00121 1457 KKAEEAKkkaEEAKKADEAKKKaeeakkadEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD---EAKKAEEA 1533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1547 LEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTsldAETRSRNEALRVKKKMEGDLNEMEIQLS 1626
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK---AEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1627 QANRTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKENIAIVERRNNLLQAElEELRAVVEQTERSRKLAEQELIETS 1706
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAA-EEAKKAEEDKKKAEEAKKAEEDEKK 1689
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1707 ERVQLLHSQNtslinQKKKMESDLTQLQSEVEEAvQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTI 1786
Cdd:PTZ00121 1690 AAEALKKEAE-----EAKKAEELKKKEAEEKKKA-EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK 1763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1787 KDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESV-KGMRKSERRIKELTYQTEEDKKNLLRLQDLVD 1865
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIiEGGKEGNLVINDSKEMEDSAIKEVADSKNMQL 1843
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 431907173 1866 KLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEEraDIAESQVNK 1915
Cdd:PTZ00121 1844 EEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEE--EIEEADEIE 1891
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
855-1585 |
2.91e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 102.53 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 855 KEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQ-DNLNDAEERCDQLIKNKIQLEAKVKEMNERLED--- 930
Cdd:PTZ00121 1165 KAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEakk 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 931 -EEEMNAELTAK---------KRKLEDECSELKRDIDDLEltlaKVEKEKHATENKVknlTEEMAGLDEIIAKLTKEKKA 1000
Cdd:PTZ00121 1245 aEEERNNEEIRKfeearmahfARRQAAIKAEEARKADELK----KAEEKKKADEAKK---AEEKKKADEAKKKAEEAKKA 1317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1001 ------LQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEgDLKLTQESIMDLEND 1074
Cdd:PTZ00121 1318 deakkkAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD-AAKKKAEEKKKADEA 1396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1075 KLQLEEKLKKKEfdisqQNSKIEDEQALALQLQKKLKENQarieeleeeleaertaRAKVEKLRSDLSRELEEISERLEE 1154
Cdd:PTZ00121 1397 KKKAEEDKKKAD-----ELKKAAAAKKKADEAKKKAEEKK----------------KADEAKKKAEEAKKADEAKKKAEE 1455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1155 AGGATSVQIEMNKKREAEfqKMRRDLEEATLQHEATAAALR-KKHADSVAELGEQIDNLQRVKQKLEKEKSEfKLELDDV 1233
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKAD--EAKKKAEEAKKADEAKKKAEEaKKKADEAKKAAEAKKKADEAKKAEEAKKAD-EAKKAEE 1532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1234 TSNMEQIIKA--KANLEKVSRTLEDQANEYRTKLEEAQRSLNDfttqqAKLQTENGELARQLEEKEaLISQLTRGKLSYT 1311
Cdd:PTZ00121 1533 AKKADEAKKAeeKKKADELKKAEELKKAEEKKKAEEAKKAEED-----KNMALRKAEEAKKAEEAR-IEEVMKLYEEEKK 1606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1312 QQTEDLKRqlEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQ----RTEE 1387
Cdd:PTZ00121 1607 MKAEEAKK--AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKaeeaKKAE 1684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1388 LEEAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNfDKILAEWKQKYEESQSELESSQ 1467
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE-DKKKAEEAKKDEEEKKKIAHLK 1763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1468 KEARSLSTELFKLKNAY--EESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLE-----LQSAL 1540
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKevadsKNMQL 1843
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 431907173 1541 EEAEASLEH------EEGKILRAQLEFNQikaeiERKLAEKD-EEMEQAKRN 1585
Cdd:PTZ00121 1844 EEADAFEKHkfnknnENGEDGNKEADFNK-----EKDLKEDDeEEIEEADEI 1890
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
845-1598 |
8.48e-21 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 100.82 E-value: 8.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 845 AETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEM 924
Cdd:pfam02463 275 KEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 925 NERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEA 1004
Cdd:pfam02463 355 EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1005 HQQALDDLQA--EEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQES--------------- 1067
Cdd:pfam02463 435 EEESIELKQGklTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSqkeskarsglkvlla 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1068 -IMDLENDKLQLEEKLKKKEFDISQ----QNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLS 1142
Cdd:pfam02463 515 lIKDGVGGRIISAHGRLGDLGVAVEnykvAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSI 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1143 RELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAElGEQIDNLQRVKQKLEKE 1222
Cdd:pfam02463 595 AVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEE-GLAEKSEVKASLSELTK 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1223 KSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQ---LEEKEAL 1299
Cdd:pfam02463 674 ELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQkidEEEEEEE 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1300 ISQLTRGKLSYTQQTEDLKRQLEEEGKAKNALAHALQSARHDC----DLLREQYEEETEAKAELQRVLSKANSEVAQWRT 1375
Cdd:pfam02463 754 KSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLkaqeEELRALEEELKEEAELLEEEQLLIEQEEKIKEE 833
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1376 KYETDAIQRTEELEEAKLqdAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRN-------FDKI 1448
Cdd:pfam02463 834 ELEELALELKEEQKLEKL--AEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKeleeesqKLNL 911
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1449 LAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLE-HLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRK 1527
Cdd:pfam02463 912 LEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEEnNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYN 991
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 431907173 1528 QLEAEKLELQSALEEAEASLEHEEGKILRaqlEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLD 1598
Cdd:pfam02463 992 KDELEKERLEEEKKKLIRAIIEETCQRLK---EFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSG 1059
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
834-1713 |
1.19e-20 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 100.05 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 834 LYFKIKplLKSAETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQ--DNLNDAEERCDQLI 911
Cdd:pfam02463 166 RLKRKK--KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLylDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 912 KNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEII 991
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 992 AKLTKEKKALQEahqQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDL 1071
Cdd:pfam02463 324 KKAEKELKKEKE---EIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1072 ENDKLQLEEKLKKKEfdisqqnSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISER 1151
Cdd:pfam02463 401 SEEEKEAQLLLELAR-------QLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1152 LEEAggATSVQIEMNKKREAEFQKMRRDLEEatLQHEATAAALRKKHADSVAELGEQIDNLQRVKQK-LEKEKSEFKLEL 1230
Cdd:pfam02463 474 LKET--QLVKLQEQLELLLSRQKLEERSQKE--SKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVaVENYKVAISTAV 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1231 DDVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFttqqAKLQTENGELARQLEEKEALISQLTRGKLSY 1310
Cdd:pfam02463 550 IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSI----AVLEIDPILNLAQLDKATLEADEDDKRAKVV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1311 TQQTEDLKRQLEEEGKAKNAL----AHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTE 1386
Cdd:pfam02463 626 EGILKDTELTKLKESAKAKESglrkGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1387 ELEEAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYeesqSELESS 1466
Cdd:pfam02463 706 QREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKE----LAEERE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1467 QKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEisDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEAS 1546
Cdd:pfam02463 782 KTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEE--EQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERL 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1547 LEHEEGKILRAQLEFNQIKAEIERKLAEK-DEEMEQAKRNHLRVVDSLQ--TSLDAETRSRNEALRVKKKMEGDLNEMEI 1623
Cdd:pfam02463 860 EEEITKEELLQELLLKEEELEEQKLKDELeSKEEKEKEEKKELEEESQKlnLLEEKENEIEERIKEEAEILLKYEEEPEE 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1624 QLSQANRTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKENIAIVERRNNLLQAELEELravveQTERSRKLAEQELI 1703
Cdd:pfam02463 940 LLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERL-----EEEKKKLIRAIIEE 1014
|
890
....*....|
gi 431907173 1704 ETSERVQLLH 1713
Cdd:pfam02463 1015 TCQRLKEFLE 1024
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
903-1551 |
1.19e-20 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 99.75 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 903 AEERCDQLIKNKIQ-LEAKVKEMNERLEDEEEMNAELtAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLT 981
Cdd:PRK03918 187 RTENIEELIKEKEKeLEEVLREINEISSELPELREEL-EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 982 EEMAGLDEIIAKLTKEKKALQEahqqalddLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEqekkvrmdlerakrKLEGDL 1061
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKE--------LKEKAEEYIKLSEFYEEYLDELREIEKRLS--------------RLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1062 KLTQESIMDLENDKLQLEEkLKKKEFDISQQNSKIEdEQALALQLQKKLKENQARIEELEEELEAERTARA--KVEKLRS 1139
Cdd:PRK03918 324 NGIEERIKELEEKEERLEE-LKKKLKELEKRLEELE-ERHELYEEAKAKKEELERLKKRLTGLTPEKLEKEleELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1140 DLSRELEEISER---LEEAGGATSVQIEMNKKREAEFQKMRRDLEE---ATLQHEATAAAlrKKHADSVAELGEQIDNLQ 1213
Cdd:PRK03918 402 EIEEEISKITARigeLKKEIKELKKAIEELKKAKGKCPVCGRELTEehrKELLEEYTAEL--KRIEKELKEIEEKERKLR 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1214 RVKQKLEKEKSEFKlELDDVTSNMEQIIKAKANLEKVS-RTLEDQANEYRTKLEEAqrslndfttqqAKLQTENGELARQ 1292
Cdd:PRK03918 480 KELRELEKVLKKES-ELIKLKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKL-----------IKLKGEIKSLKKE 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1293 LEEKEALISQLTrgklsytqQTEDLKRQLEEEGKaknalahalqsarhdcDLLREQYEEETEAKAELQRvlskansevaq 1372
Cdd:PRK03918 548 LEKLEELKKKLA--------ELEKKLDELEEELA----------------ELLKELEELGFESVEELEE----------- 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1373 wrtkyetdaiqRTEELEEAKlqdaEEAVEAVNAkcsslEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEW 1452
Cdd:PRK03918 593 -----------RLKELEPFY----NEYLELKDA-----EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1453 KQKYeeSQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEIsdltEQLGEGGKNVHELEKVRKQLEA- 1531
Cdd:PRK03918 653 EKKY--SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL----EEREKAKKELEKLEKALERVEEl 726
|
650 660
....*....|....*....|.
gi 431907173 1532 -EKLELQSALEEAEASLEHEE 1551
Cdd:PRK03918 727 rEKVKKYKALLKERALSKVGE 747
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1238-1935 |
1.40e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 100.14 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1238 EQIIKAKANLEKVSRTLE------DQANEYRTKLEEAQRSLNDFTTQQAKLQ-TENGELARQLEEKEALISQLTRGKLSY 1310
Cdd:TIGR02169 170 RKKEKALEELEEVEENIErldliiDEKRQQLERLRREREKAERYQALLKEKReYEGYELLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1311 TQQTEDLKRQLEEEGKAKNALAHALQSarhdcdlLREQYEEETEAKA-ELQRVLSKANSEVAQwrtkyetdaIQRTEELE 1389
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEE-------LNKKIKDLGEEEQlRVKEKIGELEAEIAS---------LERSIAEK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1390 EAKLQDAEEAVEavnakcsSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKkqrnfdkILAEWKQKYEESQSELESSQKE 1469
Cdd:TIGR02169 314 ERELEDAEERLA-------KLEAEIDKLLAEIEELEREIEEERKRRDKLTE-------EYAELKEELEDLRAELEEVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1470 ARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGeggknvhELEKVRKQLEAEKLELQSALEEAEASLEH 1549
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA-------DLNAAIAGIEAKINELEEEKEDKALEIKK 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1550 EEGKILRAQLEFNQIKAEIERKLAEKD---EEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNemeiQLS 1626
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEEYDrveKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHG----TVA 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1627 QANRTASEAQKHLKIAQAHlkdtqlQMDDAVRANDDL-KENIAIVERRN---------NLLQAELEELRA---------- 1686
Cdd:TIGR02169 529 QLGSVGERYATAIEVAAGN------RLNNVVVEDDAVaKEAIELLKRRKagratflplNKMRDERRDLSIlsedgvigfa 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1687 ----------------------VVEQTERSRKLA------------------------------------EQELIETSER 1708
Cdd:TIGR02169 603 vdlvefdpkyepafkyvfgdtlVVEDIEAARRLMgkyrmvtlegelfeksgamtggsraprggilfsrsePAELQRLRER 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1709 VQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKD 1788
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1789 LQHRLDEAEQiALKGGKKQLQKLEAR-----VRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDL 1863
Cdd:TIGR02169 763 LEARIEELEE-DLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 431907173 1864 VDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKAQLARALYD 1935
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
861-1424 |
3.50e-20 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 98.17 E-value: 3.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 861 LKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEercDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTA 940
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLK---DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 941 KKRKLEDECSELKRDID-DLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKV 1019
Cdd:TIGR04523 293 LKSEISDLNNQKEQDWNkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEI 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1020 NTLTK-------SKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQ 1092
Cdd:TIGR04523 373 EKLKKenqsykqEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1093 NSKIEDEQALALQLQKKLKEnqarieeleeeleaertarakveklrsdLSRELEEISERLEEaggaTSVQIEMNKKREAE 1172
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKV----------------------------LSRSINKIKQNLEQ----KQKELKSKEKELKK 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1173 FQKMRRDLEEatlqheataaalrkkhadSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQI--IKAKANLEKV 1250
Cdd:TIGR04523 501 LNEEKKELEE------------------KVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDdfELKKENLEKE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1251 srtlEDQANEYRTKLEEAQRSLNDFTTQQ----AKLQTENGELARQLEEKEALISQLTRGKLSYTQQTEDLKRQLEEEGK 1326
Cdd:TIGR04523 563 ----IDEKNKEIEELKQTQKSLKKKQEEKqeliDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1327 AKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQW----RTKYETDAIQRTEELEEAKLQDAEEAVEA 1402
Cdd:TIGR04523 639 KKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWlkelSLHYKKYITRMIRIKDLPKLEEKYKEIEK 718
|
570 580
....*....|....*....|..
gi 431907173 1403 VNAKcssLEKTKHRLQNEIEDL 1424
Cdd:TIGR04523 719 ELKK---LDEFSKELENIIKNF 737
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
843-1507 |
6.17e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 98.29 E-value: 6.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 843 KSAETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSllQEKNDLQLQVQAEQDnlNDAEERCDQLIKNKIQLEAKVK 922
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE--EKKKADEAKKKAEEA--KKADEAKKKAEEAKKKADAAKK 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 923 EMNERLEDEEEMNAELTAKKRKLEDecSELKRDIDDLEltlaKVEKEKHATENKVKnlTEEMAGLDEIIAKLTKEKKALQ 1002
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEA--AEEKAEAAEKK----KEEAKKKADAAKKK--AEEKKKADEAKKKAEEDKKKAD 1408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1003 EAHQQALDDLQAEEdkvntlTKSKVKLEQQVDDLEGSLEQEKKVrmdlERAKRKLEGDLKltqesimdLENDKLQLEEKL 1082
Cdd:PTZ00121 1409 ELKKAAAAKKKADE------AKKKAEEKKKADEAKKKAEEAKKA----DEAKKKAEEAKK--------AEEAKKKAEEAK 1470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1083 KKKEFdisqqnSKIEDEQALALQLQKKLKENQARIEELEEELEAERTA---RAKVEKLRSDLSRELEEiSERLEEAGGAT 1159
Cdd:PTZ00121 1471 KADEA------KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAdeaKKAEEAKKADEAKKAEE-AKKADEAKKAE 1543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1160 SVQI--EMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAElGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNM 1237
Cdd:PTZ00121 1544 EKKKadELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1238 EQIIKAKANLEKVSRTLEDQANEYRT-----KLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLTRGKLSYTQ 1312
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKKKaeelkKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1313 QTEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQyEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAK 1392
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE-AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1393 LQDAEEAVEAVNAKCSSLEK-TKHRLQNEIE-----DLMVDVERS---NAAAAALDKKQRNFDKILAEWKQKYEESQSEL 1463
Cdd:PTZ00121 1782 EEELDEEDEKRRMEVDKKIKdIFDNFANIIEggkegNLVINDSKEmedSAIKEVADSKNMQLEEADAFEKHKFNKNNENG 1861
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 431907173 1464 ESSQKEARSlSTELFKLKNAYEESLEHLETFKRENKNLQEEISD 1507
Cdd:PTZ00121 1862 EDGNKEADF-NKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPN 1904
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
859-1421 |
1.43e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 96.26 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 859 GRLKETLEK-SEAR---RKELEEKMVSLLQ--------EKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNE 926
Cdd:PRK02224 162 GKLEEYRERaSDARlgvERVLSDQRGSLDQlkaqieekEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 927 RLEDEEEMNAELTakkrkledecsELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEkKALQEAHQ 1006
Cdd:PRK02224 242 VLEEHEERREELE-----------TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAE-AGLDDADA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1007 QALDDLQAEedkvntltkskvkLEQQVDDLEGSLEQekkVRMDLERAKRKLEGdlklTQESIMDLENDKLQLEEKLKKKE 1086
Cdd:PRK02224 310 EAVEARREE-------------LEDRDEELRDRLEE---CRVAAQAHNEEAES----LREDADDLEERAEELREEAAELE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1087 FDISQQNSKIEDEQALALQLQKKLKENQARIEELEeeleaerTARAKVEKLRSDLSRELEEISERLEEaggatsvqiemn 1166
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFGDAP-------VDLGNAEDFLEELREERDELREREAE------------ 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1167 kkREAEFQKMRRDLEEAtlqhEATAAALR----------KKHADSVAELGEQIDnlqrvkqKLEKEKSEFKLELDDVTSN 1236
Cdd:PRK02224 431 --LEATLRTARERVEEA----EALLEAGKcpecgqpvegSPHVETIEEDRERVE-------ELEAELEDLEEEVEEVEER 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1237 MEQIIKAKAnLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLTRGKLSYTQQTED 1316
Cdd:PRK02224 498 LERAEDLVE-AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1317 LKRQLEEEGKAKNALAH------ALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIqrtEELEE 1390
Cdd:PRK02224 577 LNSKLAELKERIESLERirtllaAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARI---EEARE 653
|
570 580 590
....*....|....*....|....*....|.
gi 431907173 1391 AKlQDAEEAVEAVNAKCSSLEKTKHRLQNEI 1421
Cdd:PRK02224 654 DK-ERAEEYLEQVEEKLDELREERDDLQAEI 683
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
839-1387 |
1.59e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 96.29 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 839 KPLLKSAETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQlqvqAEQDNLNDAEERCDQLIKNKIQLE 918
Cdd:PRK03918 183 KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 919 AKVKEMNERLEdeeemnaELTAKKRKLED-------------ECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMA 985
Cdd:PRK03918 259 EKIRELEERIE-------ELKKEIEELEEkvkelkelkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 986 GLDEIIAKLTKEKKALQEahqqALDDLQAEEDKVNTLTKSKVKLEQ--QVDDLEGSLEQEKKVRM--DLERAKRKLEGDL 1061
Cdd:PRK03918 332 ELEEKEERLEELKKKLKE----LEKRLEELEERHELYEEAKAKKEEleRLKKRLTGLTPEKLEKEleELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1062 KLTQESIMDLENDKLQLE---EKLKKKEF-------------------DISQQNSKIEDEQALALQLQKKLKENQARIEE 1119
Cdd:PRK03918 408 SKITARIGELKKEIKELKkaiEELKKAKGkcpvcgrelteehrkelleEYTAELKRIEKELKEIEEKERKLRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1120 LEEELEAERTARAKVEKLRS-----------DLSRELEEISERLEEAGGATSVQIEMNK--KREAEFQKMRRDLEEATLQ 1186
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKEleeklkkynleELEKKAEEYEKLKEKLIKLKGEIKSLKKelEKLEELKKKLAELEKKLDE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1187 HEATAAALRKKHAD----SVAELGEQIDNLQRVKQK---LEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEdqan 1259
Cdd:PRK03918 568 LEEELAELLKELEElgfeSVEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE---- 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1260 EYRTKLEEAQRSLNDftTQQAKLQTENGELARQLEEKEALISQLTRGKLSYTQQTEDLKRQLEEEGKAKNALaHALQSAR 1339
Cdd:PRK03918 644 ELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL-EKLEKAL 720
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1340 HDCDLLREQY-----EEETEAKAELQRVLSKANSEVAQwrTKYETDAIQRTEE 1387
Cdd:PRK03918 721 ERVEELREKVkkykaLLKERALSKVGEIASEIFEELTE--GKYSGVRVKAEEN 771
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
845-1451 |
3.83e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 95.13 E-value: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 845 AETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEM 924
Cdd:TIGR02169 346 EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 925 NERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQ-- 1002
Cdd:TIGR02169 426 NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEer 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1003 -----------------------------EAHQQAL--------------DDLQAEED--------------------KV 1019
Cdd:TIGR02169 506 vrggraveevlkasiqgvhgtvaqlgsvgERYATAIevaagnrlnnvvveDDAVAKEAiellkrrkagratflplnkmRD 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1020 NTLTKSKVKLEQQVDDLEGSLEQEKKVR-------------MDLERAKR--------KLEGDL--------------KLT 1064
Cdd:TIGR02169 586 ERRDLSILSEDGVIGFAVDLVEFDPKYEpafkyvfgdtlvvEDIEAARRlmgkyrmvTLEGELfeksgamtggsrapRGG 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1065 QESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRE 1144
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1145 LEEISERLEEAggatsvqiemnkkrEAEFQKMRRDLEEatlqHEATAAALRKKHADSVAELG-EQIDNLQRVKQKLEKEK 1223
Cdd:TIGR02169 746 LSSLEQEIENV--------------KSELKELEARIEE----LEEDLHKLEEALNDLEARLShSRIPEIQAELSKLEEEV 807
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1224 SEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRslndfttQQAKLQTENGELARQLEEKEALISQL 1303
Cdd:TIGR02169 808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK-------EIENLNGKKEELEEELEELEAALRDL 880
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1304 TRGKLSYTQQTEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQwrTKYETDAIQ 1383
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE--ELSLEDVQA 958
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 431907173 1384 RTEELEEA--KLQD----AEEAVEAVNAKCSSLEKTKHRLQNEIEDL-----MVDVERSNAAAAALDKKQRNFDKILAE 1451
Cdd:TIGR02169 959 ELQRVEEEirALEPvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAIlerieEYEKKKREVFMEAFEAINENFNEIFAE 1037
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1015-1923 |
6.12e-19 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 94.73 E-value: 6.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1015 EEDKVNTLTKSKvKLEQQVDDLEG------SLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLEN--DKLQLEEKLKKKE 1086
Cdd:TIGR00606 158 QEDSNWPLSEGK-ALKQKFDEIFSatryikALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEirDQITSKEAQLESS 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1087 FDISQQNskiEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGatsvQIEMN 1166
Cdd:TIGR00606 237 REIVKSY---ENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLN----DLYHN 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1167 KKREA-EFQKMRRDLEEATLQHEATAAALRKKHADSVAELGE-----QIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQI 1240
Cdd:TIGR00606 310 HQRTVrEKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRlqlqaDRHQEHIRARDSLIQSLATRLELDGFERGPFSE 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1241 IKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALIS----QLTRGKLSYTQQTED 1316
Cdd:TIGR00606 390 RQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEkkqeELKFVIKELQQLEGS 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1317 LKRQLEEEG---KAKNALAHALQSARHDCDLLREQYEEETeaKAELQRVLSKANSEVAQwrTKYETDAIQRTEELEEAKL 1393
Cdd:TIGR00606 470 SDRILELDQelrKAERELSKAEKNSLTETLKKEVKSLQNE--KADLDRKLRKLDQEMEQ--LNHHTTTRTQMEMLTKDKM 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1394 qDAEEAVEAVNAKCSS--------------LEKTKHRLQNEI---EDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKY 1456
Cdd:TIGR00606 546 -DKDEQIRKIKSRHSDeltsllgyfpnkkqLEDWLHSKSKEInqtRDRLAKLNKELASLEQNKNHINNELESKEEQLSSY 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1457 E-------------ESQSELESSQKEARSLSTELFKLKNAYEESLEHLET------------FKREnKNLQEEISDLTEQ 1511
Cdd:TIGR00606 625 EdklfdvcgsqdeeSDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDenqsccpvcqrvFQTE-AELQEFISDLQSK 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1512 LGEGGKNVHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLA--EKDEEMEQAKRNHLRV 1589
Cdd:TIGR00606 704 LRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNdiEEQETLLGTIMPEEES 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1590 VDSLQTSLDAETRSRNEALRVKKKMEGDLNEMeiQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKENIAI 1669
Cdd:TIGR00606 784 AKVCLTDVTIMERFQMELKDVERKIAQQAAKL--QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQH 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1670 VERRNNLLQAELEELRavvEQTERSRKLAEQeLIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQEcrnAEE 1749
Cdd:TIGR00606 862 LKSKTNELKSEKLQIG---TNLQRRQQFEEQ-LVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISS---KET 934
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1750 KAKKAITDAAMMAEELKK--------EQDTSAHLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEARVRELENE 1821
Cdd:TIGR00606 935 SNKKAQDKVNDIKEKVKNihgymkdiENKIQDGKDDYLKQKETELNTVNAQLEECEK--------HQEKINEDMRLMRQD 1006
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1822 LEAE--QKRNAESVKGMRKSERRIKEL-----TYQTEEDKKNLLRLQDLVDKLQLKVKAYKR-------QAEEAEEQANT 1887
Cdd:TIGR00606 1007 IDTQkiQERWLQDNLTLRKRENELKEVeeelkQHLKEMGQMQVLQMKQEHQKLEENIDLIKRnhvlalgRQKGYEKEIKH 1086
|
970 980 990
....*....|....*....|....*....|....*.
gi 431907173 1888 NLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDI 1923
Cdd:TIGR00606 1087 FKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDI 1122
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1604-1965 |
1.47e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.08 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1604 RNEALRVKKKMEGDLN-------EMEIQLSQANRTASEAQKHLKIaQAHLKDTQLQMddAVRANDDLKENIAIVERRNNL 1676
Cdd:COG1196 174 KEEAERKLEATEENLErledilgELERQLEPLERQAEKAERYREL-KEELKELEAEL--LLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1677 LQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQntslinqkkkmesdLTQLQSEVEEAVQECRNAEEKAKKAIT 1756
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAE--------------EYELLAELARLEQDIARLEERRRELEE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1757 DAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGM 1836
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA-ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1837 RKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKL 1916
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 431907173 1917 RAKSRDIGAKAQLARALYDNTAESPQELSFRRGDVLRVLQREGAGGLDG 1965
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1335-1927 |
1.86e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 92.82 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1335 LQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQwrtkyetdAIQRTEELEEaKLQDAEEAVEAVNAKCSSLEKTK 1414
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEE--------VLREINEISS-ELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1415 hrlqNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEwKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETF 1494
Cdd:PRK03918 238 ----EEIEELEKELESLEGSKRKLEEKIRELEERIEE-LKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1495 KRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEaeklELQSALEEAEASLE-HEEGKILRAQLEfnQIKAEIE---- 1569
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK----ELEKRLEELEERHElYEEAKAKKEELE--RLKKRLTgltp 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1570 RKLAEKDEEMEQAK---RNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRTASEAQKHLKIAqahl 1646
Cdd:PRK03918 387 EKLEKELEELEKAKeeiEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELK---- 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1647 kdtqlqmddavrandDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEqelietservqllhsqntsLINQKKKM 1726
Cdd:PRK03918 463 ---------------RIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE-------------------LAEQLKEL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1727 ESDLTQLQSE-VEEAVQECRNAEEKAKKAITDAAMMAEELKKEQD---TSAHLERMKKNMEQTIKDLQHRLDEA------ 1796
Cdd:PRK03918 509 EEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELgfesve 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1797 --------------EQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQ-TEEDKKNLLRLQ 1861
Cdd:PRK03918 589 eleerlkelepfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKySEEEYEELREEY 668
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 431907173 1862 DLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERAD---IAESQVNKLRAKSRDIGAKA 1927
Cdd:PRK03918 669 LELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEkleKALERVEELREKVKKYKALL 737
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
842-1417 |
1.85e-17 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 89.79 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 842 LKSAETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNlndAEERCDQLIKNKIQLEAKV 921
Cdd:pfam15921 250 LKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ---ARNQNSMYMRQLSDLESTV 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 922 kemnerledeEEMNAELTAKKRKLEDECSELKRD--IDDLELTLAKVEKEKHATENkvKNLTEEmagLDEIIAKLTKEKK 999
Cdd:pfam15921 327 ----------SQLRSELREAKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQ---LQKLLADLHKREK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1000 ALQEAHQQ--------------------ALDDLQAEEDKVNTLTKS-----KVKLEQQVDDLEG---SLEQEKKVRMDLE 1051
Cdd:pfam15921 392 ELSLEKEQnkrlwdrdtgnsitidhlrrELDDRNMEVQRLEALLKAmksecQGQMERQMAAIQGkneSLEKVSSLTAQLE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1052 RAKRKLEGDLKLTQESIMDLENDKL---QLEEKLKKKEFDISQQNSKIEDEQA---LALQLQKKLKENQARIEELEEELE 1125
Cdd:pfam15921 472 STKEMLRKVVEELTAKKMTLESSERtvsDLTASLQEKERAIEATNAEITKLRSrvdLKLQELQHLKNEGDHLRNVQTECE 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1126 AERTARAKVEKLRSDLSRELEEISERLEEAG---GATSV-----QIEMNKKR-EAEFQKMRRDLEEATLQH-EATAAALR 1195
Cdd:pfam15921 552 ALKLQMAEKDKVIEILRQQIENMTQLVGQHGrtaGAMQVekaqlEKEINDRRlELQEFKILKDKKDAKIRElEARVSDLE 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1196 KKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDF 1275
Cdd:pfam15921 632 LEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQT 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1276 TTQQAKLQTENGE-------LARQLEEKEALISQLtRGKLSYTQQ----TEDLKRQLEEEgkaKNALAHALQSARH---- 1340
Cdd:pfam15921 712 RNTLKSMEGSDGHamkvamgMQKQITAKRGQIDAL-QSKIQFLEEamtnANKEKHFLKEE---KNKLSQELSTVATeknk 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1341 ---DCDLLREQYEEETEAKAELQRVLSKANSEVAQWRtkyetDAIQRTE-ELEEAKLQDAEEAVEAVNAKCSSLEKTKHR 1416
Cdd:pfam15921 788 magELEVLRSQERRLKEKVANMEVALDKASLQFAECQ-----DIIQRQEqESVRLKLQHTLDVKELQGPGYTSNSSMKPR 862
|
.
gi 431907173 1417 L 1417
Cdd:pfam15921 863 L 863
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
832-1577 |
3.03e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 88.88 E-value: 3.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 832 MKLYFKIKPLLKSAETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNL---------ND 902
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSellklerrkVD 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 903 AEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKH----ATENKVK 978
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKleseRLSSAAK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 979 NLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLE 1058
Cdd:pfam02463 392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1059 GDLKLTQESimdLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQ--LQKKLKENQARIEELEEELEAERTARAKVEK 1136
Cdd:pfam02463 472 DLLKETQLV---KLQEQLELLLSRQKLEERSQKESKARSGLKVLLALikDGVGGRIISAHGRLGDLGVAVENYKVAISTA 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1137 LRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVK 1216
Cdd:pfam02463 549 VIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGI 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1217 QKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAK--LQTENGELARQLE 1294
Cdd:pfam02463 629 LKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEilRRQLEIKKKEQRE 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1295 EK-------EALISQLTRGKLSYTQQTEDLKRQLEEEGKAKNALAHALQSARHDCDLLREqyEEETEAKAELQRVLSKAN 1367
Cdd:pfam02463 709 KEelkklklEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE--LSLKEKELAEEREKTEKL 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1368 SEVAQWRTKYETDAIQRTEELEEAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVER----------SNAAAAA 1437
Cdd:pfam02463 787 KVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEklaeeelerlEEEITKE 866
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1438 LDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGK 1517
Cdd:pfam02463 867 ELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEAD 946
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1518 NVHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDE 1577
Cdd:pfam02463 947 EKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKK 1006
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
839-1514 |
5.94e-17 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 87.85 E-value: 5.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 839 KPLLKSAETEKEMANM-KEEFGRLKETLEKSEARRKELE----------EKMVSLLQEkndlqLQVQAEQdnlndaeerc 907
Cdd:pfam05483 144 KDLIKENNATRHLCNLlKETCARSAEKTKKYEYEREETRqvymdlnnniEKMILAFEE-----LRVQAEN---------- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 908 dqlikNKIQLEAKVKEMNERLED-EEEMNAELTAKKRK---LEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEE 983
Cdd:pfam05483 209 -----ARLEMHFKLKEDHEKIQHlEEEYKKEINDKEKQvslLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDEN 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 984 MAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKL----EQQVDDLEGSLEQEKKVRMDLERAKRKLEG 1059
Cdd:pfam05483 284 LKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1060 DLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRS 1139
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIF 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1140 DLSRELEEISErLEEAGGATSVQIEMNKKreaEFQKMRRDLEEATLQHeataaalrkkhadsvAELGEQIDNLQRVKQKL 1219
Cdd:pfam05483 444 LLQAREKEIHD-LEIQLTAIKTSEEHYLK---EVEDLKTELEKEKLKN---------------IELTAHCDKLLLENKEL 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1220 EKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDfTTQQAKLQTENGELARQLEEKEAL 1299
Cdd:pfam05483 505 TQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQ-KGDEVKCKLDKSEENARSIEYEVL 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1300 ISQLTRGKLSytQQTEDLKRQLEEEGKAknalahaLQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYET 1379
Cdd:pfam05483 584 KKEKQMKILE--NKCNNLKKQIENKNKN-------IEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEE 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1380 DAIQRTEELEEAKLQDAEEAVEAVNAKCSSLEKTKhrLQNEIeDLMVDvERSNAAAAALDKKQRNFDKILAEWKQKYEES 1459
Cdd:pfam05483 655 IIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVK--LQKEI-DKRCQ-HKIAEMVALMEKHKHQYDKIIEERDSELGLY 730
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1460 QSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGE 1514
Cdd:pfam05483 731 KNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1210-1923 |
7.08e-17 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 87.72 E-value: 7.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1210 DNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRsLNDFTTQQAKLQTENGEL 1289
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQ-KREAQEEQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1290 ARQLEEKEALISqltrgKLSYTQQTEDLKRQLEEEGKAKNALAHALQSARhdcdllrEQYEEETEAKAELQRVLSKANSE 1369
Cdd:TIGR00618 266 RARIEELRAQEA-----VLEETQERINRARKAAPLAAHIKAVTQIEQQAQ-------RIHTELQSKMRSRAKLLMKRAAH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1370 VAQWRTKYETDAIQRTEELEEAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKIL 1449
Cdd:TIGR00618 334 VKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATID 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1450 AEwKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGgKNVHELEKVRKQL 1529
Cdd:TIGR00618 414 TR-TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK-EQIHLQETRKKAV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1530 EAEKLELQSALE-EAEASLEHEEGKIlraqlefnqIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAEtrsRNEAL 1608
Cdd:TIGR00618 492 VLARLLELQEEPcPLCGSCIHPNPAR---------QDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSE---RKQRA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1609 RVKKKMEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMddavRANDDLKENIAIVERRnnlLQAELEELRAVV 1688
Cdd:TIGR00618 560 SLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS----EAEDMLACEQHALLRK---LQPEQDLQDVRL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1689 EQTERSRKLAEQELIETSERVQLL-----HSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAitdaAMMAE 1763
Cdd:TIGR00618 633 HLQQCSQELALKLTALHALQLTLTqervrEHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQ----TLLRE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1764 ELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELEN---ELEAEQKRNAESVKGMRKSE 1840
Cdd:TIGR00618 709 LETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNnneEVTAALQTGAELSHLAAEIQ 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1841 RRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKS 1920
Cdd:TIGR00618 789 FFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQ 868
|
...
gi 431907173 1921 RDI 1923
Cdd:TIGR00618 869 AKI 871
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1260-1836 |
7.10e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.79 E-value: 7.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1260 EYRTKLEEAQRSLNDFTTQQaklQTENGELARQLEEKEA--LISQLTRGKLSYTQQTEDLKRQLEEEGKAKNALAHA--- 1334
Cdd:PRK02224 166 EYRERASDARLGVERVLSDQ---RGSLDQLKAQIEEKEEkdLHERLNGLESELAELDEEIERYEEQREQARETRDEAdev 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1335 ---LQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKLQDAEEavEAVNAKCSSLE 1411
Cdd:PRK02224 243 leeHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADA--EAVEARREELE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1412 KTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHL 1491
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1492 ETFKRENKNLQEEISDLTEQLGEggknVHELEkvrKQLEAEKLELQSALEEAEASLEH----------EEGKILRAQLEF 1561
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREERDE----LRERE---AELEATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEED 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1562 NQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAEtRSRNEALRVKKKMEGDLNEMEIQLSQANRTASEAQKHLKI 1641
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIE-RLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1642 AQAHLKDTQLQMDDAvranDDLKENIAIVERRNNLLQAELEELRAVVEQTERsRKLAEQELIETSERVQLLHSQNTSLIN 1721
Cdd:PRK02224 553 AEEKREAAAEAEEEA----EEAREEVAELNSKLAELKERIESLERIRTLLAA-IADAEDEIERLREKREALAELNDERRE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1722 QKKKMESDLTQLQSEVEEA-VQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDeaeqiA 1800
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERRE-----A 702
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 431907173 1801 LKGGKKQLQKLEARVRELEN---ELEAE-QKRNAESVKGM 1836
Cdd:PRK02224 703 LENRVEALEALYDEAEELESmygDLRAElRQRNVETLERM 742
|
|
| SH3_CASS4 |
cd12000 |
Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding protein family member 4; ... |
1929-1985 |
8.78e-17 |
|
Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding protein family member 4; CASS4, also called HEPL (HEF1-EFS-p130Cas-like), localizes to focal adhesions and plays a role in regulating FAK activity, focal adhesion integrity, and cell spreading. It is most abundant in blood cells and lung tissue, and is also found in high levels in leukemia and ovarian cell lines. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure that includes an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. The SH3 domain of CAS proteins binds to diverse partners including FAK, FRNK, Pyk2, PTP-PEST, DOCK180, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212933 Cd Length: 57 Bit Score: 76.46 E-value: 8.78e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1929 LARALYDNTAESPQELSFRRGDVLRVLQREGAGGlDGWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd12000 2 LARALYDNKADCSDELAFRRGDILTVLEQNVPGS-EGWWKCLLHGRQGLAPANRLQL 57
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1566-1925 |
2.72e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 85.89 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1566 AEIERKLAEKDEEMEQAKRNHLR---VVDSLQTSLDAETRSRNEALRV------KKKMEG-----DLNEMEIQLSQANRT 1631
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERldlIIDEKRQQLERLRREREKAERYqallkeKREYEGyellkEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1632 ASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKENI-AIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQ 1710
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1711 LLHSQNTSLINQKKKMESDL-------TQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDtsaHLERMKKNME 1783
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIeeerkrrDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE---KLEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1784 QTIKDLQHRLDEAEQIALKGG--KKQLQKLEARVRELENELEAEQKRnaesvkgMRKSERRIKELTYQTEEDKKNLLRLQ 1861
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELAdlNAAIAGIEAKINELEEEKEDKALE-------IKKQEWKLEQLAADLSKYEQELYDLK 475
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1862 DLVDKLQlkvkaykrqaeeaeeqantnlSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGA 1925
Cdd:TIGR02169 476 EEYDRVE---------------------KELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
848-1596 |
3.95e-16 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 85.48 E-value: 3.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 848 EKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQ--VQAEQDNLNDAEERCDQL----------IKNKI 915
Cdd:TIGR00606 311 QRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQadRHQEHIRARDSLIQSLATrleldgfergPFSER 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 916 QLEAKVKEMNERLEDEEEMNA----ELTAKKR-------KLEDECSELKRDIddlELTLAKVEKEKHATENKVKNLTEEM 984
Cdd:TIGR00606 391 QIKNFHTLVIERQEDEAKTAAqlcaDLQSKERlkqeqadEIRDEKKGLGRTI---ELKKEILEKKQEELKFVIKELQQLE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 985 AGLDEIIAK---LTKEKKALQEAHQQALDDLQAEEDKV-----NTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRK 1056
Cdd:TIGR00606 468 GSSDRILELdqeLRKAERELSKAEKNSLTETLKKEVKSlqnekADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDK 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1057 LEGDLKLTQESIMDLEN------DKLQLEEKLKKKEFDISQQNSKIED---EQALALQLQKKLKENQARIEELEEELEAE 1127
Cdd:TIGR00606 548 DEQIRKIKSRHSDELTSllgyfpNKKQLEDWLHSKSKEINQTRDRLAKlnkELASLEQNKNHINNELESKEEQLSSYEDK 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1128 RTARAKVEKLRSDLSR---ELEEISERLEEAGGATSVQ-----------------IEMNKKREAEFQKMRRDLEEATL-- 1185
Cdd:TIGR00606 628 LFDVCGSQDEESDLERlkeEIEKSSKQRAMLAGATAVYsqfitqltdenqsccpvCQRVFQTEAELQEFISDLQSKLRla 707
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1186 --QHEATAAALRKKHADSVAELGeQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIikaKANLEKVSRTLEdqanEYRT 1263
Cdd:TIGR00606 708 pdKLKSTESELKKKEKRRDEMLG-LAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRL---KNDIEEQETLLG----TIMP 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1264 KLEEAQRSLNDFTTQQaklqtengELARQLEEKEALISQLTRgklsyTQQTEDLKRQLEEEGKAKNALAHALQSARHDCD 1343
Cdd:TIGR00606 780 EEESAKVCLTDVTIME--------RFQMELKDVERKIAQQAA-----KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIE 846
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1344 LLREQYEEETEAKAELQRVLSKANSEVAQWRTkyetdAIQRTEELEE------AKLQDAEEAVEAVNAKCSSLEKTKHRL 1417
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLKSKTNELKSEKLQIGT-----NLQRRQQFEEqlvelsTEVQSLIREIKDAKEQDSPLETFLEKD 921
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1418 QNEIEDLMVDVERSNAAAA-ALDKKQRNFDKILAEWK--QKYEESQSELESSQKEarslsTELFKLKNAYEESLEHLETF 1494
Cdd:TIGR00606 922 QQEKEELISSKETSNKKAQdKVNDIKEKVKNIHGYMKdiENKIQDGKDDYLKQKE-----TELNTVNAQLEECEKHQEKI 996
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1495 KRENKNLQEEI-------SDLTEQLGEGGKN--VHELEKVRKQLEAEKLELQ--------SALEEAEASLEHEEGKILRA 1557
Cdd:TIGR00606 997 NEDMRLMRQDIdtqkiqeRWLQDNLTLRKREneLKEVEEELKQHLKEMGQMQvlqmkqehQKLEENIDLIKRNHVLALGR 1076
|
810 820 830
....*....|....*....|....*....|....*....
gi 431907173 1558 QLEFNQIKAEIERKLAEKdeEMEQAKRNHLRVVDSLQTS 1596
Cdd:TIGR00606 1077 QKGYEKEIKHFKKELREP--QFRDAEEKYREMMIVMRTT 1113
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1541-1932 |
4.19e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.37 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1541 EEAEASLEHEEGKILRAQLefnqIKAEIERKLAEKDEEMEQAKRnhlrvVDSLQTSLdaETRSRNEALRVKKKMEGDLNE 1620
Cdd:COG1196 175 EEAERKLEATEENLERLED----ILGELERQLEPLERQAEKAER-----YRELKEEL--KELEAELLLLKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1621 MEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDavranddlkeniaiverrnnlLQAELEELRAvveqterSRKLAEQ 1700
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEE---------------------LELELEEAQA-------EEYELLA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1701 ELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKK 1780
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1781 NMEQTIKDLQHRLDEAEQIALKgGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRL 1860
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAE-LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 431907173 1861 QDLVDKLQLKVKAYKRQAEEAEEQAntnlskfRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKAQLARA 1932
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAAL-------AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
849-1422 |
6.41e-16 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 84.30 E-value: 6.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 849 KEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEkndlqlqVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNERL 928
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE-------IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 929 EDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKekhaTENKVKNLTEEmagLDEIIAKLTKEKKALQEAHQQA 1008
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISE----LKKQNNQLKDN---IEKKQQEINEKTTEISNTQTQL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1009 LDDLQAEEDKVNTLTKSKVKLEQ---QVDDLEGSLEQEKKVRMDLEraKRKLEGDLKLTQESIMDLENDKLQLEEKLKKK 1085
Cdd:TIGR04523 256 NQLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLN--NQKEQDWNKELKSELKNQEKKLEEIQNQISQN 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1086 EFDISQQNSKIED-EQALA------LQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSREL---EEISERLEEa 1155
Cdd:TIGR04523 334 NKIISQLNEQISQlKKELTnsesenSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIqnqEKLNQQKDE- 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1156 ggatsvQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKhaDSVAELgeQIDNLQRVKQKLEKEKSEFKLElddvts 1235
Cdd:TIGR04523 413 ------QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ--DSVKEL--IIKNLDNTRESLETQLKVLSRS------ 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1236 nmeqIIKAKANLEKVSRTLEDQANEyrtkleeaqrsLNDFTTQQAKLQTENGELARQLEEKEALISQLTRGKLSYTQQTE 1315
Cdd:TIGR04523 477 ----INKIKQNLEQKQKELKSKEKE-----------LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKIS 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1316 DLKRQLEE--EGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETdAIQRTEELEEaKL 1393
Cdd:TIGR04523 542 DLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE-KEKKISSLEK-EL 619
|
570 580
....*....|....*....|....*....
gi 431907173 1394 QDAEEAVEAVNAKCSSLEKTKHRLQNEIE 1422
Cdd:TIGR04523 620 EKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
909-1854 |
2.30e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 82.79 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 909 QLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKrklEDECSELKRDIDDLELTLAKVekekHATENKVKNLTEEMAGLD 988
Cdd:TIGR00606 210 KYLKQYKEKACEIRDQITSKEAQLESSREIVKSY---ENELDPLKNRLKEIEHNLSKI----MKLDNEIKALKSRKKQME 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 989 EIIAKLTKEKKALQEAHQQALDDL-QAEEDKVNTLTKSKVKLEQQVDDL--EGSLEQEKKVRMDLERAKRKLEGDLKLTQ 1065
Cdd:TIGR00606 283 KDNSELELKMEKVFQGTDEQLNDLyHNHQRTVREKERELVDCQRELEKLnkERRLLNQEKTELLVEQGRLQLQADRHQEH 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1066 ESIMDLENDKLQLeeklkKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKveklrsdlsREL 1145
Cdd:TIGR00606 363 IRARDSLIQSLAT-----RLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ---------EQA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1146 EEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHE---ATAAALRKKHAD-SVAELGEQIDNLQRVKQKLEK 1221
Cdd:TIGR00606 429 DEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDrilELDQELRKAERElSKAEKNSLTETLKKEVKSLQN 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1222 EKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQ----------QAKLQTENGELAR 1291
Cdd:TIGR00606 509 EKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpnkkqlEDWLHSKSKEINQ 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1292 QLEEKEALISQLTRGKLSYTQQTEDLKRQLEEEGKAKNALAHALQSARHDCDL--LREQYEEETEAKAELQRVLSKANSE 1369
Cdd:TIGR00606 589 TRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLerLKEEIEKSSKQRAMLAGATAVYSQF 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1370 VAQWRTKYET-----DAIQRTEELEEAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVErsnAAAAALDKKQrn 1444
Cdd:TIGR00606 669 ITQLTDENQSccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAP---GRQSIIDLKE-- 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1445 fdKILAEWKQKyeesqselessqkeARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLT--EQLGEggknvhEL 1522
Cdd:TIGR00606 744 --KEIPELRNK--------------LQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTimERFQM------EL 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1523 EKVRKQLEAEKLELQSAleEAEASLEHEEGKILRAQLEFNQIKAEIE--RKLAEKDEEMEQakrnHLRvvdSLQTSLDAE 1600
Cdd:TIGR00606 802 KDVERKIAQQAAKLQGS--DLDRTVQQVNQEKQEKQHELDTVVSKIElnRKLIQDQQEQIQ----HLK---SKTNELKSE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1601 TRSRNEALRVKKKMEGDLNEMEIQLSQANRTASEAQKHLkiaqahlkdtqlqMDDAVRANDDLKENIAIVERR---NNLL 1677
Cdd:TIGR00606 873 KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQD-------------SPLETFLEKDQQEKEELISSKetsNKKA 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1678 QAELEELRAVVEQTERSRKLAEQELIETSERvqllhsqntslinQKKKMESDLTQLQSEVEEAVQECRNAEE--KAKKAI 1755
Cdd:TIGR00606 940 QDKVNDIKEKVKNIHGYMKDIENKIQDGKDD-------------YLKQKETELNTVNAQLEECEKHQEKINEdmRLMRQD 1006
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1756 TDAAMMAEELKKEQDTSAHLERMKKNMEQTIKdlQHrLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKG 1835
Cdd:TIGR00606 1007 IDTQKIQERWLQDNLTLRKRENELKEVEEELK--QH-LKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKE 1083
|
970
....*....|....*....
gi 431907173 1836 MRKSERRIKELTYQTEEDK 1854
Cdd:TIGR00606 1084 IKHFKKELREPQFRDAEEK 1102
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
32-76 |
3.13e-15 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 71.31 E-value: 3.13e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 431907173 32 DIRTECFVPDDKEEFVKAKIVSREGGKVTAETENGKTVTLKEDQV 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
848-1519 |
3.77e-15 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 81.94 E-value: 3.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 848 EKEMANMKEEFGRLKETLEKSEARRKELEEKMvSLLQEKNDLQLQVQ---AEQDNLNDAEERCDQLIKnKIQLEAKVKEM 924
Cdd:TIGR00618 225 EKELKHLREALQQTQQSHAYLTQKREAQEEQL-KKQQLLKQLRARIEelrAQEAVLEETQERINRARK-AAPLAAHIKAV 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 925 NERLEDEEEMNAELTAKKRKLEDE---CSELKRDIDDLElTLAKVEKEKHATENKVKNLTEEMAGLDEIiakLTKEKKAL 1001
Cdd:TIGR00618 303 TQIEQQAQRIHTELQSKMRSRAKLlmkRAAHVKQQSSIE-EQRRLLQTLHSQEIHIRDAHEVATSIREI---SCQQHTLT 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1002 QEAHQQAlDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEgdLKLTQESIMDLENDKLQLEEK 1081
Cdd:TIGR00618 379 QHIHTLQ-QQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE--LQQRYAELCAAAITCTAQCEK 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1082 LKKKEFDISQQNSKIEDEQalaLQLQKKLKENQARIeeleeeleaeRTARAKVEKLRSDLSRELEEiSERLEEAGGATSV 1161
Cdd:TIGR00618 456 LEKIHLQESAQSLKEREQQ---LQTKEQIHLQETRK----------KAVVLARLLELQEEPCPLCG-SCIHPNPARQDID 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1162 QIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQII 1241
Cdd:TIGR00618 522 NPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQ----RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQ 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1242 KAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLTRGKLSYTQQTEDLK--- 1318
Cdd:TIGR00618 598 DLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELlas 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1319 --RQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKA---ELQRVLSKANSEVAQwRTKYETDAIQRTEELEEAKL 1393
Cdd:TIGR00618 678 rqLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRefnEIENASSSLGSDLAA-REDALNQSLKELMHQARTVL 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1394 QDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSL 1473
Cdd:TIGR00618 757 KARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSR 836
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 431907173 1474 STELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGE-GGKNV 1519
Cdd:TIGR00618 837 LEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKlNGINQ 883
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1310-1901 |
5.09e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 81.70 E-value: 5.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1310 YTQQTEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQW--RTKYETDAiqrTEE 1387
Cdd:pfam15921 83 YSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQlqNTVHELEA---AKC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1388 LEEAKLQDAEEAVEAVNAKCSSLEKTKHrlqnEIEDLMVDVERSNAaaaaldkkqrnfDKILAEWKQKYEESQSELESSQ 1467
Cdd:pfam15921 160 LKEDMLEDSNTQIEQLRKMMLSHEGVLQ----EIRSILVDFEEASG------------KKIYEHDSMSTMHFRSLGSAIS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1468 KEARSLSTELFKLKNAYEESLEHLETFKRENKN-----LQE--------------EISDLTEQLGEGGKNVH----ELEK 1524
Cdd:pfam15921 224 KILRELDTEISYLKGRIFPVEDQLEALKSESQNkiellLQQhqdrieqlisehevEITGLTEKASSARSQANsiqsQLEI 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1525 VRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAK--RNHL-----RVVDSLQTSL 1597
Cdd:pfam15921 304 IQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARteRDQFsqesgNLDDQLQKLL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1598 dAETRSRNEALRVKKKMEGDLNEME----IQLSQANRTASEAQKHLKIAQAHLK----DTQLQMDDAVRANDDLKENIAI 1669
Cdd:pfam15921 384 -ADLHKREKELSLEKEQNKRLWDRDtgnsITIDHLRRELDDRNMEVQRLEALLKamksECQGQMERQMAAIQGKNESLEK 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1670 VERRNNLLQAELEELRAVVEQTErsrklAEQELIETSERVqlLHSQNTSLINQKKKME---SDLTQLQSEVEEAVQEC-- 1744
Cdd:pfam15921 463 VSSLTAQLESTKEMLRKVVEELT-----AKKMTLESSERT--VSDLTASLQEKERAIEatnAEITKLRSRVDLKLQELqh 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1745 -RNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTI------------------KDLQHRLDEAEQIALKGGK 1805
Cdd:pfam15921 536 lKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVgqhgrtagamqvekaqleKEINDRRLELQEFKILKDK 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1806 KqlqklEARVRELE---NELEAEQKRNAESVKGMRKSERRIKELTYQ-TEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEA 1881
Cdd:pfam15921 616 K-----DAKIRELEarvSDLELEKVKLVNAGSERLRAVKDIKQERDQlLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEM 690
|
650 660
....*....|....*....|
gi 431907173 1882 EEQANTNLSKFRKVQHELDE 1901
Cdd:pfam15921 691 ETTTNKLKMQLKSAQSELEQ 710
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
863-1654 |
7.42e-15 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 81.17 E-value: 7.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 863 ETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDnlnDAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAK- 941
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTL---CTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKr 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 942 -----KRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKnlteemagldeiIAKLTKEKKALQEAHQQALDDLQAEE 1016
Cdd:TIGR00618 250 eaqeeQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARK------------AAPLAAHIKAVTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1017 DKVNTLTKSKVKLEQQVDDlEGSLEQEKKVRMDLERAKRKLEgDLKLTQESIMDLENDKLQLEEKLKKkefdISQQNSKI 1096
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQ-QSSIEEQRRLLQTLHSQEIHIR-DAHEVATSIREISCQQHTLTQHIHT----LQQQKTTL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1097 EDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKlrsdlSRELEEISERLEEAGGATSVQIEmnKKREAEFQKM 1176
Cdd:TIGR00618 392 TQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKK-----QQELQQRYAELCAAAITCTAQCE--KLEKIHLQES 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1177 RRDLEEATlQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDV------TSNMEQIIKAKANLEKV 1250
Cdd:TIGR00618 465 AQSLKERE-QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdnpgplTRRMQRGEQTYAQLETS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1251 SRTLEDQANEYRtkleeaqrslndfttQQAKLQTENGELARQLEEKEALISQLTRGKLSYTQQTEDLKRqleeegkakna 1330
Cdd:TIGR00618 544 EEDVYHQLTSER---------------KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQ----------- 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1331 lahalqsarhdcDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAklqdaeeaveavnakcssl 1410
Cdd:TIGR00618 598 ------------DLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLT------------------- 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1411 ekTKHRLQneiEDLMVDVERSNAAAAALDKKQRNFDKILAEwkqkyeesqselessqKEARSLSTELFKLKnayeESLEH 1490
Cdd:TIGR00618 647 --ALHALQ---LTLTQERVREHALSIRVLPKELLASRQLAL----------------QKMQSEKEQLTYWK----EMLAQ 701
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1491 LETFKREnknlqeeisdLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIER 1570
Cdd:TIGR00618 702 CQTLLRE----------LETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1571 KLAEKDEEMEQAKRNHLRVVDSLQTSLdAETRSRNEALRVKKKMEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQ 1650
Cdd:TIGR00618 772 AALQTGAELSHLAAEIQFFNRLREEDT-HLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQ 850
|
....
gi 431907173 1651 LQMD 1654
Cdd:TIGR00618 851 LLKY 854
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1473-1919 |
8.70e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 80.45 E-value: 8.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1473 LSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEA---EASLEH 1549
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIknkLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1550 ---------EEGKILRAQL-----EFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQ------TSLDAETRSRNEALR 1609
Cdd:TIGR04523 202 llsnlkkkiQKNKSLESQIselkkQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDeqnkikKQLSEKQKELEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1610 VKKKMEGDLNEMEIQLSQANR-----TASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKENIAIVERRNNLLQAELEEL 1684
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNqkeqdWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1685 RAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEE 1764
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1765 LKKEQDTSAHLERMKKNMEQTIKDLQHRLD-------------EAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAE 1831
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinkikqnlEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1832 SVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQL-KVKAYKRQAEEAEEQANTNLSKfrkvqhELDEAEERADIAE 1910
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLeKEIDEKNKEIEELKQTQKSLKK------KQEEKQELIDQKE 595
|
....*....
gi 431907173 1911 SQVNKLRAK 1919
Cdd:TIGR04523 596 KEKKDLIKE 604
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1468-1953 |
1.18e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.96 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1468 KEARSLSTELFKLKNAYEESLEHLETFKR-ENKNLQEEISDLTE-QLGEGGKNVHELEKV---RKQLEAEKLELQSALEE 1542
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAEEAKKKAEDARKaEEARKAEDARKAEEaRKAEDAKRVEIARKAedaRKAEEARKAEDAKKAEA 1180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1543 AEASLEHEEGKILRAQLEFNQI----KAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDL 1618
Cdd:PTZ00121 1181 ARKAEEVRKAEELRKAEDARKAeaarKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEA 1260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1619 NEMEIQLSQANRTASEAQK--HLKIAQAHLKDTQLQMDDAVRANDDLKENiAIVERRNNLLQAELEELR----AVVEQTE 1692
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKadELKKAEEKKKADEAKKAEEKKKADEAKKK-AEEAKKADEAKKKAEEAKkkadAAKKKAE 1339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1693 RSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQsEVEEAVQECRNAEEKAKKAITDAAMmAEELKKEQDTS 1772
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD-AAKKKAEEKKKADEAKKKAEEDKKK-ADELKKAAAAK 1417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1773 AHLERMKKNMEQTIKdlqhrLDEAEQialkggkkqlqKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEE 1852
Cdd:PTZ00121 1418 KKADEAKKKAEEKKK-----ADEAKK-----------KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1853 DKKnllrlqdlVDKLQLKVKAYKRQAEEAE--EQANTNLSKFRKVQH-----ELDEAEERADIAESQVNKLRAKSRDIGA 1925
Cdd:PTZ00121 1482 AKK--------ADEAKKKAEEAKKKADEAKkaAEAKKKADEAKKAEEakkadEAKKAEEAKKADEAKKAEEKKKADELKK 1553
|
490 500
....*....|....*....|....*...
gi 431907173 1926 KAQLARALYDNTAESPQELSFRRGDVLR 1953
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKKAEEDKNMALR 1581
|
|
| SH3 |
smart00326 |
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ... |
1926-1984 |
1.23e-14 |
|
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.
Pssm-ID: 214620 [Multi-domain] Cd Length: 56 Bit Score: 70.26 E-value: 1.23e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1926 KAQLARALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSLH-GQQGIVPANRVK 1984
Cdd:smart00326 1 EGPQVRALYDYTAQDPDELSFKKGDIITVLEKSD----DGWWKGRLGrGKEGLFPSNYVE 56
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
833-1831 |
2.03e-14 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 80.10 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 833 KLYFKIKPLlKSAETEKEMANMKEEFGRLKETL-EKSEARRKELEEKMVSLLQeknDLQLQVQAEQDNLNDAEERCDQLI 911
Cdd:TIGR01612 707 KEYDKIQNM-ETATVELHLSNIENKKNELLDIIvEIKKHIHGEINKDLNKILE---DFKNKEKELSNKINDYAKEKDELN 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 912 KNKiqleAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRdiddlelTLAKVEKEKHATENKVKNLTEE-MAGLDEI 990
Cdd:TIGR01612 783 KYK----SKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIK-------TISIKEDEIFKIINEMKFMKDDfLNKVDKF 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 991 IAKLTKEKKALQEAHQQ---ALDDLQAE--EDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLerakRKLEGDLKL-- 1063
Cdd:TIGR01612 852 INFENNCKEKIDSEHEQfaeLTNKIKAEisDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTL----KKVDEYIKIce 927
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1064 -TQESIMDLENDKLQLEEKLKKK----------------EFDISQQNSKIEDEQALA--------------LQLQKKLKE 1112
Cdd:TIGR01612 928 nTKESIEKFHNKQNILKEILNKNidtikesnlieksykdKFDNTLIDKINELDKAFKdaslndyeaknnelIKYFNDLKA 1007
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1113 NQARIEELEEELEAERTARA------KVEKLRSDLSR-------ELEEISERLEEAGGATSVQIEMNKKREAE-----FQ 1174
Cdd:TIGR01612 1008 NLGKNKENMLYHQFDEKEKAtndieqKIEDANKNIPNieiaihtSIYNIIDEIEKEIGKNIELLNKEILEEAEinitnFN 1087
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1175 KMRRDLEEATLQHEATAAALrkKHADSVAELGEQIDNLQrvkQKLEKEKSEFKlELDDVTSNMEQIIKAKAN-LEKVSRT 1253
Cdd:TIGR01612 1088 EIKEKLKHYNFDDFGKEENI--KYADEINKIKDDIKNLD---QKIDHHIKALE-EIKKKSENYIDEIKAQINdLEDVADK 1161
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1254 LedQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLTRGK---LSYTQQTEDL-KRQLEEEGKAKN 1329
Cdd:TIGR01612 1162 A--ISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKginLSYGKNLGKLfLEKIDEEKKKSE 1239
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1330 ALAHALQSARHDCDLLREQYEE-------ETEAKAELQrVLSKANSEVAQWRTKYETDAiQRTEELEEAKLQDAEEavea 1402
Cdd:TIGR01612 1240 HMIKAMEAYIEDLDEIKEKSPEienemgiEMDIKAEME-TFNISHDDDKDHHIISKKHD-ENISDIREKSLKIIED---- 1313
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1403 vNAKCSSLEKTKHRLQNEIedlmVDVERSNAAAAALDKKQRNFDKILaewkqkyeesqselessqkearslstELFKLKN 1482
Cdd:TIGR01612 1314 -FSEESDINDIKKELQKNL----LDAQKHNSDINLYLNEIANIYNIL--------------------------KLNKIKK 1362
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1483 AYEESLEHLETFKRENKNLQEEISDlTEQLgeggknvhelekvrkqleAEKLELQSALEEAEASLEHE-EGKILRAQLE- 1560
Cdd:TIGR01612 1363 IIDEVKEYTKEIEENNKNIKDELDK-SEKL------------------IKKIKDDINLEECKSKIESTlDDKDIDECIKk 1423
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1561 FNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNeALRVKKK-----MEGDLNEMEIQLSQANRTASEA 1635
Cdd:TIGR01612 1424 IKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQH-ILKIKKDnatndHDFNINELKEHIDKSKGCKDEA 1502
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1636 QKHLK-IAQAHLKDTQLQMDDAVRAND----DLKENIAIVERRNNLLQAELEELRAVV----EQTERSRKLAEQELIETS 1706
Cdd:TIGR01612 1503 DKNAKaIEKNKELFEQYKKDVTELLNKysalAIKNKFAKTKKDSEIIIKEIKDAHKKFileaEKSEQKIKEIKKEKFRIE 1582
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1707 ERVQLLHSQNTSLINQKKKMESDLTQLQ--SEVEEAVQECRNAEEKAKKAITDAAMMAEE--LKKEQDTSAHLERMKKNM 1782
Cdd:TIGR01612 1583 DDAAKNDKSNKAAIDIQLSLENFENKFLkiSDIKKKINDCLKETESIEKKISSFSIDSQDteLKENGDNLNSLQEFLESL 1662
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*....
gi 431907173 1783 EQTIKDLQHRldeaeqialkggKKQLQKLEARVRELENELEaEQKRNAE 1831
Cdd:TIGR01612 1663 KDQKKNIEDK------------KKELDELDSEIEKIEIDVD-QHKKNYE 1698
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
837-1329 |
3.36e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.41 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 837 KIKPLLKSAETEKEMANMKEEfgrlkETLEKSEARRKELEEKmvsllqeKNDLQLQVQAEQDNlNDAEERCDQLIKNKIQ 916
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKE-----EAKKKADAAKKKAEEK-------KKADEAKKKAEEDK-KKADELKKAAAAKKKA 1420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 917 LEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRdiddLELTLAKVEKEKHATENKVKnlTEEMAGLDEIIAKLTK 996
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK----AEEAKKKAEEAKKADEAKKK--AEEAKKADEAKKKAEE 1494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 997 EKKALQEAHQQALDDLQAEEDKvntltkskvKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLEnDKL 1076
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAK---------KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE-EKK 1564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1077 QLEEKlKKKEFDISQQNSKIEdeqaLALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAg 1156
Cdd:PTZ00121 1565 KAEEA-KKAEEDKNMALRKAE----EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL- 1638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1157 gatsvqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEqidnlQRVKQKLEKEKSEFKLELDDVTSN 1236
Cdd:PTZ00121 1639 ----------KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE-----AKKAEEDEKKAAEALKKEAEEAKK 1703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1237 MEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGE------LARQLEEKEALISQLTRGKLSY 1310
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEkkkiahLKKEEEKKAEEIRKEKEAVIEE 1783
|
490
....*....|....*....
gi 431907173 1311 TQQTEDLKRQLEEEGKAKN 1329
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIKD 1802
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1351-1947 |
3.45e-14 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 78.61 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1351 EETEAKAELQRVLSKANSEVAQWRTKYETDAIQRteeleEAKLQDAEEAVEAVNAKCSSL----EKTKHRLQNEIEDLMV 1426
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQK-----ENKLQENRKIIEAQRKAIQELqfenEKVSLKLEEEIQENKD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1427 DVERSNAA----------AAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTEL--------FKLKNAYEEsL 1488
Cdd:pfam05483 146 LIKENNATrhlcnllketCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAenarlemhFKLKEDHEK-I 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1489 EHLET-FKRENKNLQEEIS--------------DLTEQLGEGGKNVHELEKVRK-------QLEAEKLELQSALEEAEAS 1546
Cdd:pfam05483 225 QHLEEeYKKEINDKEKQVSllliqitekenkmkDLTFLLEESRDKANQLEEKTKlqdenlkELIEKKDHLTKELEDIKMS 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1547 LEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQ---AKRNHLRVVdslqTSLDAETRSRNEALRV-KKKMEGDLNEME 1622
Cdd:pfam05483 305 LQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEElnkAKAAHSFVV----TEFEATTCSLEELLRTeQQRLEKNEDQLK 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1623 IQLSQANRTASEAQKHLKIAQAhlKDTQLQMDDAVRANDD--LKENIAiVERRNNLLQAELEELRAVVEQTERSRKLAEQ 1700
Cdd:pfam05483 381 IITMELQKKSSELEEMTKFKNN--KEVELEELKKILAEDEklLDEKKQ-FEKIAEELKGKEQELIFLLQAREKEIHDLEI 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1701 EL--IETSERVQLlhsqntsliNQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERM 1778
Cdd:pfam05483 458 QLtaIKTSEEHYL---------KEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQ 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1779 KKNMEQTIKDLQHR----LDEAEQIAlKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDK 1854
Cdd:pfam05483 529 EERMLKQIENLEEKemnlRDELESVR-EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1855 KNllrlqdlVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEA----EERADIAESQVNKLRAKSRDIGAKAQLA 1930
Cdd:pfam05483 608 KN-------IEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAkqkfEEIIDNYQKEIEDKKISEEKLLEEVEKA 680
|
650
....*....|....*..
gi 431907173 1931 RALYDNTAESPQELSFR 1947
Cdd:pfam05483 681 KAIADEAVKLQKEIDKR 697
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1055-1892 |
3.55e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 78.52 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1055 RKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIeeleeeleaertarakv 1134
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKI----------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1135 EKLRSDLSRELEEISERLEEaggatsvqieMNKKrEAEFQKMRRDLEEATLQHEATAAALRKKHADsVAELGEQIDNLQR 1214
Cdd:TIGR04523 99 NKLNSDLSKINSEIKNDKEQ----------KNKL-EVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1215 VKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEdqaneyrtKLEEAQRSLndfTTQQAKLQTENGELARQLE 1294
Cdd:TIGR04523 167 QKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK--------KKIQKNKSL---ESQISELKKQNNQLKDNIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1295 EKEALISQLTRGKLSYTQQTEDLKrqleeegkaknalahalqsarhdcdllreqyEEETEAKAELQrvlskansevaqwr 1374
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLNQLK-------------------------------DEQNKIKKQLS-------------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1375 tkyetdaiQRTEELEEAklqdaeeaveavNAKCSSLEKTKHRLQNEIEDLMvdversnaaaaalDKKQRNFDKILAEWKQ 1454
Cdd:TIGR04523 271 --------EKQKELEQN------------NKKIKELEKQLNQLKSEISDLN-------------NQKEQDWNKELKSELK 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1455 KyeesqselesSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVR-------K 1527
Cdd:TIGR04523 318 N----------QEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENqsykqeiK 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1528 QLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRnhlrvvdslqtsldaetrsrnea 1607
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD----------------------- 444
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1608 lrvkkkMEGDLNEMEIQLSQANRTaseaqkhlkiaqahlkdtqlqmddavraNDDLKENIAIVERRNNLLQAELEELRAV 1687
Cdd:TIGR04523 445 ------LTNQDSVKELIIKNLDNT----------------------------RESLETQLKVLSRSINKIKQNLEQKQKE 490
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1688 VEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVeeavqecRNAEEKAKKaitdaamMAEELKK 1767
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI-------SDLEDELNK-------DDFELKK 556
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1768 EQdtsahLERMKKNMEQTIKDLQHrldeaEQIALKGGKKQLQklearvrELENELEAEQKrnaESVKGMRKSERRIKELT 1847
Cdd:TIGR04523 557 EN-----LEKEIDEKNKEIEELKQ-----TQKSLKKKQEEKQ-------ELIDQKEKEKK---DLIKEIEEKEKKISSLE 616
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 431907173 1848 YQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKF 1892
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKW 661
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
846-1112 |
3.77e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 78.52 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 846 ETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMN 925
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 926 ERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEah 1005
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE-- 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1006 qqalddlqaeedKVNTLTKSKVKLEQQVDDLEgsleqEKKVRMDLERAKRKLEG----------DLKLTQESimdLENDK 1075
Cdd:TIGR04523 525 ------------KIEKLESEKKEKESKISDLE-----DELNKDDFELKKENLEKeideknkeieELKQTQKS---LKKKQ 584
|
250 260 270
....*....|....*....|....*....|....*..
gi 431907173 1076 LQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKE 1112
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1200-1867 |
6.54e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.03 E-value: 6.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1200 DSVAELGEQIDNLQRVKQKLEKEKSEFKLeLDDVTSNMEQIIKAKANLEKVsRTLEDQANEYR--TKLEEAQRSLNDFTT 1277
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIEL-LEPIRELAERYAAARERLAEL-EYLRAALRLWFaqRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1278 QQAKLQTENGELARQLEEKEALISQLTRGKL-SYTQQTEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAK 1356
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRgNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1357 AELQRVLSKANSEVAQWRTKYETDAIQRteeleEAKLQDAEEAVEAVNAKCSSLEKTKHRL------------------- 1417
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEA-----EAALRDLRRELRELEAEIASLERRKSNIparllalrdalaealglde 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1418 -------------------QNEIE--------DLMVDVERSNAAAAALDK---KQR-NFDKIlaewkqkyEESQSELESS 1466
Cdd:COG4913 458 aelpfvgelievrpeeerwRGAIErvlggfalTLLVPPEHYAAALRWVNRlhlRGRlVYERV--------RTGLPDPERP 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1467 QKEARSLSTELFKLKNAYEESLEHL-------------ETFKRENKNlqeeisdLTEQ-LGEGGKNVHelEKVRKQLEAE 1532
Cdd:COG4913 530 RLDPDSLAGKLDFKPHPFRAWLEAElgrrfdyvcvdspEELRRHPRA-------ITRAgQVKGNGTRH--EKDDRRRIRS 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1533 KLELQSaleEAEASLEHEEGKILRAQLEFNQIKAEIErKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRnealrvkk 1612
Cdd:COG4913 601 RYVLGF---DNRAKLAALEAELAELEEELAEAEERLE-ALEAELDALQERREALQRLAEYSWDEIDVASAER-------- 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1613 kmegDLNEMEIQLSQANRTASEaqkhLKIAQAHLKDTQLQMDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTE 1692
Cdd:COG4913 669 ----EIAELEAELERLDASSDD----LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1693 RSRKLAEQELIEtsERVQLLHSQNtSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKK--------------AITDA 1758
Cdd:COG4913 741 DLARLELRALLE--ERFAAALGDA-VERELRENLEERIDALRARLNRAEEELERAMRAFNRewpaetadldadleSLPEY 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1759 AMMAEELkKEQDTSAHLERMK----KNMEQTIKDLQHRLDEAEQIAlkggKKQLQKLEARVRELE-NE-----LEAEQKR 1828
Cdd:COG4913 818 LALLDRL-EEDGLPEYEERFKellnENSIEFVADLLSKLRRAIREI----KERIDPLNDSLKRIPfGPgrylrLEARPRP 892
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 431907173 1829 NAEsVKGMRKSERRIKELTYQTEED--KKNLLRLQDLVDKL 1867
Cdd:COG4913 893 DPE-VREFRQELRAVTSGASLFDEElsEARFAALKRLIERL 932
|
|
| SH3 |
cd00174 |
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ... |
1930-1981 |
9.05e-14 |
|
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.
Pssm-ID: 212690 [Multi-domain] Cd Length: 51 Bit Score: 67.49 E-value: 9.05e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSLH-GQQGIVPAN 1981
Cdd:cd00174 2 ARALYDYEAQDDDELSFKKGDIITVLEKDD----DGWWEGELNgGREGLFPAN 50
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
848-1766 |
9.98e-14 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 77.39 E-value: 9.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 848 EKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQ--------EKNDLQLQ-------------VQAEQDNLNDAEER 906
Cdd:TIGR00606 230 EAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKldneikalKSRKKQMEkdnselelkmekvFQGTDEQLNDLYHN 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 907 CDQLIKNKIQLEAKVKEMNERLEDEEEmnaELTAKKRKLEDE------------CSELKRDIDDLELTL-AKVEKEKHA- 972
Cdd:TIGR00606 310 HQRTVREKERELVDCQRELEKLNKERR---LLNQEKTELLVEqgrlqlqadrhqEHIRARDSLIQSLATrLELDGFERGp 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 973 -TENKVKN----LTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKV-NTLTKSKVKLEQQVDDLE------GSL 1040
Cdd:TIGR00606 387 fSERQIKNfhtlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLgRTIELKKEILEKKQEELKfvikelQQL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1041 EQEKKVRMDLERAKRKLEGDLKLTQES---------IMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLK 1111
Cdd:TIGR00606 467 EGSSDRILELDQELRKAERELSKAEKNsltetlkkeVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMD 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1112 ENQaRIEELEEELEAERTARA-------KVEKLRSDLSRELEEISERLEEaggatsVQIEMNKKREAEFQkMRRDLEEAT 1184
Cdd:TIGR00606 547 KDE-QIRKIKSRHSDELTSLLgyfpnkkQLEDWLHSKSKEINQTRDRLAK------LNKELASLEQNKNH-INNELESKE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1185 LQheatAAALRKKHADSVAELGEQIDnLQRVKQKLEKEK-------------SEFKLELDDVTSN----MEQIIKAKANL 1247
Cdd:TIGR00606 619 EQ----LSSYEDKLFDVCGSQDEESD-LERLKEEIEKSSkqramlagatavySQFITQLTDENQSccpvCQRVFQTEAEL 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1248 EKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLTRGKLSYTQQTEDLKRQLEEEGKA 1327
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETL 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1328 KNALAHALQSARhDCDL---LREQYEEETEakaELQRvlskansEVAQWRTKYETDAIQRTEELEEAKLQDAEEAVEAVN 1404
Cdd:TIGR00606 774 LGTIMPEEESAK-VCLTdvtIMERFQMELK---DVER-------KIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVV 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1405 AKCSSLEKTKHRLQNEIEDLmvdversnaaaaaldkkqrnfdkilaewkqkyeesqselessqkeaRSLSTELFKLKNAY 1484
Cdd:TIGR00606 843 SKIELNRKLIQDQQEQIQHL----------------------------------------------KSKTNELKSEKLQI 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1485 EESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSAleeaeaslEHEEGKIlrAQLEFNQI 1564
Cdd:TIGR00606 877 GTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISS--------KETSNKK--AQDKVNDI 946
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1565 KAEIERKLAEKDeemeqakrnhlrvvdslqtslDAETRSRNEALRVKKKMEGDLNEMEIQLsqanrtaSEAQKHLKIAQA 1644
Cdd:TIGR00606 947 KEKVKNIHGYMK---------------------DIENKIQDGKDDYLKQKETELNTVNAQL-------EECEKHQEKINE 998
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1645 HLKDTQLQMDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKK 1724
Cdd:TIGR00606 999 DMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQK 1078
|
970 980 990 1000
....*....|....*....|....*....|....*....|..
gi 431907173 1725 KMESDLTQLQSEVEEavQECRNAEEKAKKAITDAAMMAEELK 1766
Cdd:TIGR00606 1079 GYEKEIKHFKKELRE--PQFRDAEEKYREMMIVMRTTELVNK 1118
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1128-1802 |
1.35e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.03 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1128 RTARAKVEKLRSDLSRElEEISERLEEAGGA-TSVQIEMNKKREaEFQKMRRDLEEAtlqheataaalrKKHADSVAELG 1206
Cdd:PRK03918 172 KEIKRRIERLEKFIKRT-ENIEELIKEKEKElEEVLREINEISS-ELPELREELEKL------------EKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1207 EQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEdQANEYRTKLEEAQRSLNDFTTQQAKLQTEN 1286
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1287 GELARQLEEKEALISQLTRGKlsytQQTEDLKRQLEEEGKAKNALAHALqsarhdcdllrEQYEEETEAKAELQRVLSKa 1366
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKE----ERLEELKKKLKELEKRLEELEERH-----------ELYEEAKAKKEELERLKKR- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1367 nsevaqwRTKYETDAIQRT-EELEEAKLQdAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRnf 1445
Cdd:PRK03918 381 -------LTGLTPEKLEKElEELEKAKEE-IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHR-- 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1446 dkilAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKReNKNLQEEISDLTEQLGegGKNVHELEKv 1525
Cdd:PRK03918 451 ----KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK-LKELAEQLKELEEKLK--KYNLEELEK- 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1526 rKQLEAEKLELQSALEEAEASLEHEEGKILRaqlEFNQIKAEIERKLAEKDEEMEqakrnhlrvvdslqtslDAETRSRN 1605
Cdd:PRK03918 523 -KAEEYEKLKEKLIKLKGEIKSLKKELEKLE---ELKKKLAELEKKLDELEEELA-----------------ELLKELEE 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1606 EALRVKKKMEGDLNEMEIQLSQANRtASEAQKHLKIAQAHLKDTQLQMDDAvranddlKENIAIVERRNNLLQAELEELR 1685
Cdd:PRK03918 582 LGFESVEELEERLKELEPFYNEYLE-LKDAEKELEREEKELKKLEEELDKA-------FEELAETEKRLEELRKELEELE 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1686 AVVEQTERSRKlaEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAvqecrnaeEKAKKaitdaammaeEL 1765
Cdd:PRK03918 654 KKYSEEEYEEL--REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER--------EKAKK----------EL 713
|
650 660 670
....*....|....*....|....*....|....*..
gi 431907173 1766 KKeqdtsahLERMKKNMEQTIKDLQHRLDEAEQIALK 1802
Cdd:PRK03918 714 EK-------LEKALERVEELREKVKKYKALLKERALS 743
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1526-1915 |
1.65e-13 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 76.87 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1526 RKQLEAEKLELQSALEEAEASLEheegKILRAQLEFNQIKaeieRKLAEKDEEMEQAKRNhlrvVDSLQTSLDAETRSRN 1605
Cdd:PRK11281 51 QKLLEAEDKLVQQDLEQTLALLD----KIDRQKEETEQLK----QQLAQAPAKLRQAQAE----LEALKDDNDEETRETL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1606 EALRVKK------KMEGDLNEMEIQLSQAN------RTASE-AQKHLKIAQahlkdTQLQMDDAVRANDDLKENIAIVER 1672
Cdd:PRK11281 119 STLSLRQlesrlaQTLDQLQNAQNDLAEYNsqlvslQTQPErAQAALYANS-----QRLQQIRNLLKGGKVGGKALRPSQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1673 RnNLLQAELEELRAvveQTERSRKLAE-----QELI-----ETSERVQLLHSQNTSL---INQKKKMESdltqlqsevEE 1739
Cdd:PRK11281 194 R-VLLQAEQALLNA---QNDLQRKSLEgntqlQDLLqkqrdYLTARIQRLEHQLQLLqeaINSKRLTLS---------EK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1740 AVQECRNAEEKAKkaITDAAMMAEELKKEQDTSAHL----ERMKKNMEQTIKdLQHRLDEA--------EQI-ALKGG-- 1804
Cdd:PRK11281 261 TVQEAQSQDEAAR--IQANPLVAQELEINLQLSQRLlkatEKLNTLTQQNLR-VKNWLDRLtqsernikEQIsVLKGSll 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1805 -----KKQLQKLEArvreleneleaeqkrnAESVKGMRKserRIKEL-TYQTE--EDKKNLLRLQDLVDKLQlkvkayKR 1876
Cdd:PRK11281 338 lsrilYQQQQALPS----------------ADLIEGLAD---RIADLrLEQFEinQQRDALFQPDAYIDKLE------AG 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 431907173 1877 QAEEAEEQANTNLskfrkvqheLDEAEERADIAEsQVNK 1915
Cdd:PRK11281 393 HKSEVTDEVRDAL---------LQLLDERRELLD-QLNK 421
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1483-1920 |
2.40e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 76.23 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1483 AYEESLEHLETfkrenknLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEfn 1562
Cdd:PRK02224 245 EHEERREELET-------LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEAR-- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1563 qiKAEIERKLAEKDEEMEQAK---RNHLRVVDSLQTSLDaETRSRNEALRVK-KKMEGDLNEMEIQLSQANRTASEAQKH 1638
Cdd:PRK02224 316 --REELEDRDEELRDRLEECRvaaQAHNEEAESLREDAD-DLEERAEELREEaAELESELEEAREAVEDRREEIEELEEE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1639 LKIAQAHLKDTQLQMDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSR---KLAE--QElIETSERVQLLH 1713
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLeagKCPEcgQP-VEGSPHVETIE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1714 SQNtsliNQKKKMESDLTQLQSEVEEAvqecrnaEEKAKKAitdaammaEELKKEQDTSAHLERMKKNMEQTIKDLQHRL 1793
Cdd:PRK02224 472 EDR----ERVEELEAELEDLEEEVEEV-------EERLERA--------EDLVEAEDRIERLEERREDLEELIAERRETI 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1794 DEAEQialkggkkQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKL------ 1867
Cdd:PRK02224 533 EEKRE--------RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLaaiada 604
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1868 --QLKVKAYKRQA-EEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKS 1920
Cdd:PRK02224 605 edEIERLREKREAlAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEE 660
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
849-1276 |
2.61e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 75.57 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 849 KEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQD--NLNDAEERCDQLIKNKIQLEAKVKEMNE 926
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 927 RLEDEEEMNAELTAKKRKLEDEC-----------SELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT 995
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLeqlslateeelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 996 KEKKaLQEAHQQAL------------DDLQAEEDKV---------------NTLTKSKVKLEQQVDDLEGSLEQEKKVRM 1048
Cdd:COG4717 241 LEER-LKEARLLLLiaaallallglgGSLLSLILTIagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1049 DLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEfdisqqnskiedEQALALQLQKKLKENQARIEELEEELEAER 1128
Cdd:COG4717 320 ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE------------ELEEELQLEELEQEIAALLAEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1129 TARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKR--EAEFQKMRRDLEEATLQHEataaALRKKHADSVAELG 1206
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELE----ELREELAELEAELE 463
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1207 --EQIDNLQRVKQKLEKEKSEFKLELDDVTSNMeqiiKAKANLEKVSRTLEDqanEYRTK-LEEAQRSLNDFT 1276
Cdd:COG4717 464 qlEEDGELAELLQELEELKAELRELAEEWAALK----LALELLEEAREEYRE---ERLPPvLERASEYFSRLT 529
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1475-1905 |
3.74e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.49 E-value: 3.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1475 TELFKLKNAYEESLEHLETFKRENKNLQEEIS---DLTEQLGEGGKN-------VHELEKVRKQLEAEKLELQSALEEAE 1544
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKrteNIEELIKEKEKEleevlreINEISSELPELREELEKLEKEVKELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1545 ------ASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNhLRVVDSLQTslDAETRSRNEALRVKKKMEgdL 1618
Cdd:PRK03918 235 elkeeiEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-VKELKELKE--KAEEYIKLSEFYEEYLDE--L 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1619 NEMEIQLSQANRTASEAQKHLKiaqahlkdtqlQMDDAVRANDDLKENIAIVERRNNLLQA---ELEELRAVVEQTERSR 1695
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIK-----------ELEEKEERLEELKKKLKELEKRLEELEErheLYEEAKAKKEELERLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1696 K-LAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAvqecRNAEEKAKKAITDAAMMAEELKKEqdtsaH 1774
Cdd:PRK03918 379 KrLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL----KKAIEELKKAKGKCPVCGRELTEE-----H 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1775 LERMKKNMEQTIKDLQHRLDEAEqialkggkKQLQKLEARVRELENELEAEQK--RNAESVKGMRKSERRIKELTYQT-E 1851
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELKEIE--------EKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEElE 521
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1852 EDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANtnlsKFRKVQHELDEAEER 1905
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK----KLAELEKKLDELEEE 571
|
|
| FAT-like_CASS4_C |
cd11568 |
C-terminal FAT-like Four helix bundle domain, also called DUF3513, of CAS (Crk-Associated ... |
2350-2464 |
4.58e-13 |
|
C-terminal FAT-like Four helix bundle domain, also called DUF3513, of CAS (Crk-Associated Substrate) scaffolding protein family member 4; a protein interaction module; CASS4, also called HEPL (HEF1-EFS-p130Cas-like), localizes to focal adhesions and plays a role in regulating FAK activity, focal adhesion integrity, and cell spreading. It is most abundant in blood cells and lung tissue, and is also found in high levels in leukemia and ovarian cell lines. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure containing protein interaction modules that enable their scaffolding function, including an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain, which binds to the C-terminal domain of NSPs (novel SH2-containing proteins) to form multidomain signaling modules that mediate cell migration and invasion.
Pssm-ID: 211409 Cd Length: 123 Bit Score: 67.95 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2350 QCQSHYSALQAAVEALTSSTRANQPPRLFVPHSKRVVVAAHRLVfvgDTLSRLAASTPLRAQVGAAGTALGQALRATVLA 2429
Cdd:cd11568 11 HCRLYFGALQKAISVFHSSLSSNQPPEVFISHSKLIIMVGQKLV---DTLCQEAKEREARNEILAGSSQLCALLKNLALA 87
|
90 100 110
....*....|....*....|....*....|....*
gi 431907173 2430 VKAAALGYPSSPATEEMAQCVAELAGRALQFTNLL 2464
Cdd:cd11568 88 TKNAALQYPSPAALRELQDIADELAKHTQQFRAML 122
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
833-1677 |
8.64e-13 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 74.70 E-value: 8.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 833 KLYFKIKPLLKSAETEKEMANMKEEFGRLKET-LEK--SEARRKELEEKMVSLLQEKNDLQLQVQAEQDNL--------- 900
Cdd:TIGR01612 946 ILNKNIDTIKESNLIEKSYKDKFDNTLIDKINeLDKafKDASLNDYEAKNNELIKYFNDLKANLGKNKENMlyhqfdeke 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 901 ---NDAEERCDQLIKN----KIQLEAKVKEMNERLEDEEEMNAELTAKK--RKLEDECSELKRDIDDLEL----TLAKVE 967
Cdd:TIGR01612 1026 katNDIEQKIEDANKNipniEIAIHTSIYNIIDEIEKEIGKNIELLNKEilEEAEINITNFNEIKEKLKHynfdDFGKEE 1105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 968 KEKHATE-NKVKNlteEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVkleqQVDDLEGSLEQEKKV 1046
Cdd:TIGR01612 1106 NIKYADEiNKIKD---DIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAI----SNDDPEEIEKKIENI 1178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1047 RMDLERAKRKLEGDLKLTQEsIMDLENDKLQLEEkLKKKEFDISQQNSKIEDEQalaLQLQKKLKENQARieeleeelea 1126
Cdd:TIGR01612 1179 VTKIDKKKNIYDEIKKLLNE-IAEIEKDKTSLEE-VKGINLSYGKNLGKLFLEK---IDEEKKKSEHMIK---------- 1243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1127 ertaraKVEKLRSDLSrELEEISERLEEAGGatsvqIEMNKKREAEFQKMRRDLEE----ATLQHEATAAALRKKHADSV 1202
Cdd:TIGR01612 1244 ------AMEAYIEDLD-EIKEKSPEIENEMG-----IEMDIKAEMETFNISHDDDKdhhiISKKHDENISDIREKSLKII 1311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1203 AELGEQID------NLQRVKQKLEKEKSEFKLELDDVTsNMEQIIKakanLEKVSRTLeDQANEYRTKLEEAQRSLNDFT 1276
Cdd:TIGR01612 1312 EDFSEESDindikkELQKNLLDAQKHNSDINLYLNEIA-NIYNILK----LNKIKKII-DEVKEYTKEIEENNKNIKDEL 1385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1277 TQQAKL----------QTENGELARQLEEKE--ALISQLTRGK---LSYTQQTEDLKRQLEEEGK-----------AKNA 1330
Cdd:TIGR01612 1386 DKSEKLikkikddinlEECKSKIESTLDDKDidECIKKIKELKnhiLSEESNIDTYFKNADENNEnvlllfkniemADNK 1465
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1331 LAHALQSAR------HDCDL--LREQYEEETEAKAELQR----------VLSKANSEVAQWRTKYETDAIQ----RTEEL 1388
Cdd:TIGR01612 1466 SQHILKIKKdnatndHDFNIneLKEHIDKSKGCKDEADKnakaieknkeLFEQYKKDVTELLNKYSALAIKnkfaKTKKD 1545
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1389 EEAKLQDAEEAVEAVNAKCSSLEKTKHRLQNE---IEDLMVDVERSNAAAAALDKKQRNFDkilaewkqkyeesqseles 1465
Cdd:TIGR01612 1546 SEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEkfrIEDDAAKNDKSNKAAIDIQLSLENFE------------------- 1606
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1466 sqkearslsTELFKLKNAYEESLEHLetfkRENKNLQEEISDLT-----EQLGEGGKNVHELEKVRKQLEAEKlelqSAL 1540
Cdd:TIGR01612 1607 ---------NKFLKISDIKKKINDCL----KETESIEKKISSFSidsqdTELKENGDNLNSLQEFLESLKDQK----KNI 1669
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1541 EEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHL------------RVVDSLQTSlDAETRSRNEAL 1608
Cdd:TIGR01612 1670 EDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEIesikelieptieNLISSFNTN-DLEGIDPNEKL 1748
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 431907173 1609 RVKKKMEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQlqmddaVRANDDLKENIAIVERRNNLL 1677
Cdd:TIGR01612 1749 EEYNTEIGDIYEEFIELYNIIAGCLETVSKEPITYDEIKNTR------INAQNEFLKIIEIEKKSKSYL 1811
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
942-1570 |
9.60e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.18 E-value: 9.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 942 KRKLEDECSELKRDIDDLELTLAKVEKEKHATE--NKVKNLTEEMAGLDEIIAKLTKEKKALQ-EAHQQALDDLQAEEDK 1018
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1019 vntLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDlkltqeSIMDLENDKLQLEEKLKKKEfdisqQNSKIED 1098
Cdd:COG4913 300 ---LRAELARLEAELERLEARLDALREELDELEAQIRGNGGD------RLEQLEREIERLERELEERE-----RRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1099 EQALALQLQ-----KKLKENQARIEELEEELEAER----TARAKVEKLRSDLSRELEEISERLEEaggatsvqIEMNKKR 1169
Cdd:COG4913 366 ALLAALGLPlpasaEEFAALRAEAAALLEALEEELealeEALAEAEAALRDLRRELRELEAEIAS--------LERRKSN 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1170 -EAEFQKMRRDLEEATLQHEA-------------------TAA--ALR---------KKHADSVAELGEQID-----NLQ 1213
Cdd:COG4913 438 iPARLLALRDALAEALGLDEAelpfvgelievrpeeerwrGAIerVLGgfaltllvpPEHYAAALRWVNRLHlrgrlVYE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1214 RVKQKLEKEKSEF--------KLELDD--VTSNMEQIIKAKANLEKVsRTLEDQANEYR-------TKLEEAQRSLND-- 1274
Cdd:COG4913 518 RVRTGLPDPERPRldpdslagKLDFKPhpFRAWLEAELGRRFDYVCV-DSPEELRRHPRaitragqVKGNGTRHEKDDrr 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1275 FTTQQAKLQTENgelARQLEEKEALISQLTRGKLSYTQQTEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQyEEETE 1354
Cdd:COG4913 597 RIRSRYVLGFDN---RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE-REIAE 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1355 AKAELQRvLSKANSEVAQwrtkyetdaIQRTEELEEAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVErsnaA 1434
Cdd:COG4913 673 LEAELER-LDASSDDLAA---------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE----A 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1435 AAALDKKQRNFDkiLAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKnlqeeisDLTEQLGE 1514
Cdd:COG4913 739 AEDLARLELRAL--LEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWP-------AETADLDA 809
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 431907173 1515 GGKNVHELEKVRKQLEAEKL-ELQSALEEAEASLEHEEGKILRAQL--EFNQIKAEIER 1570
Cdd:COG4913 810 DLESLPEYLALLDRLEEDGLpEYEERFKELLNENSIEFVADLLSKLrrAIREIKERIDP 868
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
845-1302 |
9.65e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.92 E-value: 9.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 845 AETEKEMANMKEEFGRLKETL---------------------EKSEARRKELEEKMVSLLQEKNDLQLQVQA-------E 896
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLeeleeerddllaeaglddadaEAVEARREELEDRDEELRDRLEECRVAAQAhneeaesL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 897 QDNLNDAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENK 976
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 977 VKNLTEEMAGLDEIIAkltkEKKALQEAHQ-----QALDDlqaeEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLE 1051
Cdd:PRK02224 428 EAELEATLRTARERVE----EAEALLEAGKcpecgQPVEG----SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1052 RAKrklegDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTAR 1131
Cdd:PRK02224 500 RAE-----DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1132 AKVEKLRSDLSRE---LEEISERLEEAGGATSVQIEMNKKRE--AEFQKMRRDleeatlqheaTAAALRKKHADSVAEL- 1205
Cdd:PRK02224 575 AELNSKLAELKERiesLERIRTLLAAIADAEDEIERLREKREalAELNDERRE----------RLAEKRERKRELEAEFd 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1206 GEQIDNLQRVKQKLEKeksefklELDDVTSNMEQIIKAKANLEK----VSRTLEDQAN--EYRTKLEEAQRSLNDFTTQQ 1279
Cdd:PRK02224 645 EARIEEAREDKERAEE-------YLEQVEEKLDELREERDDLQAeigaVENELEELEElrERREALENRVEALEALYDEA 717
|
490 500
....*....|....*....|....*...
gi 431907173 1280 AKLQTENGEL-----ARQLEEKEALISQ 1302
Cdd:PRK02224 718 EELESMYGDLraelrQRNVETLERMLNE 745
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1987-2231 |
1.05e-12 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 74.05 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1987 PAGPTPKPSLSQ-VPPAEPGsPYPAPEHSNEDQEVYVVPPPARPcltseSPAGPCLPSPDPiykvprgsGTQPATPGDAL 2065
Cdd:PHA03307 108 PPGPSSPDPPPPtPPPASPP-PSPAPDLSEMLRPVGSPGPPPAA-----SPPAAGASPAAV--------ASDAASSRQAA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2066 EVYDVPPAALRVSASGPYDTPASFSHLLARVAPQPPGEDEAPYDVPLAPKPPSELE---------------PDLEWeGGR 2130
Cdd:PHA03307 174 LPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAAddagasssdssssesSGCGW-GPE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2131 EPGPPLYAAPSNLKRASALLNLYEAPEELLADGEEGGSDEGIYDVPL----LGPETPPSPEPLGALASNDPDTLALLLAR 2206
Cdd:PHA03307 253 NECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSpsspGSGPAPSSPRASSSSSSSRESSSSSTSSS 332
|
250 260
....*....|....*....|....*
gi 431907173 2207 SPPPSHRPRLPSAeSLSRRPLPALP 2231
Cdd:PHA03307 333 SESSRGAAVSPGP-SPSRSPSPSRP 356
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
843-1423 |
1.06e-12 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 74.06 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 843 KSAETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVK 922
Cdd:pfam01576 455 KNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 923 EMNERLEDEEE----MNAELTAKKRKLEDECSE----------LKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLD 988
Cdd:pfam01576 535 EDAGTLEALEEgkkrLQRELEALTQQLEEKAAAydklektknrLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEK 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 989 EIIAKLT------------KEKKALQEAHqqALDDLQaeeDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRK 1056
Cdd:pfam01576 615 AISARYAeerdraeaeareKETRALSLAR--ALEEAL---EAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRA 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1057 LEGDLKLTQESIMDLEnDKLQLEEKLKKKeFDISQQNSKIEDEQALAL----------QLQKKLKENQARIeeleeelEA 1126
Cdd:pfam01576 690 LEQQVEEMKTQLEELE-DELQATEDAKLR-LEVNMQALKAQFERDLQArdeqgeekrrQLVKQVRELEAEL-------ED 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1127 ERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHE---ATAAALRKKHADSVA 1203
Cdd:pfam01576 761 ERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDeilAQSKESEKKLKNLEA 840
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1204 E---LGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNmeqiikaKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQA 1280
Cdd:pfam01576 841 EllqLQEDLAASERARRQAQQERDELADEIASGASG-------KSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLR 913
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1281 KLQTENGELARQLEEKEALISQLTRGKLSYTQQTEDLKRQL-EEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAEL 1359
Cdd:pfam01576 914 KSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLqEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAA 993
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1360 QRVLSKANSEVAQWRTKYETD---AIQRTEELEEA---------KLQDAEEAVEAVNAkcsslekTKHRLQNEIED 1423
Cdd:pfam01576 994 NKLVRRTEKKLKEVLLQVEDErrhADQYKDQAEKGnsrmkqlkrQLEEAEEEASRANA-------ARRKLQRELDD 1062
|
|
| SH3_PEX13_eumet |
cd11864 |
Src Homology 3 domain of eumetazoan Peroxisomal biogenesis factor 13; PEX13 is a peroxin and ... |
1929-1985 |
1.27e-12 |
|
Src Homology 3 domain of eumetazoan Peroxisomal biogenesis factor 13; PEX13 is a peroxin and is required for protein import into the peroxisomal matrix and membrane. It is an integral membrane protein that is essential for the localization of PEX14 and the import of proteins containing the peroxisome matrix targeting signals, PTS1 and PTS2. Mutations of the PEX13 gene in humans lead to a wide range of peroxisome biogenesis disorders (PBDs), the most severe of which is known as Zellweger syndrome (ZS), a severe multisystem disorder characterized by hypotonia, psychomotor retardation, and neuronal migration defects. PEX13 contains two transmembrane regions and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212798 Cd Length: 58 Bit Score: 64.57 E-value: 1.27e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1929 LARALYDNTAESPQELSFRRGDVLRVLQREGAGGLDGWCLCSLHGQQ-GIVPANRVKL 1985
Cdd:cd11864 1 VARAEYDFVAESEDELSFRAGDKLRLAPKELQPRVRGWLLATVDGQKiGLVPANYVKI 58
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1217-1710 |
1.92e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.88 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1217 QKLEKEKSE-FKLELDDVTSNMEQIIKAKANLekvsRTLEDQANEYRTKLEEaqrsLNDFTTQQAKLQTENGELARQLEE 1295
Cdd:COG4717 49 ERLEKEADElFKPQGRKPELNLKELKELEEEL----KEAEEKEEEYAELQEE----LEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1296 KEALISQLtrgklSYTQQTEDLKRQLEEEGKAKNALahalqsarhdcdllREQYEEETEAKAELQRvlskANSEVAQWRT 1375
Cdd:COG4717 121 LEKLLQLL-----PLYQELEALEAELAELPERLEEL--------------EERLEELRELEEELEE----LEAELAELQE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1376 KyETDAIQRTEELEEAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDK-------- 1447
Cdd:COG4717 178 E-LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaa 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1448 ----ILAEWKQKYEESQSELESSQKEARSLS---TELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLG-EGGKNV 1519
Cdd:COG4717 257 allaLLGLGGSLLSLILTIAGVLFLVLGLLAllfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1520 HELEKVRKQLEaEKLELQSALEEAEASLEHEEGKILRAQLeFNQIKAEIERKLAEKDEEMEQAkRNHLRVVDSLQTSLDA 1599
Cdd:COG4717 337 EELLELLDRIE-ELQELLREAEELEEELQLEELEQEIAAL-LAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEE 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1600 ETRSRNEALRvkkkmEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMddavranDDLKENIAIVErrnnlLQA 1679
Cdd:COG4717 414 LLGELEELLE-----ALDEEELEEELEELEEELEELEEELEELREELAELEAEL-------EQLEEDGELAE-----LLQ 476
|
490 500 510
....*....|....*....|....*....|....
gi 431907173 1680 ELEELRAVVEQTER---SRKLAEQELIETSERVQ 1710
Cdd:COG4717 477 ELEELKAELRELAEewaALKLALELLEEAREEYR 510
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
843-1421 |
2.09e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.15 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 843 KSAETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEErcdqliknkiqleakvk 922
Cdd:PRK02224 231 QARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEE----------------- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 923 EMNERLEDEEEMNAELTAkkrkLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEiiakltkEKKALQ 1002
Cdd:PRK02224 294 ERDDLLAEAGLDDADAEA----VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE-------RAEELR 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1003 EAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEqekkvrmDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKL 1082
Cdd:PRK02224 363 EEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG-------DAPVDLGNAEDFLEELREERDELREREAELEATL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1083 KKKEFDIsqqnskiedEQALALQLQKKLKENQARIEELE--EELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATS 1160
Cdd:PRK02224 436 RTARERV---------EEAEALLEAGKCPECGQPVEGSPhvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1161 VQIEMNKKREAefqkmRRDLEEATLQHEATAAALRkkhadsvaelgEQIDNLQRVKQKLEKEKSEFKlelddvtsnmEQI 1240
Cdd:PRK02224 507 AEDRIERLEER-----REDLEELIAERRETIEEKR-----------ERAEELRERAAELEAEAEEKR----------EAA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1241 IKAKANLEKVSRTLEDqANEYRTKLEEAQRSLNDFTTQQAKLqTENGELARQLEEKEALISQLTRGKLSYTQQTEDLKRQ 1320
Cdd:PRK02224 561 AEAEEEAEEAREEVAE-LNSKLAELKERIESLERIRTLLAAI-ADAEDEIERLREKREALAELNDERRERLAEKRERKRE 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1321 LEEE--GKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEvaqwrtkyetdaIQRTEELEE--AKLQDA 1396
Cdd:PRK02224 639 LEAEfdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENE------------LEELEELRErrEALENR 706
|
570 580
....*....|....*....|....*
gi 431907173 1397 EEAVEAVNAKCSSLEKTKHRLQNEI 1421
Cdd:PRK02224 707 VEALEALYDEAEELESMYGDLRAEL 731
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1469-1948 |
2.29e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.03 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1469 EARSLSTELFKLKNAYEESLEhletfKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEasLE 1548
Cdd:COG4913 226 AADALVEHFDDLERAHEALED-----AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE--LE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1549 HEEGKILRAQLEFNQIKAEIERkLAEKDEEMEQAKRNH-LRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQ 1627
Cdd:COG4913 299 ELRAELARLEAELERLEARLDA-LREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1628 A----NRTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKEN-------IAIVERRNNLLQAELEELRAVVEqteRSRK 1696
Cdd:COG4913 378 SaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRElreleaeIASLERRKSNIPARLLALRDALA---EALG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1697 LAEQ------ELIETS----------ERVqlLHSQNTSL-------------INQKK----------------------- 1724
Cdd:COG4913 455 LDEAelpfvgELIEVRpeeerwrgaiERV--LGGFALTLlvppehyaaalrwVNRLHlrgrlvyervrtglpdperprld 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1725 ------KMESDLTQLQSEVEEAVQE------CRNAEE--KAKKAITDAAMMAEELKK-EQDTSAHLER---MKKNMEQTI 1786
Cdd:COG4913 533 pdslagKLDFKPHPFRAWLEAELGRrfdyvcVDSPEElrRHPRAITRAGQVKGNGTRhEKDDRRRIRSryvLGFDNRAKL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1787 KDLQHRLDEAEQiALKGGKKQLQKLEARVRELENELEAEQK--RNAESVKGMRKSERRIKELtyqtEEDKKNLLRLQDLV 1864
Cdd:COG4913 613 AALEAELAELEE-ELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAEL----EAELERLDASSDDL 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1865 DKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNklRAKSRDIGAKAQLARALYDNTAESPQEL 1944
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE--AAEDLARLELRALLEERFAAALGDAVER 765
|
....
gi 431907173 1945 SFRR 1948
Cdd:COG4913 766 ELRE 769
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1050-1749 |
2.42e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 72.83 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1050 LERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQ----ALALQLQKKLKENQARIEELeeele 1125
Cdd:pfam05483 76 LSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQfeneKVSLKLEEEIQENKDLIKEN----- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1126 aeRTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREaefqKMRRDLEEATLQHEATAAALRKKhadsvaeL 1205
Cdd:pfam05483 151 --NATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIE----KMILAFEELRVQAENARLEMHFK-------L 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1206 GEQIDNLQRVKQKLEKEKSEfklELDDVTSNMEQIIKAKANLEKVSRTLEdqanEYRTKLEEAQrslndfttQQAKLQTE 1285
Cdd:pfam05483 218 KEDHEKIQHLEEEYKKEIND---KEKQVSLLLIQITEKENKMKDLTFLLE----ESRDKANQLE--------EKTKLQDE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1286 NgeLARQLEEKEALISQLtrgklsytqqtEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAkaelqrvLSK 1365
Cdd:pfam05483 283 N--LKELIEKKDHLTKEL-----------EDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEE-------LNK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1366 ANSEVAQWRTKYETDAIQRTEEL--EEAKLQDAEEAVEAV----NAKCSSLEKTKhRLQNEIEDLMVDVERSNAAAAALD 1439
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLrtEQQRLEKNEDQLKIItmelQKKSSELEEMT-KFKNNKEVELEELKKILAEDEKLL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1440 KKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKR---------------------EN 1498
Cdd:pfam05483 422 DEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTelekeklknieltahcdklllEN 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1499 KNLQEEISDLTEQLGEGGKNV----HELEKVRKQ---LEAEKLELQSALEEAEASL--EHEEGKILRAQLEFNQIKAEIE 1569
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIinckKQEERMLKQienLEEKEMNLRDELESVREEFiqKGDEVKCKLDKSEENARSIEYE 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1570 RKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEG-DLNEMEIQLSQAN-RTASEAQKHLKIAQAHLK 1647
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENkQLNAYEIKVNKLElELASAKQKFEEIIDNYQK 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1648 DTQLQ-------MDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQ---------TERSRKLA-----EQEliETS 1706
Cdd:pfam05483 662 EIEDKkiseeklLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKhkhqydkiiEERDSELGlyknkEQE--QSS 739
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 431907173 1707 ERVQLlhsqNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEE 1749
Cdd:pfam05483 740 AKAAL----EIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1477-1930 |
2.65e-12 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 72.19 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1477 LFKLKNAYEEsLEHLETFKRE--NKNLQEEISDLtEQL---GEGGKNVHELEKVRKQLEAEKL-ELQSALEEAEASLEhe 1550
Cdd:pfam06160 2 LLLRKKIYKE-IDELEERKNElmNLPVQEELSKV-KKLnltGETQEKFEEWRKKWDDIVTKSLpDIEELLFEAEELND-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1551 EGKILRAQLEFNqikaEIERKLAEKDEEMEQakrnhlrVVDSLQTSLDAETRSRNEALRVKKK----------------- 1613
Cdd:pfam06160 78 KYRFKKAKKALD----EIEELLDDIEEDIKQ-------ILEELDELLESEEKNREEVEELKDKyrelrktllanrfsygp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1614 ----MEGDLNEMEIQLSQA-NRTAS----EAQKHLKIAQAHLKDTQLQMDDavranddlkenI-AIVERRNNLLQAELEE 1683
Cdd:pfam06160 147 aideLEKQLAEIEEEFSQFeELTESgdylEAREVLEKLEEETDALEELMED-----------IpPLYEELKTELPDQLEE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1684 LRAVVEQTERSR-KLAEQELIETSERVQLLHSQNTSLINQK--KKMESDLTQLQSEVEEaVQECRNAEEKAKKaitdaam 1760
Cdd:pfam06160 216 LKEGYREMEEEGyALEHLNVDKEIQQLEEQLEENLALLENLelDEAEEALEEIEERIDQ-LYDLLEKEVDAKK------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1761 maeELKKEQDT-SAHLERMKKNMEQTIKDLQH-----RLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVK 1834
Cdd:pfam06160 288 ---YVEKNLPEiEDYLEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1835 GMRKSERRIKELTYQTEEDKKNL-------LRLQDLVDKLQLKVKAYKRQAE----------------EAEEQANTNLSK 1891
Cdd:pfam06160 365 ELEEILEQLEEIEEEQEEFKESLqslrkdeLEAREKLDEFKLELREIKRLVEksnlpglpesyldyffDVSDEIEDLADE 444
|
490 500 510
....*....|....*....|....*....|....*....
gi 431907173 1892 FRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKAQLA 1930
Cdd:pfam06160 445 LNEVPLNMDEVNRLLDEAQDDVDTLYEKTEELIDNATLA 483
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
837-1286 |
3.53e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.48 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 837 KIKPLLKSAETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQ 916
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 917 LEAKVKEMNERLEDEEEMNAEltaKKRKLEDEcselkrdiddleltLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTK 996
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAE---ELKKAEEE--------------KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 997 EKKALQEAHQQALDDLQAEEDkvntltksKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKL 1076
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEED--------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1077 QLEEKLKKKEfdisqqNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEI---SERLE 1153
Cdd:PTZ00121 1738 EAEEDKKKAE------EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIfdnFANII 1811
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1154 EAGGATSVQIEMNKKRE-------AEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEF 1226
Cdd:PTZ00121 1812 EGGKEGNLVINDSKEMEdsaikevADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIE 1891
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 431907173 1227 KLELDDVTS---------NMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTEN 1286
Cdd:PTZ00121 1892 KIDKDDIEReipnnnmagKNNDIIDDKLDKDEYIKRDAEETREEIIKISKKDMCINDFSSKFCDYMKDN 1960
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
809-1901 |
6.01e-12 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 72.01 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 809 RRDALLVIQWNIRAfmgvknwpwmKLYFKIKPLLKSAET-----EKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLL 883
Cdd:TIGR01612 523 KNIIGFDIDQNIKA----------KLYKEIEAGLKESYElaknwKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEID 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 884 QEK---NDLQLQVQAEQDNLNDAEErcdqLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDEC-----SELKR- 954
Cdd:TIGR01612 593 DEIiyiNKLKLELKEKIKNISDKNE----YIKKAIDLKKIIENNNAYIDELAKISPYQVPEHLKNKDKIystikSELSKi 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 955 ---DIDDLELTLAKVEKEkhateNKVKNlTEEMAGLDEIIAKLTKEKKALQEAHQQALD-DLQAEEDKVNTLTKSKVKLE 1030
Cdd:TIGR01612 669 yedDIDALYNELSSIVKE-----NAIDN-TEDKAKLDDLKSKIDKEYDKIQNMETATVElHLSNIENKKNELLDIIVEIK 742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1031 QQV-----DDLEGSLE----QEKKVRMDL-ERAKRKLEGDLKLTQES-IMDLENDKLQLE---EKLKKKEFDISQQNSKI 1096
Cdd:TIGR01612 743 KHIhgeinKDLNKILEdfknKEKELSNKInDYAKEKDELNKYKSKISeIKNHYNDQINIDnikDEDAKQNYDKSKEYIKT 822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1097 ----EDEQALALQLQKKLKEN-----QARIEELEEELEAERTARAKVEKLRSDLSREL--EEISERLEEAGGATSVQIEM 1165
Cdd:TIGR01612 823 isikEDEIFKIINEMKFMKDDflnkvDKFINFENNCKEKIDSEHEQFAELTNKIKAEIsdDKLNDYEKKFNDSKSLINEI 902
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1166 NKKREAEFQKMRrdleeaTLQHEATAAALRKKHADSVAELgeqidnlqRVKQKLEKEKSEFKLeldDVTSNMEQIIKAKA 1245
Cdd:TIGR01612 903 NKSIEEEYQNIN------TLKKVDEYIKICENTKESIEKF--------HNKQNILKEILNKNI---DTIKESNLIEKSYK 965
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1246 NleKVSRTLEDQANEYRTKLEEAqrSLNDFttqqaklQTENGELarqleekealisqltrgklsyTQQTEDLKRQLeeeG 1325
Cdd:TIGR01612 966 D--KFDNTLIDKINELDKAFKDA--SLNDY-------EAKNNEL---------------------IKYFNDLKANL---G 1010
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1326 KAKNalahalqsarhdcDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKLQDAE----EAVE 1401
Cdd:TIGR01612 1011 KNKE-------------NMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIEllnkEILE 1077
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1402 AVNAKCSSLEKTKHRLqneiedlmvdversnaaaaaldkKQRNFDKILAEWKQKYEesqselessqKEARSLSTELFKLK 1481
Cdd:TIGR01612 1078 EAEINITNFNEIKEKL-----------------------KHYNFDDFGKEENIKYA----------DEINKIKDDIKNLD 1124
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1482 NAYEESLEHLETFKRENKNLQEEISdlteqlgeggKNVHELEKVrkqleAEKLELQSALEEAEASLEHEEGKILRAQL-- 1559
Cdd:TIGR01612 1125 QKIDHHIKALEEIKKKSENYIDEIK----------AQINDLEDV-----ADKAISNDDPEEIEKKIENIVTKIDKKKNiy 1189
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1560 -EFNQIKAEIERklAEKDE-EMEQAKRNHLRVVDSLQT----SLDAEtrsrnealrvKKKMEGDLNEMEIQLSQANRTAS 1633
Cdd:TIGR01612 1190 dEIKKLLNEIAE--IEKDKtSLEEVKGINLSYGKNLGKlfleKIDEE----------KKKSEHMIKAMEAYIEDLDEIKE 1257
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1634 EAQKhLKIAQAHLKDTQLQMDDAVRANDDLKENIAIVERRN-NLLQAELEELRAVVEQTERS-----RKLAEQELIETSE 1707
Cdd:TIGR01612 1258 KSPE-IENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDeNISDIREKSLKIIEDFSEESdindiKKELQKNLLDAQK 1336
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1708 R---VQLLHSQNTSLINQKKkmesdLTQLQSEVEEaVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQ 1784
Cdd:TIGR01612 1337 HnsdINLYLNEIANIYNILK-----LNKIKKIIDE-VKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIES 1410
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1785 TIKDlqhrldeaeqialkggkKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTE----------EDK 1854
Cdd:TIGR01612 1411 TLDD-----------------KDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEmadnksqhilKIK 1473
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1855 K---------NLLRLQDLVDklqlKVKAYKRQAEEAEEQANTNLSKFRKVQHELDE 1901
Cdd:TIGR01612 1474 KdnatndhdfNINELKEHID----KSKGCKDEADKNAKAIEKNKELFEQYKKDVTE 1525
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
869-1211 |
7.86e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.10 E-value: 7.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 869 EARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLiknkiqleAKVKEMNERLEDEEEmnaeltakkrkLEDE 948
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL--------QRLAEYSWDEIDVAS-----------AERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 949 CSELKRDIDDLELT---LAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKS 1025
Cdd:COG4913 670 IAELEAELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1026 KvkLEQQVDDLEGSlEQEKKVRMDLERAKRKLEGDLKLTQESIMDLendklqLEEKLKKKEFDISQQNSKIEDEQALALQ 1105
Cdd:COG4913 750 L--LEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELERA------MRAFNREWPAETADLDADLESLPEYLAL 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1106 LQK----KLKENQARIEELEEeleaeRTARAKVEKLRSDLSRELEEISERLEEA---------GGATSVQIEMNKKREAE 1172
Cdd:COG4913 821 LDRleedGLPEYEERFKELLN-----ENSIEFVADLLSKLRRAIREIKERIDPLndslkripfGPGRYLRLEARPRPDPE 895
|
330 340 350
....*....|....*....|....*....|....*....
gi 431907173 1173 FQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDN 1211
Cdd:COG4913 896 VREFRQELRAVTSGASLFDEELSEARFAALKRLIERLRS 934
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
873-1867 |
8.13e-12 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 71.62 E-value: 8.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 873 KELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNK--IQLEAKVKEMNERLEDEEEMNAELtakkRKLEDECS 950
Cdd:TIGR01612 1125 QKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDdpEEIEKKIENIVTKIDKKKNIYDEI----KKLLNEIA 1200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 951 ELKRDIDDLE---------------LTLAKVEKEKHATENKVKNLTEEMAGLDEIiakltKEKKALQEAHQQALDDLQAE 1015
Cdd:TIGR01612 1201 EIEKDKTSLEevkginlsygknlgkLFLEKIDEEKKKSEHMIKAMEAYIEDLDEI-----KEKSPEIENEMGIEMDIKAE 1275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1016 EDKVNT--------LTKSKVKLEQQVDDLEGSLE--QEKKVRMDLERAKRKLEGDLKLTQE----------------SIM 1069
Cdd:TIGR01612 1276 METFNIshdddkdhHIISKKHDENISDIREKSLKiiEDFSEESDINDIKKELQKNLLDAQKhnsdinlylneianiyNIL 1355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1070 DLENDKlQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENqarieeleeelEAERTARAKVEKL--RSDLSRELEE 1147
Cdd:TIGR01612 1356 KLNKIK-KIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDD-----------INLEECKSKIESTldDKDIDECIKK 1423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1148 ISER-----LEEAGGATSVQ---------------IEMNKKREAEFQKMRRDleEATLQHEATAAALrKKHADSVAELGE 1207
Cdd:TIGR01612 1424 IKELknhilSEESNIDTYFKnadennenvlllfknIEMADNKSQHILKIKKD--NATNDHDFNINEL-KEHIDKSKGCKD 1500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1208 QIDnlqRVKQKLEKEKSEFKLELDDVTSNMEQ---------IIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQ 1278
Cdd:TIGR01612 1501 EAD---KNAKAIEKNKELFEQYKKDVTELLNKysalaiknkFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKE 1577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1279 QAKLQTENGELARQ-------------LEEKEALISQLTRGKLSYTQQTEDLKRQ------------LEEEGKAKNALAH 1333
Cdd:TIGR01612 1578 KFRIEDDAAKNDKSnkaaidiqlslenFENKFLKISDIKKKINDCLKETESIEKKissfsidsqdteLKENGDNLNSLQE 1657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1334 ALQSarhdcdlLREQYEEETEAKAELQRVLSKANS---EVAQWRTKYETDAIQRTEELEEAKLQDaeeaveavnakcssL 1410
Cdd:TIGR01612 1658 FLES-------LKDQKKNIEDKKKELDELDSEIEKieiDVDQHKKNYEIGIIEKIKEIAIANKEE--------------I 1716
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1411 EKTKHRLQNEIEDLMV-----DVERSNaAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYE 1485
Cdd:TIGR01612 1717 ESIKELIEPTIENLISsfntnDLEGID-PNEKLEEYNTEIGDIYEEFIELYNIIAGCLETVSKEPITYDEIKNTRINAQN 1795
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1486 ESLEHLETFKRENKNLQEeisdlteqlgeggKNVHELEKVRKQleaekleLQSALEEAEASLEHEEGKILRAqleFNQIK 1565
Cdd:TIGR01612 1796 EFLKIIEIEKKSKSYLDD-------------IEAKEFDRIINH-------FKKKLDHVNDKFTKEYSKINEG---FDDIS 1852
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1566 AEIERKLAEKDEE-----MEQAKRNHLRVVDSLQTSLdaetrsRNEALRVKKKMEGDLNEMEIqlsqanrtaseaqkhlk 1640
Cdd:TIGR01612 1853 KSIENVKNSTDENllfdiLNKTKDAYAGIIGKKYYSY------KDEAEKIFINISKLANSINI----------------- 1909
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1641 iaqahlkdtQLQMDDAVRANDDLkeNIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQ--ELIETSERVQLLH---SQ 1715
Cdd:TIGR01612 1910 ---------QIQNNSGIDLFDNI--NIAILSSLDSEKEDTLKFIPSPEKEPEIYTKIRDSydTLLDIFKKSQDLHkkeQD 1978
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1716 NTSLINQKKKMESDLTQlQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKK----EQDTSAHLERMKKNMEQTIKDLQH 1791
Cdd:TIGR01612 1979 TLNIIFENQQLYEKIQA-SNELKDTLSDLKYKKEKILNDVKLLLHKFDELNKlscdSQNYDTILELSKQDKIKEKIDNYE 2057
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1792 RldEAEQIAL----KGGKKQLQKLEARVRELENELEAEQKRN---AESVKGMRKSERRIKELT--YQTE----EDKknLL 1858
Cdd:TIGR01612 2058 K--EKEKFGIdfdvKAMEEKFDNDIKDIEKFENNYKHSEKDNhdfSEEKDNIIQSKKKLKELTeaFNTEikiiEDK--II 2133
|
....*....
gi 431907173 1859 RLQDLVDKL 1867
Cdd:TIGR01612 2134 EKNDLIDKL 2142
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
916-1296 |
8.19e-12 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 70.31 E-value: 8.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 916 QLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT 995
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 996 KEKKAL---QEAHQQALDDLqaeEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLE 1072
Cdd:pfam07888 115 EEKDALlaqRAAHEARIREL---EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1073 NDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSreleeiserl 1152
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELS---------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1153 eEAGGATSvqiemnkKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDD 1232
Cdd:pfam07888 262 -SMAAQRD-------RTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEER 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1233 VTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGEL---ARQLEEK 1296
Cdd:pfam07888 334 LQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELleyIRQLEQR 400
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1442-1930 |
1.71e-11 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 69.48 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1442 QRNFDKI---LAEWKQKYeesqselessqkEARSLSTELFKLKNAY--EESLEHLETFKRENknlqEEISDlteqlgegg 1516
Cdd:PRK04778 24 RKRNYKRideLEERKQEL------------ENLPVNDELEKVKKLNltGQSEEKFEEWRQKW----DEIVT--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1517 knvHELEKVRKQL-EAEKL-------ELQSALEEAEASLEHEEGKILRAQLEFNQIKaEIERKLaekDEEMEQAKRNHlr 1588
Cdd:PRK04778 79 ---NSLPDIEEQLfEAEELndkfrfrKAKHEINEIESLLDLIEEDIEQILEELQELL-ESEEKN---REEVEQLKDLY-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1589 vvDSLQTSLDAETRSRNEALrvkKKMEGDLNEMEIQLSQANRTAS-----EAQKHLKIAQAHLKDTQLQMDDavranddl 1663
Cdd:PRK04778 150 --RELRKSLLANRFSFGPAL---DELEKQLENLEEEFSQFVELTEsgdyvEAREILDQLEEELAALEQIMEE-------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1664 kenI-AIVERRNNLLQAELEELRAVVEQ-TERSRKLAEQELIETSERVQLLHSQNTSLINQK--KKMESDLTQLQSEVEE 1739
Cdd:PRK04778 217 ---IpELLKELQTELPDQLQELKAGYRElVEEGYHLDHLDIEKEIQDLKEQIDENLALLEELdlDEAEEKNEEIQERIDQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1740 --AVQEcrnAEEKAKKaitdaammaeELKKEQDT-SAHLERMKKNMEQTIKDLQH-----RLDEAEQIALKGGKKQLQKL 1811
Cdd:PRK04778 294 lyDILE---REVKARK----------YVEKNSDTlPDFLEHAKEQNKELKEEIDRvkqsyTLNESELESVRQLEKQLESL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1812 EARVRELE------------------------NELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRlqdLVDKL 1867
Cdd:PRK04778 361 EKQYDEITeriaeqeiayselqeeleeilkqlEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKR---YLEKS 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 431907173 1868 QL-----KVKAYKRQAEEAEEQANTNLSKFR----KVQHELDEAEEradiaesQVNKLRAKSRDIGAKAQLA 1930
Cdd:PRK04778 438 NLpglpeDYLEMFFEVSDEIEALAEELEEKPinmeAVNRLLEEATE-------DVETLEEETEELVENATLT 502
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1480-1939 |
1.96e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.41 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1480 LKNAYEESLEHLETFK-RENKNLQEEISDLTEQLGEGGKNV---HELEKVRKQLEAEKLELQSALEEAEASLEHEEgkIL 1555
Cdd:COG4717 47 LLERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLE--KL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1556 RAQLEFNQIKAEIERKLAEKDEEMEQAKRnHLRVVDSLQTSLDAETRSRNEALR-VKKKMEGDLNEMEIQLSQANRTASE 1634
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEE-RLEELRELEEELEELEAELAELQEeLEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1635 AQKHLKIAQAHLKDTQLQMDDAVRANDDLKENIAIVERRNNLLQAE----LEELRAVVEQTERSRKLAEQELIE-TSERV 1709
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARllllIAAALLALLGLGGSLLSLILTIAGvLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1710 QLLHSQNTSLINQKKKMESDLTQLQseveeAVQECRNAEEKAKKAITDAAMMAEELKKEqdtsaHLERMKKNMEQTIKDL 1789
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQ-----ALPALEELEEEELEELLAALGLPPDLSPE-----ELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1790 QHRLDEAEQIALKGGKKQLQKLEARV-----RELENELEAEQKRNAEsvkgmrksERRIKELTYQTEEDKKNLLRLQDLV 1864
Cdd:COG4717 354 REAEELEEELQLEELEQEIAALLAEAgvedeEELRAALEQAEEYQEL--------KEELEELEEQLEELLGELEELLEAL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1865 DKLQLKVKA--YKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIA------ESQVNKLRAKSRDIgAKAQLARALYDN 1936
Cdd:COG4717 426 DEEELEEELeeLEEELEELEEELEELREELAELEAELEQLEEDGELAellqelEELKAELRELAEEW-AALKLALELLEE 504
|
...
gi 431907173 1937 TAE 1939
Cdd:COG4717 505 ARE 507
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
837-1329 |
1.96e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.17 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 837 KIKPLLKSAETEKEMANMK---------EEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERC 907
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKkkaeeakkaDEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA 1524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 908 DQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVknltEEMAGL 987
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI----EEVMKL 1600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 988 DEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDlKLTQES 1067
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED-KKKAEE 1679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1068 IMDLENDKLQLEEKLKKKEFD---ISQQNSKIEDEQALALQLQKKLKENqarieeleeeleaertaRAKVEKLRsdlsRE 1144
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEakkAEELKKKEAEEKKKAEELKKAEEEN-----------------KIKAEEAK----KE 1738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1145 LEEISERLEEAggatsvqiemnKKREAEFQKMRRDLEEatlqhEATAAALRKKHADSVAELGeqidnlqrVKQKLEKEKS 1224
Cdd:PTZ00121 1739 AEEDKKKAEEA-----------KKDEEEKKKIAHLKKE-----EEKKAEEIRKEKEAVIEEE--------LDEEDEKRRM 1794
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1225 EFKLELDDVTSNMEQIIK-----------AKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQL 1293
Cdd:PTZ00121 1795 EVDKKIKDIFDNFANIIEggkegnlvindSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEK 1874
|
490 500 510
....*....|....*....|....*....|....*.
gi 431907173 1294 EEKEALISQLTRGKLSYTQQTEDLKRQLEEEGKAKN 1329
Cdd:PTZ00121 1875 DLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGK 1910
|
|
| SH3_9 |
pfam14604 |
Variant SH3 domain; |
1932-1984 |
2.07e-11 |
|
Variant SH3 domain;
Pssm-ID: 434066 [Multi-domain] Cd Length: 49 Bit Score: 60.71 E-value: 2.07e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSLHGQQGIVPANRVK 1984
Cdd:pfam14604 1 ALYPYEPKDDDELSLQRGDVITVIEESE----DGWWEGINTGRTGLVPANYVE 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1436-1876 |
2.45e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.03 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1436 AALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLtEQLGEG 1515
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1516 GKNVHELEKVRKQLEAEKLELQsALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQT 1595
Cdd:COG4717 128 LPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1596 SLDAETRSRNEALRVKKKMEGDLNEMEIQL--SQANRTASEAQKHLKIA---------QAHLKDTQLQMDDAVRANDDLk 1664
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELeaAALEERLKEARLLLLIAaallallglGGSLLSLILTIAGVLFLVLGL- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1665 enIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQEC 1744
Cdd:COG4717 286 --LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1745 RNAEEKAKKA----------ITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKggkKQLQKLEAR 1814
Cdd:COG4717 364 QLEELEQEIAallaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE---EELEELEEE 440
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 431907173 1815 VRELENELEAEQKRnaesvkgMRKSERRIKELTYQTEEDKKnLLRLQDLVDKLQLKVKAYKR 1876
Cdd:COG4717 441 LEELEEELEELREE-------LAELEAELEQLEEDGELAEL-LQELEELKAELRELAEEWAA 494
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
846-1424 |
4.29e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 846 ETEKEMANMKEEFGRLKET---LEKSEARRKELE------EKMVSLLQEKNDLQ-----LQVQAEQDNLNDAEERCDQLI 911
Cdd:COG4913 222 DTFEAADALVEHFDDLERAheaLEDAREQIELLEpirelaERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 912 KNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLE-DECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEI 990
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 991 IAKLTKEKKALQEAHQQALDDLQAEEDKvntLTKSKVKLEQQVDDLEG---SLEQeKKVRMD--LERAKRKLEGDLKLTQ 1065
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAE---AEAALRDLRRELRELEAeiaSLER-RKSNIParLLALRDALAEALGLDE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1066 ESI------MDLEN----------------------------------DKLQLEEKL---KKKEFDISQQNSKIeDEQAL 1102
Cdd:COG4913 458 AELpfvgelIEVRPeeerwrgaiervlggfaltllvppehyaaalrwvNRLHLRGRLvyeRVRTGLPDPERPRL-DPDSL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1103 ALQLqkKLKENQARieELEEELEAERTARAKVEKLrsdlsRELEEISERLEEAGgatsvQIEMNKKReaeFQKMRRDLEE 1182
Cdd:COG4913 537 AGKL--DFKPHPFR--AWLEAELGRRFDYVCVDSP-----EELRRHPRAITRAG-----QVKGNGTR---HEKDDRRRIR 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1183 AT--LQHEATA--AALRKKHA---DSVAELGEQIDNLQRVKQKLEKEKS------EFKLELDDVTSNMEQIIKAKANLEK 1249
Cdd:COG4913 600 SRyvLGFDNRAklAALEAELAeleEELAEAEERLEALEAELDALQERREalqrlaEYSWDEIDVASAEREIAELEAELER 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1250 VS------RTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLtrGKLSYTQQTEDLKRQLEE 1323
Cdd:COG4913 680 LDassddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA--EDLARLELRALLEERFAA 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1324 EGKAK--NALAHALQSARHDCDLLREQYEEETEAK------------AELQRVLSkANSEVAQWRTKYETDAI-QRTEEL 1388
Cdd:COG4913 758 ALGDAveRELRENLEERIDALRARLNRAEEELERAmrafnrewpaetADLDADLE-SLPEYLALLDRLEEDGLpEYEERF 836
|
650 660 670
....*....|....*....|....*....|....*.
gi 431907173 1389 EEAKLQDAEEAVEAVnakCSSLEKTKHRLQNEIEDL 1424
Cdd:COG4913 837 KELLNENSIEFVADL---LSKLRRAIREIKERIDPL 869
|
|
| SH3_1 |
pfam00018 |
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ... |
1931-1980 |
5.07e-11 |
|
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.
Pssm-ID: 394975 [Multi-domain] Cd Length: 47 Bit Score: 59.52 E-value: 5.07e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSLH-GQQGIVPA 1980
Cdd:pfam00018 1 VALYDYTAQEPDELSFKKGDIIIVLEKSE----DGWWKGRNKgGKEGLIPS 47
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
835-1305 |
5.92e-11 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 68.39 E-value: 5.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 835 YFKIKPLLKSAETE-KEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQA---EQDNLNDAEERCDQL 910
Cdd:PRK01156 168 YDKLKDVIDMLRAEiSNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNamdDYNNLKSALNELSSL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 911 IKNKIQLEAKVKEMNERLEDEEEMNAELTA--------------KKRKLEDECSELKRDIDDLELTLAKVEKEKHATENK 976
Cdd:PRK01156 248 EDMKNRYESEIKTAESDLSMELEKNNYYKEleerhmkiindpvyKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAI 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 977 VKNLTEEMAGLDEIIakltkEKKALQEAHQQALDDLQAEEDKVNTLTKS----KVKLE---------------------- 1030
Cdd:PRK01156 328 IKKLSVLQKDYNDYI-----KKKSRYDDLNNQILELEGYEMDYNSYLKSieslKKKIEeyskniermsafiseilkiqei 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1031 ----------------QQVDDLEGSLEQEKKV----RMDLERAKRKLEGDLK-------LTQESIMDL----ENDKLQLE 1079
Cdd:PRK01156 403 dpdaikkelneinvklQDISSKVSSLNQRIRAlrenLDELSRNMEMLNGQSVcpvcgttLGEEKSNHIinhyNEKKSRLE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1080 EKLKKKEFDISQQNSKIEDEQALALQLQK-----------KLKENQARIEELEEELEAERTARAKVEKLRSDL-SRELEE 1147
Cdd:PRK01156 483 EKIREIEIEVKDIDEKIVDLKKRKEYLESeeinksineynKIESARADLEDIKIKINELKDKHDKYEEIKNRYkSLKLED 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1148 ISERLEEAGGATSV----QIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEK 1223
Cdd:PRK01156 563 LDSKRTSWLNALAVisliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1224 SEFKlELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQL 1303
Cdd:PRK01156 643 ILIE-KLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDI 721
|
..
gi 431907173 1304 TR 1305
Cdd:PRK01156 722 NE 723
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
835-1280 |
6.16e-11 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 67.94 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 835 YFKIKPLLKSAE-----TEKEMANMKEEFGRLKETLEKSEARRKELEEKmvslLQEkndLQLQVQAEQDNLNDAEErcdq 909
Cdd:PRK04778 100 FRKAKHEINEIEslldlIEEDIEQILEELQELLESEEKNREEVEQLKDL----YRE---LRKSLLANRFSFGPALD---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 910 liknkiQLEAKVKEMNERLEDEEEMNAE---LTAKK--RKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKN----L 980
Cdd:PRK04778 169 ------ELEKQLENLEEEFSQFVELTESgdyVEAREilDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyreL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 981 TEEMAGLDEIiaKLTKEKKALQEAHQQALDDLQAEE-DKVNTLTKskvKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEG 1059
Cdd:PRK04778 243 VEEGYHLDHL--DIEKEIQDLKEQIDENLALLEELDlDEAEEKNE---EIQERIDQLYDILEREVKARKYVEKNSDTLPD 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1060 DLKLTQEsimdlENDKLQLEEKLKKKEFDISqqnskiEDEQALALQLQKKLKENQARIEELEEELeaertarAKVEKLRS 1139
Cdd:PRK04778 318 FLEHAKE-----QNKELKEEIDRVKQSYTLN------ESELESVRQLEKQLESLEKQYDEITERI-------AEQEIAYS 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1140 DLSRELEEISERLEEAggatsvqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAEL---------GEQID 1210
Cdd:PRK04778 380 ELQEELEEILKQLEEI-----------EKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLeksnlpglpEDYLE 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1211 NLQRVK---QKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQA----------NEYRT-------KLEEAQR 1270
Cdd:PRK04778 449 MFFEVSdeiEALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVENAtlteqliqyaNRYRSdneevaeALNEAER 528
|
490
....*....|
gi 431907173 1271 SLNDFTTQQA 1280
Cdd:PRK04778 529 LFREYDYKAA 538
|
|
| SH3_iASPP |
cd11952 |
Src Homology 3 (SH3) domain of Inhibitor of ASPP protein (iASPP); iASPP, also called ... |
1932-1981 |
6.92e-11 |
|
Src Homology 3 (SH3) domain of Inhibitor of ASPP protein (iASPP); iASPP, also called RelA-associated inhibitor (RAI), is an oncoprotein that inhibits the apoptotic transactivation potential of p53. It is upregulated in human breast cancers expressing wild-type p53, in acute leukemias regardless of the p53 mutation status, as well as in ovarian cancer where it is associated with poor patient outcome and chemoresistance. iASPP is also a binding partner and negative regulator of p65RelA, which promotes cell proliferation and inhibits apoptosis; p65RelA has the opposite effect on cell growth compared to the p53 family. It contains a proline-rich region, four ankyrin (ANK) repeats, and an SH3 domain at its C-terminal half. The SH3 domain and the ANK repeats of iASPP contribute to the p53 binding site; they bind to the DNA binding domain of p53. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212885 [Multi-domain] Cd Length: 56 Bit Score: 59.56 E-value: 6.92e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQREGAGGldGWCLCSLHGQQGIVPAN 1981
Cdd:cd11952 5 ALWDYSAEFPDELSFKEGDMVTVLRKDGEGT--DWWWASLCGREGYVPRN 52
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1677-1957 |
7.52e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 67.89 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1677 LQAELEELRAVVEQteRSRKLaEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEavQECRNAEEKAKKAIT 1756
Cdd:pfam01576 55 LCAEAEEMRARLAA--RKQEL-EEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE--EEAARQKLQLEKVTT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1757 DAAM--MAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAlKGGKKQLQKLEARVRELENELEAEQKRNAESVK 1834
Cdd:pfam01576 130 EAKIkkLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKA-KSLSKLKNKHEAMISDLEERLKKEEKGRQELEK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1835 GMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVN 1914
Cdd:pfam01576 209 AKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARN 288
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 431907173 1915 KLRAKSRDIGAKAQLARALYDNTAESP---QELSFRRGDVLRVLQR 1957
Cdd:pfam01576 289 KAEKQRRDLGEELEALKTELEDTLDTTaaqQELRSKREQEVTELKK 334
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1492-1948 |
7.93e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 67.84 E-value: 7.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1492 ETFKRENKNLQEEISDLTEQLGEGGKnVHELEKVrkQLEAEKLELQSALEEaeasLEHEEGKILRAQLEFNQIKAEIERK 1571
Cdd:pfam15921 74 EHIERVLEEYSHQVKDLQRRLNESNE-LHEKQKF--YLRQSVIDLQTKLQE----MQMERDAMADIRRRESQSQEDLRNQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1572 LAEKDEEMEQAKrnhlrvvdSLQTSLDAETRSRNEALR-VKKKMEGDLNEM-EIQLSQANRTASEAQKHLKIAQAHLKDT 1649
Cdd:pfam15921 147 LQNTVHELEAAK--------CLKEDMLEDSNTQIEQLRkMMLSHEGVLQEIrSILVDFEEASGKKIYEHDSMSTMHFRSL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1650 QLQMDDAVRANDD----LKENIAIVERRNNLLQAELE-----------------------ELRAVVEQTERSRKLA---- 1698
Cdd:pfam15921 219 GSAISKILRELDTeisyLKGRIFPVEDQLEALKSESQnkielllqqhqdrieqlisehevEITGLTEKASSARSQAnsiq 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1699 -EQELIETSERvqllhSQNTSLINQKKKMESDLTQLQSEVEEA--------------------------------VQECR 1745
Cdd:pfam15921 299 sQLEIIQEQAR-----NQNSMYMRQLSDLESTVSQLRSELREAkrmyedkieelekqlvlanseltearterdqfSQESG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1746 NAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEARVRELENELEAE 1825
Cdd:pfam15921 374 NLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNM--------EVQRLEALLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1826 QKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKR----------QAEEAEEQANTNLSKFR-- 1893
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERtvsdltaslqEKERAIEATNAEITKLRsr 525
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1894 ------KVQHELDEAEERADI-AESQVNKLRAKSRD----------------IGAKAQLARALYDNTAESPQELSFRR 1948
Cdd:pfam15921 526 vdlklqELQHLKNEGDHLRNVqTECEALKLQMAEKDkvieilrqqienmtqlVGQHGRTAGAMQVEKAQLEKEINDRR 603
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
854-1295 |
9.42e-11 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 67.54 E-value: 9.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 854 MKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLiknkiqlEAKVKEMNERLEDEEE 933
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL-------QTEVDALRLRLEEKES 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 934 MNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQA----- 1008
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTdtalt 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1009 -LDDLQAEEDKV-NTLTKSKVKLEQQVDDlegSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKE 1086
Cdd:pfam10174 440 tLEEALSEKERIiERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKD 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1087 FDISQQNSKIEDEQALALQLQKKLKENQarieeleeelEAERTARAKVEklRSDLSRELE-EISERLEEAGGA-TSVQIE 1164
Cdd:pfam10174 517 SKLKSLEIAVEQKKEECSKLENQLKKAH----------NAEEAVRTNPE--INDRIRLLEqEVARYKEESGKAqAEVERL 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1165 MNKKREAEFQKMRRDLEEATLqhEATAAALRKKHADSVAEL--GEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIK 1242
Cdd:pfam10174 585 LGILREVENEKNDKDKKIAEL--ESLTLRQMKEQNKKVANIkhGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMG 662
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1243 AkanLEKVSRTLEdqanEYRTKLEEAQRSLndfTTQQAKLQTENGELARQLEE 1295
Cdd:pfam10174 663 A---LEKTRQELD----ATKARLSSTQQSL---AEKDGHLTNLRAERRKQLEE 705
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1137-1587 |
1.26e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.71 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1137 LRSDLSRELEEISERLEEAGGATSvqiEMNKKreaEFQKMRRDLEEATLQHEATAAALRKKHadsvaELGEQIDNLQRVK 1216
Cdd:COG4717 43 IRAMLLERLEKEADELFKPQGRKP---ELNLK---ELKELEEELKEAEEKEEEYAELQEELE-----ELEEELEELEAEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1217 QKLEKEKSEfklelddvtsnMEQIIKAKANLEKVsRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEK 1296
Cdd:COG4717 112 EELREELEK-----------LEKLLQLLPLYQEL-EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1297 EALISQLTRGKLsytQQTEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYE--EETEAKAELQRVLSKANSE----- 1369
Cdd:COG4717 180 EELLEQLSLATE---EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKEARLLlliaa 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1370 --------------------------------VAQWRTKYETDAIQRTEELEEAKLQDAEEAVEavnakcsslektkhrL 1417
Cdd:COG4717 257 allallglggsllsliltiagvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEE---------------L 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1418 QNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQkyeesqSELESSQKEARSLSTELFKLKNA-YEESLEHLETFKR 1496
Cdd:COG4717 322 EELLAALGLPPDLSPEELLELLDRIEELQELLREAEE------LEEELQLEELEQEIAALLAEAGVeDEEELRAALEQAE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1497 ENKNLQEEISDLTEQLGEGGKNVHELEKV--RKQLEAEKLELQSALEEAEASLE--HEEGKILRAQLE-------FNQIK 1565
Cdd:COG4717 396 EYQELKEELEELEEQLEELLGELEELLEAldEEELEEELEELEEELEELEEELEelREELAELEAELEqleedgeLAELL 475
|
490 500
....*....|....*....|..
gi 431907173 1566 AEIERKLAEKDEEMEQAKRNHL 1587
Cdd:COG4717 476 QELEELKAELRELAEEWAALKL 497
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1148-1905 |
1.85e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 66.79 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1148 ISERLEEAGgatSVQIEMNKKReaefQKMRRDLEEatlqHEATAAALRKKHadSVAELGEQIDNLQRVKQKLEKEKSEFK 1227
Cdd:pfam12128 202 IVAILEDDG---VVPPKSRLNR----QQVEHWIRD----IQAIAGIMKIRP--EFTKLQQEFNTLESAELRLSHLHFGYK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1228 LELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEeaqrslNDFTTQQAKLQTENGELARqLEEKEALISQLTRGK 1307
Cdd:pfam12128 269 SDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELN------GELSAADAAVAKDRSELEA-LEDQHGAFLDADIET 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1308 LSYTQQTEDLKR-QLEEEGKAKNALAHALQsarhdcDLLREQYEEETEAKAELQRVLSKANSEVAQWRtkyetDAIQRTE 1386
Cdd:pfam12128 342 AAADQEQLPSWQsELENLEERLKALTGKHQ------DVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIR-----EARDRQL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1387 ELEEAKLQDAEEAV-EAVNAKCSSLEKTKHRLQNEIEDLMVdveRSNAAAAALDKK--QRNFDKILAEWKQKyeesqseL 1463
Cdd:pfam12128 411 AVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGELKL---RLNQATATPELLlqLENFDERIERAREE-------Q 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1464 ESSQKEARSLSTELFKLKNAYEESLEHLetfKRENKNLQEEISdlteqlgeggknvhELEKVRKQLEAEKLELQSALEEA 1543
Cdd:pfam12128 481 EAANAEVERLQSELRQARKRRDQASEAL---RQASRRLEERQS--------------ALDELELQLFPQAGTLLHFLRKE 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1544 EASLEHEEGKIL-RAQLEFNQIKAEIERKlAEKDEEMEQAKRNHLRVVDSlqtsldAETRSRNEALRVKkkmegdLNEME 1622
Cdd:pfam12128 544 APDWEQSIGKVIsPELLHRTDLDPEVWDG-SVGGELNLYGVKLDLKRIDV------PEWAASEEELRER------LDKAE 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1623 IQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDAVRAnddLKENIAIVERRNNLLQAeleELRAVVEQTERSRKLAEQEL 1702
Cdd:pfam12128 611 EALQSAREKQAAAEEQLVQANGELEKASREETFARTA---LKNARLDLRRLFDEKQS---EKDKKNKALAERKDSANERL 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1703 IE-TSERVQLLHSQNTSLINQKKKMESDLTQLQS---EVEEA-------VQECRNAEEKAKKAITDA--AMMAEELKK-- 1767
Cdd:pfam12128 685 NSlEAQLKQLDKKHQAWLEEQKEQKREARTEKQAywqVVEGAldaqlalLKAAIAARRSGAKAELKAleTWYKRDLASlg 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1768 -EQDTSAHLERMKKNMEQTIKDLQHRLDEA---EQIALKGGKKQLQKLEARVRELEN---ELEAEQKRNAESVKGMRKS- 1839
Cdd:pfam12128 765 vDPDVIAKLKREIRTLERKIERIAVRRQEVlryFDWYQETWLQRRPRLATQLSNIERaisELQQQLARLIADTKLRRAKl 844
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1840 ERRIKELTYQTEEDKKNLLRLQDLVDKL-QLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEER 1905
Cdd:pfam12128 845 EMERKASEKQQVRLSENLRGLRCEMSKLaTLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKK 911
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
865-1563 |
1.95e-10 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 66.38 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 865 LEKSEARRKE-------LEEKMVSLLQEKNDLQLQVQAEQDNLndaeercdqliknKIQleakvKEMNERLEDEEEMNAE 937
Cdd:pfam10174 41 LKKERALRKEeaarisvLKEQYRVTQEENQHLQLTIQALQDEL-------------RAQ-----RDLNQLLQQDFTTSPV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 938 LTAKK---RKLEDEC-----SELKRDIDDLELTLAKVEKekhaTENKVKNLTEEMAGLDEIIAKLtkekkaLQEAHQQAL 1009
Cdd:pfam10174 103 DGEDKfstPELTEENfrrlqSEHERQAKELFLLRKTLEE----MELRIETQKQTLGARDESIKKL------LEMLQSKGL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1010 DDLQAEEDkvNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDL-ERAKRKLEG--------------DLKLTQESIMDLEND 1074
Cdd:pfam10174 173 PKKSGEED--WERTRRIAEAEMQLGHLEVLLDQKEKENIHLrEELHRRNQLqpdpaktkalqtviEMKDTKISSLERNIR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1075 KLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENqarieeleeeleaertaraKVEKLRSDLSR---ELEEISER 1151
Cdd:pfam10174 251 DLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKN-------------------KIDQLKQELSKkesELLALQTK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1152 LEEAGGATS---VQIEMNKkrEAEFQKMRRdleEATLQHEATAAALRKKHADSVaeLGEQIDNLQRvkqkLEKEKSEFKL 1228
Cdd:pfam10174 312 LETLTNQNSdckQHIEVLK--ESLTAKEQR---AAILQTEVDALRLRLEEKESF--LNKKTKQLQD----LTEEKSTLAG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1229 ELDDVtSNMEQIIKAKAN-LEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLtrgk 1307
Cdd:pfam10174 381 EIRDL-KDMLDVKERKINvLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERL---- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1308 lsyTQQTEDLKRQLEEEgkaKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAI---QR 1384
Cdd:pfam10174 456 ---KEQREREDRERLEE---LESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIaveQK 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1385 TEELE--EAKLQDAEEAVEAV------NAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKY 1456
Cdd:pfam10174 530 KEECSklENQLKKAHNAEEAVrtnpeiNDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLT 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1457 EESQSELESSQKEARSLSTELfKLKNAYEESLEHLETFKRENKNLQEEISDLTEqlgeggknvhELEKVRKQLEAEKLEL 1536
Cdd:pfam10174 610 LRQMKEQNKKVANIKHGQQEM-KKKGAQLLEEARRREDNLADNSQQLQLEELMG----------ALEKTRQELDATKARL 678
|
730 740 750
....*....|....*....|....*....|...
gi 431907173 1537 ---QSALEEAEA---SLEHEEGKILRAQLEFNQ 1563
Cdd:pfam10174 679 sstQQSLAEKDGhltNLRAERRKQLEEILEMKQ 711
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
843-1392 |
2.45e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 66.40 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 843 KSAETEKEMANMKEEFGRLKETLEKSEARRKELE-----------EKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLI 911
Cdd:pfam12128 302 KRDELNGELSAADAAVAKDRSELEALEDQHGAFLdadietaaadqEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRR 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 912 KN-KIQLEAKVKEMNERLED-------------------EEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKH 971
Cdd:pfam12128 382 SKiKEQNNRDIAGIKDKLAKireardrqlavaeddlqalESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 972 ATENKvKNLTEEMAGLDEIIAKLTKEKKALQE-------AHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSL---- 1040
Cdd:pfam12128 462 LLLQL-ENFDERIERAREEQEAANAEVERLQSelrqarkRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLlhfl 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1041 --------EQEKKV-------RMDLERAKRKLEGDLKLTQESI-MDLE----NDKLQLEEKLKKKefdISQQNSKIEDEQ 1100
Cdd:pfam12128 541 rkeapdweQSIGKVispellhRTDLDPEVWDGSVGGELNLYGVkLDLKridvPEWAASEEELRER---LDKAEEALQSAR 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1101 ALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMN-KKREAEFQKMRRD 1179
Cdd:pfam12128 618 EKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERlNSLEAQLKQLDKK 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1180 LEEATLQHEATAAALR-KKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQA 1258
Cdd:pfam12128 698 HQAWLEEQKEQKREARtEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREI 777
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1259 NEYRTKLEEAQRSLNDFTT----QQAKLQTENGELARQLEEKEALISQLtRGKLsyTQQTEDLKR---QLEEEGKAKNAL 1331
Cdd:pfam12128 778 RTLERKIERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIERAISEL-QQQL--ARLIADTKLrraKLEMERKASEKQ 854
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1332 AHALQSARHDCDLLREQYEEETEAK--AELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAK 1392
Cdd:pfam12128 855 QVRLSENLRGLRCEMSKLATLKEDAnsEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFK 917
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
833-1602 |
2.73e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 66.22 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 833 KLYFKIKPLLKSAETEKEMANMKEEFGRLKETLEKSE--ARRKELEEKMVSLLQEKNDL------QLQVQAEQDNLNDAE 904
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEknSLTETLKKEVKSLQNEKADLdrklrkLDQEMEQLNHHTTTR 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 905 ERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDID-------DLELTLAKVEKEKHATENKV 977
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtrdrlaKLNKELASLEQNKNHINNEL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 978 KNLTEEMAGLDEIIAKLTKekkalQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKL 1057
Cdd:TIGR00606 615 ESKEEQLSSYEDKLFDVCG-----SQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQT 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1058 EGDLkltQESIMDLEN------DKLQ-LEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKEnqarieeleeeleaertA 1130
Cdd:TIGR00606 690 EAEL---QEFISDLQSklrlapDKLKsTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPE-----------------L 749
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1131 RAKVEKLRSDLSRELEEISERlEEAGGATSVQIEMNKKREAEFQKMRRdLEEATLQHEataaalrKKHADSVAELgeQID 1210
Cdd:TIGR00606 750 RNKLQKVNRDIQRLKNDIEEQ-ETLLGTIMPEEESAKVCLTDVTIMER-FQMELKDVE-------RKIAQQAAKL--QGS 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1211 NLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANE---YRTKLEEAQRSLNDFTTQQAKLQTENG 1287
Cdd:TIGR00606 819 DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElksEKLQIGTNLQRRQQFEEQLVELSTEVQ 898
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1288 ELARQLEEKEALISQLTRGKLSYTQQTEDLKRQLEEEGKaknalahalqsarhdcdllreqyeeetEAKAELQRVLSKAN 1367
Cdd:TIGR00606 899 SLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK---------------------------KAQDKVNDIKEKVK 951
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1368 SEVAqwrtkYETDAIQRTEELEEAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALD------KK 1441
Cdd:TIGR00606 952 NIHG-----YMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQdnltlrKR 1026
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1442 QRNFDKILAEWKQKYEESQSELESSQKEA-RSLSTELFKLKN----------AYEESLEHLETFKREN--KNLQEEISDL 1508
Cdd:TIGR00606 1027 ENELKEVEEELKQHLKEMGQMQVLQMKQEhQKLEENIDLIKRnhvlalgrqkGYEKEIKHFKKELREPqfRDAEEKYREM 1106
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1509 TEQLGEGGKNVHELEKVRKQLEAEKLELQS-ALEEAEASLEHEEGKILRAQ-LEFNQIKAEIERKLAEKDEEMEQakrNH 1586
Cdd:TIGR00606 1107 MIVMRTTELVNKDLDIYYKTLDQAIMKFHSmKMEEINKIIRDLWRSTYRGQdIEYIEIRSDADENVSASDKRRNY---NY 1183
|
810
....*....|....*.
gi 431907173 1587 LRVVDSLQTSLDAETR 1602
Cdd:TIGR00606 1184 RVVMLKGDTALDMRGR 1199
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1985-2232 |
3.30e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 66.12 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1985 LLPAGPTPKPSLSqVPPAEPGSPYPAPEHSNEDQEVYVVPPPARPCL---TSESPAGPCLPS--------PDPIYKVPRG 2053
Cdd:PHA03247 2555 LPPAAPPAAPDRS-VPPPRPAPRPSEPAVTSRARRPDAPPQSARPRApvdDRGDPRGPAPPSplppdthaPDPPPPSPSP 2633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2054 SGTQPATPGDAL----EVYDVPPAALRVS-------------ASGPYD------TPASFSHLLARVAPQPPGEDEAPYDV 2110
Cdd:PHA03247 2634 AANEPDPHPPPTvpppERPRDDPAPGRVSrprrarrlgraaqASSPPQrprrraARPTVGSLTSLADPPPPPPTPEPAPH 2713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2111 PLAPKPPSELEPdlEWEGGREPGPPLYAAPSNLKRASALlnlyeaPEELLADGEEGGSDEGIYDVPLLGPETPPSPE-PL 2189
Cdd:PHA03247 2714 ALVSATPLPPGP--AAARQASPALPAAPAPPAVPAGPAT------PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRlTR 2785
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 431907173 2190 GALASNDPDTLALLLARSPPPSHRPRLPSAESLSRRPLPALPV 2232
Cdd:PHA03247 2786 PAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPL 2828
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
903-1142 |
3.36e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.40 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 903 AEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTE 982
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 983 EMAGLDEIIAKLTKekkALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLK 1062
Cdd:COG4942 98 ELEAQKEELAELLR---ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1063 LTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEE--LEEELEAERTARAKVEKLRSD 1140
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARleAEAAAAAERTPAAGFAALKGK 254
|
..
gi 431907173 1141 LS 1142
Cdd:COG4942 255 LP 256
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1077-1574 |
5.42e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1077 QLEEKLKKKEfdisQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVE--KLRSDLSRELEEISERLEE 1154
Cdd:COG4717 75 ELEEELKEAE----EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1155 AggatsvqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVT 1234
Cdd:COG4717 151 L-----------EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1235 SNMEQIIKAKANLEKVSRTLEDQAneyrtKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEAL----------ISQLT 1304
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEE-----RLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1305 RGKLSYTQQTEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQr 1384
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA- 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1385 tEELEEAKLQDAEEAVEAVNAKcssleKTKHRLQNEIEDLmvdversnaaaaaldkkqrnfdkilaewkqkyeesqsele 1464
Cdd:COG4717 374 -ALLAEAGVEDEEELRAALEQA-----EEYQELKEELEEL---------------------------------------- 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1465 ssqkEARslstelfkLKNAYEESLEHLETFKRENknLQEEISDLTEQLgeggknvHELEKVRKQLEAEKLELQSALEEAE 1544
Cdd:COG4717 408 ----EEQ--------LEELLGELEELLEALDEEE--LEEELEELEEEL-------EELEEELEELREELAELEAELEQLE 466
|
490 500 510
....*....|....*....|....*....|
gi 431907173 1545 aslehEEGKILRAQLEFNQIKAEIERKLAE 1574
Cdd:COG4717 467 -----EDGELAELLQELEELKAELRELAEE 491
|
|
| SH3_RUSC1_like |
cd11810 |
Src homology 3 domain of RUN and SH3 domain-containing proteins 1 and 2; RUSC1 and RUSC2, that ... |
1931-1979 |
6.06e-10 |
|
Src homology 3 domain of RUN and SH3 domain-containing proteins 1 and 2; RUSC1 and RUSC2, that were originally characterized in silico. They are adaptor proteins consisting of RUN, leucine zipper, and SH3 domains. RUSC1, also called NESCA (New molecule containing SH3 at the carboxy-terminus), is highly expressed in the brain and is translocated to the nuclear membrane from the cytoplasm upon stimulation with neurotrophin. It plays a role in facilitating neurotrophin-dependent neurite outgrowth. It also interacts with NEMO (or IKKgamma) and may function in NEMO-mediated activation of NF-kB. RUSC2, also called Iporin, is expressed ubiquitously with highest amounts in the brain and testis. It interacts with the small GTPase Rab1 and the Golgi matrix protein GM130, and may function in linking GTPases to certain intracellular signaling pathways. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212744 Cd Length: 50 Bit Score: 56.68 E-value: 6.06e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSLHGQQGIVP 1979
Cdd:cd11810 3 RALCHHVATDSGQLSFRKGDILRVIARVD----DDWLLCTRGSTKGLVP 47
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1100-1339 |
6.30e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1100 QALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnkkrEAEFQKMRRD 1179
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL--------------EQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1180 LEEATLQheatAAALRKKHADSVAELGEQIDNLQRVKQKlekekSEFKLELDdvTSNMEQIIKAKANLEKVSRTLEDQAN 1259
Cdd:COG4942 85 LAELEKE----IAELRAELEAQKEELAELLRALYRLGRQ-----PPLALLLS--PEDFLDAVRRLQYLKYLAPARREQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1260 EYRTKLEEAQRSLNDFTTQQAKL-------QTENGELARQLEEKEALISQLTRGKLSYTQQTEDLKRQLEEEGKAKNALA 1332
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELeallaelEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
....*..
gi 431907173 1333 HALQSAR 1339
Cdd:COG4942 234 AEAAAAA 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1128-1607 |
1.20e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1128 RTARAKVEKLRsdlsrELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATL-----------QHEATAAALRK 1196
Cdd:COG4913 245 EDAREQIELLE-----PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELeelraelarleAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1197 KHADSVAELGEQIDNLQ-RVKQKLEKEKSEFKLELDDVTSN----MEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRS 1271
Cdd:COG4913 320 ALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRrarlEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1272 LNDFTTQQAKLQTENGELARQLEEKEALISQLTRGKLSYTQQTEDLKRQLEEE--------------------------- 1324
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAlgldeaelpfvgelievrpeeerwrga 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1325 -------------------------------------GKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLS--- 1364
Cdd:COG4913 480 iervlggfaltllvppehyaaalrwvnrlhlrgrlvyERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAELGrrf 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1365 ---KANSE---------------VAQWRTKYETDAiqRTEELEEAKL-QDAEEAVEAvnakcssLEKTKHRLQNEIEDLM 1425
Cdd:COG4913 560 dyvCVDSPeelrrhpraitragqVKGNGTRHEKDD--RRRIRSRYVLgFDNRAKLAA-------LEAELAELEEELAEAE 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1426 VDVERSNAAAAALDKKQRNFDKIlaewkQKYEESQSELESSQKEARSLSTELFKLknayEESLEHLETFKRENKNLQEEI 1505
Cdd:COG4913 631 ERLEALEAELDALQERREALQRL-----AEYSWDEIDVASAEREIAELEAELERL----DASSDDLAALEEQLEELEAEL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1506 SDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEASLEHEegkiLRAQLEfnqikaeiERKLAEKDEEMEQakrn 1585
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE----LRALLE--------ERFAAALGDAVER---- 765
|
570 580
....*....|....*....|..
gi 431907173 1586 hlRVVDSLQTSLDAETRSRNEA 1607
Cdd:COG4913 766 --ELRENLEERIDALRARLNRA 785
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
837-1455 |
1.67e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.60 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 837 KIKPLLKSAETEKEM-ANMKEEFGRLKETLEKSE-------------ARRKELEEKMVSLLQEKNDLQLQ----VQAEQD 898
Cdd:pfam15921 462 KVSSLTAQLESTKEMlRKVVEELTAKKMTLESSErtvsdltaslqekERAIEATNAEITKLRSRVDLKLQelqhLKNEGD 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 899 NLNDAEERCDQLiknKIQLEAK---VKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATEN 975
Cdd:pfam15921 542 HLRNVQTECEAL---KLQMAEKdkvIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDA 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 976 KVKNLTEEMAGLDEIIAKLT-------KEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQE-KKVR 1047
Cdd:pfam15921 619 KIRELEARVSDLELEKVKLVnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTtNKLK 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1048 MDLERAKRKLEgDLKLTQESIMDLENDKLQLEEKLKKKefdISQQNSKIEdeqalALQlqkklkenqARIEELEEELEAE 1127
Cdd:pfam15921 699 MQLKSAQSELE-QTRNTLKSMEGSDGHAMKVAMGMQKQ---ITAKRGQID-----ALQ---------SKIQFLEEAMTNA 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1128 RTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQ----------HEATAAALRKK 1197
Cdd:pfam15921 761 NKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQfaecqdiiqrQEQESVRLKLQ 840
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1198 HADSVAEL-GEQIDNLQRVKQKLEKEKSeFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFT 1276
Cdd:pfam15921 841 HTLDVKELqGPGYTSNSSMKPRLLQPAS-FTRTHSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEP 919
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1277 TQQAKLQTENGEL--ARQLEE--KEALISQLTRGKLSYTQ----QTEDLKrqLEEEGKAKNALAHALQ-SARHDCDLLRE 1347
Cdd:pfam15921 920 TVQLSKAEDKGRApsLGALDDrvRDCIIESSLRSDICHSSsnslQTEGSK--SSETCSREPVLLHAGElEDPSSCFTFPS 997
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1348 QYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAK-LQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMV 1426
Cdd:pfam15921 998 TASPSVKNSASRSFHSSPKKSPVHSLLTSSAEGSIGSSSQYRSAKtIHSPDSVKDSQSLPIETTGKTCRKLQNRLESLQT 1077
|
650 660
....*....|....*....|....*....
gi 431907173 1427 DVERSNAAAAALDKKQRNFDKILAEWKQK 1455
Cdd:pfam15921 1078 LVEDLQLKNQAMSSMIRNQEKRIQKVKDQ 1106
|
|
| PHA03418 |
PHA03418 |
hypothetical E4 protein; Provisional |
2009-2188 |
1.93e-09 |
|
hypothetical E4 protein; Provisional
Pssm-ID: 177646 [Multi-domain] Cd Length: 230 Bit Score: 60.52 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2009 PAPEHSN--EDQEVYVVPPPaRPCLTSESPAGPCLPSPDPIYKVPRGSGTQ-----PATP-GDalevyDVPPAALRVSAS 2080
Cdd:PHA03418 37 PAPHHPNpqEDPDKNPSPPP-DPPLTPRPPAQPNGHNKPPVTKQPGGEGTEedhqaPLAAdAD-----DDPRPGKRSKAD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2081 GPYDTP--ASFSHLLARVAPQPP--GEDEAPYDV-PLAPKPPselepdlewEGGREPGPPLyaapsnlkrasallnlyea 2155
Cdd:PHA03418 111 EHGPAPgrAALAPFKLDLDQDPLhgDPDPPPGATgGQGEEPP---------EGGEESQPPL------------------- 162
|
170 180 190
....*....|....*....|....*....|...
gi 431907173 2156 peelladGEEGGSDEGiydVPllgPETPPSPEP 2188
Cdd:PHA03418 163 -------GEGEGAVEG---HP---PPLPPAPEP 182
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
812-1329 |
2.29e-09 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 62.67 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 812 ALLVIQWNIRAFMGVKNWpWMKLYFKIKPLlksAETEKEMANMKEEfgrLKETLEKSEARRKELEEKMVSLLQEKNDLQL 891
Cdd:COG5185 28 LLESSKSEGKTLVFITIL-FFPLGISRDSL---RVTLRSVINVLDG---LNYQNDVKKSESSVKARKFLKEKKLDTKILQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 892 QVQAEQ---DNLNDAEERCDQLIKNKIQLEAKVKEMN---------ERLEDEEEMNAELTAKKRKLEDECSELKRDIDDL 959
Cdd:COG5185 101 EYVNSLiklPNYEWSADILISLLYLYKSEIVALKDELikvekldeiADIEASYGEVETGIIKDIFGKLTQELNQNLKKLE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 960 ELTLAKVEK------EKHATE---NKVKNLTEEMAGLDEIIaKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLE 1030
Cdd:COG5185 181 IFGLTLGLLkgiselKKAEPSgtvNSIKESETGNLGSESTL-LEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1031 QQVDDLEGSLEQEKKVRM-DLERAKRKLEGDLKLTQESI------MDLENDKLQLEEKLKKKEFD------ISQQNSKIE 1097
Cdd:COG5185 260 EQNTDLRLEKLGENAESSkRLNENANNLIKQFENTKEKIaeytksIDIKKATESLEEQLAAAEAEqeleesKRETETGIQ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1098 DEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSdLSRELEEISERLEEAGGATSVQIEMNKKREA------ 1171
Cdd:COG5185 340 NLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDS-FKDTIESTKESLDEIPQNQRGYAQEILATLEdtlkaa 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1172 --EFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQ-RVKQKLEKEKSEFKLELDDVTSNMEQIIKA----K 1244
Cdd:COG5185 419 drQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQsRLEEAYDEINRSVRSKKEDLNEELTQIESRvstlK 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1245 ANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEK---------EALISQLTRGKLSYTQQTE 1315
Cdd:COG5185 499 ATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELiqasnaktdGQAANLRTAVIDELTQYLS 578
|
570
....*....|....
gi 431907173 1316 DLKRQLEEEGKAKN 1329
Cdd:COG5185 579 TIESQQAREDPIPD 592
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
951-1901 |
2.76e-09 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 63.15 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 951 ELKRDIDdleltlakvekEKHATENKVKNLTEEMAGLDEII--------AKLTKEKKALQEAHQQALDDLQAE-EDKVNT 1021
Cdd:TIGR01612 480 DIKKDID-----------ENSKQDNTVKLILMRMKDFKDIIdfmelykpDEVPSKNIIGFDIDQNIKAKLYKEiEAGLKE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1022 LTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKL-EGDLKLTQESIMdLENDKLQLEEKLKkkefDISQQNSKIEDeq 1100
Cdd:TIGR01612 549 SYELAKNWKKLIHEIKKELEEENEDSIHLEKEIKDLfDKYLEIDDEIIY-INKLKLELKEKIK----NISDKNEYIKK-- 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1101 alALQLQKKLKENQARIEELEEELEAERTARAK-VEKLRSDLSRELEEISE-RLEEAGGATSVQIEMN------------ 1166
Cdd:TIGR01612 622 --AIDLKKIIENNNAYIDELAKISPYQVPEHLKnKDKIYSTIKSELSKIYEdDIDALYNELSSIVKENaidntedkakld 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1167 ---KKREAEFQKMRrDLEEATLQ-HEATAAALRKKHADSVAEL-----GEQIDNLQRVKQKLEKEKSEFKLELDDVTSNM 1237
Cdd:TIGR01612 700 dlkSKIDKEYDKIQ-NMETATVElHLSNIENKKNELLDIIVEIkkhihGEINKDLNKILEDFKNKEKELSNKINDYAKEK 778
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1238 EQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLTRGKLSYTQQTEDL 1317
Cdd:TIGR01612 779 DELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNC 858
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1318 KRQLEEEGKAKNALAHALQSARHDcDLLREQYEEETEAKAELQRVLSKANSEVAQWRTkyetdaiqrteeleeakLQDAE 1397
Cdd:TIGR01612 859 KEKIDSEHEQFAELTNKIKAEISD-DKLNDYEKKFNDSKSLINEINKSIEEEYQNINT-----------------LKKVD 920
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1398 EAVEAVNAKCSSLEK--TKHRLQNEIEDLMVDVersnaaaaaldkkQRNFDKILAEWKQKYEesqselessqkeaRSLST 1475
Cdd:TIGR01612 921 EYIKICENTKESIEKfhNKQNILKEILNKNIDT-------------IKESNLIEKSYKDKFD-------------NTLID 974
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1476 ELFKLKNAYEESleHLETFKRENKNLQEEISDLTEQLGEGGKNVhelekvrkqleaekleLQSALEEAEASLEHEEGKIL 1555
Cdd:TIGR01612 975 KINELDKAFKDA--SLNDYEAKNNELIKYFNDLKANLGKNKENM----------------LYHQFDEKEKATNDIEQKIE 1036
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1556 RAQLEFNQIKAEIERKLAEKDEEMEQAKRNHlrvVDSLQTSL--DAETRSRNealrvkkkmegdLNEMEIQLSQANRTAS 1633
Cdd:TIGR01612 1037 DANKNIPNIEIAIHTSIYNIIDEIEKEIGKN---IELLNKEIleEAEINITN------------FNEIKEKLKHYNFDDF 1101
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1634 EAQKHLKIAQahlkDTQLQMDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTER-SRKLAEQELIETSERVQll 1712
Cdd:TIGR01612 1102 GKEENIKYAD----EINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDvADKAISNDDPEEIEKKI-- 1175
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1713 hsQN-TSLINQKKKMESDLTQLQSEVEE------AVQECRNAEEKAKKAItdAAMMAEELKKEQDTSAHlerMKKNMEQT 1785
Cdd:TIGR01612 1176 --ENiVTKIDKKKNIYDEIKKLLNEIAEiekdktSLEEVKGINLSYGKNL--GKLFLEKIDEEKKKSEH---MIKAMEAY 1248
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1786 IKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAE----QKRNAESVKGMRKSERRI--------------KEL- 1846
Cdd:TIGR01612 1249 IEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDhhiiSKKHDENISDIREKSLKIiedfseesdindikKELq 1328
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 431907173 1847 TYQTEEDKKN------LLRLQDLVDKLQL--------KVKAYKRQAEEAEEQANTNLSKFRKVQHELDE 1901
Cdd:TIGR01612 1329 KNLLDAQKHNsdinlyLNEIANIYNILKLnkikkiidEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD 1397
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1611-1832 |
2.82e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1611 KKKMEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKENIAIVERRNNLLQAELEELRAvvEQ 1690
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA--EL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1691 TERSRKLAE-----QELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEEL 1765
Cdd:COG4942 100 EAQKEELAEllralYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1766 KKEQDTS-AHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELENELEAEQKRNAES 1832
Cdd:COG4942 180 LAELEEErAALEALKAERQKLLARLEKELAELAA-ELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1009-1443 |
2.86e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1009 LDDLQAEEDKVntLTKSKVKLEQQVDDLEgSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFD 1088
Cdd:COG4717 48 LERLEKEADEL--FKPQGRKPELNLKELK-ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1089 ISQQNSKIEDEQalalqLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKK 1168
Cdd:COG4717 125 LQLLPLYQELEA-----LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1169 REAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELgeqidNLQRVKQKLEKEKSEFKL---------ELDDVTSNMEQ 1239
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERLKEARLLLLIaaallallgLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1240 I------------------IKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALIS 1301
Cdd:COG4717 275 IagvlflvlgllallflllAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1302 QLTRGKLSYT-QQTEDLKRQLEEEGKAKN--ALAHALQSArhdcdllrEQYEEETEAKAELQRVLSKANSEVAQWRTKYE 1378
Cdd:COG4717 355 EAEELEEELQlEELEQEIAALLAEAGVEDeeELRAALEQA--------EEYQELKEELEELEEQLEELLGELEELLEALD 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1379 TDAIqrteeleEAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLmvdvERSNAAAAALDKKQR 1443
Cdd:COG4717 427 EEEL-------EEELEELEEELEELEEELEELREELAELEAELEQL----EEDGELAELLQELEE 480
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1065-1292 |
2.93e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1065 QESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRE 1144
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1145 LEEISERLEE-------AGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRkkhadsvaelgEQIDNLQRVKQ 1217
Cdd:COG4942 99 LEAQKEELAEllralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR-----------ADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1218 KLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQ 1292
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
917-1684 |
2.97e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 62.93 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 917 LEAKVKEMNERLEDEEEMNAELTAKKRkledecSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTK 996
Cdd:pfam12128 263 LHFGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLD 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 997 EKKALQEAHQQALDDLQAE-----------EDKVNTLT------KSKVKlEQQVDDLEGSLEQEKKVRMDLERAKRKLEG 1059
Cdd:pfam12128 337 ADIETAAADQEQLPSWQSElenleerlkalTGKHQDVTakynrrRSKIK-EQNNRDIAGIKDKLAKIREARDRQLAVAED 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1060 DLKlTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALAlqlQKKLKENQARIEELEEELEAERT-ARAKVEKLR 1138
Cdd:pfam12128 416 DLQ-ALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATA---TPELLLQLENFDERIERAREEQEaANAEVERLQ 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1139 SDLsRELEEISERLEEAGGATSVQIEMNKKREAEFQKMrRDLEEATLQHeataaALRKKHADSVAELGEQIDNLQRVKQK 1218
Cdd:pfam12128 492 SEL-RQARKRRDQASEALRQASRRLEERQSALDELELQ-LFPQAGTLLH-----FLRKEAPDWEQSIGKVISPELLHRTD 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1219 LEKEKSE-----------FKLELDDVTSN----MEQIIKAKanLEKVSRTL----------EDQANEYRTKLEEAQRSLn 1273
Cdd:pfam12128 565 LDPEVWDgsvggelnlygVKLDLKRIDVPewaaSEEELRER--LDKAEEALqsarekqaaaEEQLVQANGELEKASREE- 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1274 dfTTQQAKLQTENGELARQLEEKEALISQLTRGKLSYTQQTEDLKRQLEEEgkaKNALAHALQSARHDCDllREQYEEET 1353
Cdd:pfam12128 642 --TFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQ---LKQLDKKHQAWLEEQK--EQKREART 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1354 EAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKLQDAEEAveavnAKCSSLEKTKHRLQNEIEDLMVDVERsna 1433
Cdd:pfam12128 715 EKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDL-----ASLGVDPDVIAKLKREIRTLERKIER--- 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1434 aAAALDKKQRNFDKILAE-WKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDlteql 1512
Cdd:pfam12128 787 -IAVRRQEVLRYFDWYQEtWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSE----- 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1513 geggknvhELEKVRKQLEA-EKLELQSALEEAEASLEHEegkilRAQLEfnqikaEIERKLAEKDEEMEQAKRNHLRVVD 1591
Cdd:pfam12128 861 --------NLRGLRCEMSKlATLKEDANSEQAQGSIGER-----LAQLE------DLKLKRDYLSESVKKYVEHFKNVIA 921
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1592 SLQTSLDAET--RSRNEALRVKKKMEGDLNEMEI--QLSQ-ANRTASEAQKHLKiAQAHLKDtqLQMDDAVRANDDLKEN 1666
Cdd:pfam12128 922 DHSGSGLAETweSLREEDHYQNDKGIRLLDYRKLvpYLEQwFDVRVPQSIMVLR-EQVSILG--VDLTEFYDVLADFDRR 998
|
810
....*....|....*...
gi 431907173 1667 IAIVERRnnlLQAELEEL 1684
Cdd:pfam12128 999 IASFSRE---LQREVGEE 1013
|
|
| SH3_FCHSD_2 |
cd11762 |
Second Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of ... |
1929-1980 |
3.19e-09 |
|
Second Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of FCH and double SH3 domains protein 1 (FCHSD1) and FCHSD2. These proteins have a common domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. They have only been characterized in silico and their functions remain unknown. This group also includes the insect protein, nervous wreck, which acts as a regulator of synaptic growth signaling. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212696 [Multi-domain] Cd Length: 57 Bit Score: 54.71 E-value: 3.19e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 431907173 1929 LARALYDNTAESPQELSFRRGDVLRVLQREGAGGLDGWCLCSLHGQQGIVPA 1980
Cdd:cd11762 1 LVRALYDYEAQSDEELSFPEGAIIRILRKDDNGVDDGWWEGEFNGRVGVFPS 52
|
|
| SH3_GRB2_like_C |
cd11805 |
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related ... |
1929-1984 |
3.20e-09 |
|
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related proteins; This family includes the adaptor protein GRB2 and related proteins including Drosophila melanogaster Downstream of receptor kinase (DRK), Caenorhabditis elegans Sex muscle abnormal protein 5 (Sem-5), GRB2-related adaptor protein (GRAP), GRAP2, and similar proteins. Family members contain an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. GRB2/Sem-5/DRK is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. GRAP2 plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. GRAP acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. The C-terminal SH3 domains (SH3c) of GRB2 and GRAP2 have been shown to bind to classical PxxP motif ligands, as well as to non-classical motifs. GRB2 SH3c binds Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, while the SH3c of GRAP2 binds to the phosphatase-like protein HD-PTP via a RxxxxK motif. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212739 [Multi-domain] Cd Length: 53 Bit Score: 54.56 E-value: 3.20e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1929 LARALYDNTAESPQELSFRRGDVLRVLQREGAGGLDGwclcSLHGQQGIVPANRVK 1984
Cdd:cd11805 1 RVQALYDFNPQEPGELEFRRGDIITVLDSSDPDWWKG----ELRGRVGIFPANYVQ 52
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1664-1932 |
3.91e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1664 KENIAIVE--RRNNLLQAELEELRAVVEQ-------TERsRKLAEQELIETSE---RVQLLHSQntslinQKKKMESdlT 1731
Cdd:TIGR02168 135 KRSYSIIEqgKISEIIEAKPEERRAIFEEaagiskyKER-RKETERKLERTREnldRLEDILNE------LERQLKS--L 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1732 QLQSEVEEAVQECRNAEEKAKKAItdAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKL 1811
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELAL--LVLRLEELREELEE---LQEELKEAEEELEELTAELQELEE--------KLEEL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1812 EARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLV-------DKLQLKVKAYKRQAEEAEEQ 1884
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLeelesklDELAEELAELEEKLEELKEE 352
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 431907173 1885 ANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKAQLARA 1932
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
853-1035 |
4.33e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 59.55 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 853 NMKEEFGRLKEtLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNERLE-DE 931
Cdd:COG1579 1 AMPEDLRALLD-LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 932 EEMNAELTAKKRK-LEDECSELKRDIDDLEltlakvEKEKHATEnKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALD 1010
Cdd:COG1579 80 EQLGNVRNNKEYEaLQKEIESLKRRISDLE------DEILELME-RIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170 180
....*....|....*....|....*
gi 431907173 1011 DLQAEEDKvntLTKSKVKLEQQVDD 1035
Cdd:COG1579 153 ELEAELEE---LEAEREELAAKIPP 174
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
923-1341 |
4.58e-09 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 61.24 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 923 EMNERLEDEEEMNAELTAKKRKLEDECSEL---KRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKK 999
Cdd:pfam19220 14 EMADRLEDLRSLKADFSQLIEPIEAILRELpqaKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1000 ALQEAHQQAldDLQAEEDKVNTLTKskvklEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLE 1079
Cdd:pfam19220 94 KLEAALREA--EAAKEELRIELRDK-----TAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1080 EKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARieeleeeleaERTARAKVEKLRSDLSRELEEiSERLEEAggat 1159
Cdd:pfam19220 167 ERLALLEQENRRLQALSEEQAAELAELTRRLAELETQ----------LDATRARLRALEGQLAAEQAE-RERAEAQ---- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1160 svQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKhADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQ 1239
Cdd:pfam19220 232 --LEEAVEAHRAERASLRMKLEALTARAAATEQLLAEA-RNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLER 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1240 IIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKealisqltrgKLSYTQQTEDLKR 1319
Cdd:pfam19220 309 RTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVE----------RAALEQANRRLKE 378
|
410 420
....*....|....*....|...
gi 431907173 1320 QLEEEgKAKNALAH-ALQSARHD 1341
Cdd:pfam19220 379 ELQRE-RAERALAQgALEIARES 400
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
843-1302 |
5.69e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.59 E-value: 5.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 843 KSAETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVK 922
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 923 EMNERLEDEEEMNAeltakkrklEDECSELKRDIDDLELTLAKVEKEkhatenkvknltEEMAGLDEIIAKLTKEKKALQ 1002
Cdd:PRK02224 437 TARERVEEAEALLE---------AGKCPECGQPVEGSPHVETIEEDR------------ERVEELEAELEDLEEEVEEVE 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1003 EAHQQAlDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEkkvrmdlerakrklegdlkltQESIMDLENDKLQLEEKL 1082
Cdd:PRK02224 496 ERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEK---------------------RERAEELRERAAELEAEA 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1083 KKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEeleeeleaertaraKVEKLRSDLSrELEEISERLEEAGGATSVQ 1162
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE--------------SLERIRTLLA-AIADAEDEIERLREKREAL 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1163 IEMNKKRE---AEFQKMRRDLEEATLQHEATAAALRKKHADSVaelgeqidnLQRVKQKLEkEKSEFKLELDDVTSNMEQ 1239
Cdd:PRK02224 619 AELNDERRerlAEKRERKRELEAEFDEARIEEAREDKERAEEY---------LEQVEEKLD-ELREERDDLQAEIGAVEN 688
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1240 IIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTEN-GELARQLEEKEALISQ 1302
Cdd:PRK02224 689 ELEELEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRNvETLERMLNETFDLVYQ 752
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
861-1424 |
6.20e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.90 E-value: 6.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 861 LKETLEKSEARRKELEEkmvsllqeknDLQLQVQAEQdNLNDAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTA 940
Cdd:PRK04863 511 LAEQLQQLRMRLSELEQ----------RLRQQQRAER-LLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARE 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 941 KKRKLEDECSELKRDIDdlelTLAKVEKEKHATENKVKNLTEEM-------AGLDEIIAKLTKEKKALQ------EAHQQ 1007
Cdd:PRK04863 580 RRMALRQQLEQLQARIQ----RLAARAPAWLAAQDALARLREQSgeefedsQDVTEYMQQLLERERELTverdelAARKQ 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1008 ALDD----LQ----AEEDKVNTL--TKSKVKLEQQVDDLE-----------GSLEQEKKVRmDLERAKRKLEG------D 1060
Cdd:PRK04863 656 ALDEeierLSqpggSEDPRLNALaeRFGGVLLSEIYDDVSledapyfsalyGPARHAIVVP-DLSDAAEQLAGledcpeD 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1061 LKLTQESIMDLENDKLQLEEKLKkkefDISQQNSKIedeqalalqlqkklkenQARIEELEEELEAERTARakvEKLRSD 1140
Cdd:PRK04863 735 LYLIEGDPDSFDDSVFSVEELEK----AVVVKIADR-----------------QWRYSRFPEVPLFGRAAR---EKRIEQ 790
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1141 LSRELEEISERLEeaggatsvqiemnkKREAEFQKMRR---DLEEATLQH---------EATAAALRKKHADSVAELGEQ 1208
Cdd:PRK04863 791 LRAEREELAERYA--------------TLSFDVQKLQRlhqAFSRFIGSHlavafeadpEAELRQLNRRRVELERALADH 856
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1209 IDNLQRVKQKLEKEKSEFKLelddvtsnMEQIIKAKANLEKvsRTLEDQANEYRTKLEEAQ----------RSLNDFTTQ 1278
Cdd:PRK04863 857 ESQEQQQRSQLEQAKEGLSA--------LNRLLPRLNLLAD--ETLADRVEEIREQLDEAEeakrfvqqhgNALAQLEPI 926
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1279 QAKLQTENGELA---RQLEEKEALISQLTRGK--LSYTQQT------EDLKRQLEEEGKAKNALAHALQSARHDCDLLRE 1347
Cdd:PRK04863 927 VSVLQSDPEQFEqlkQDYQQAQQTQRDAKQQAfaLTEVVQRrahfsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRARE 1006
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1348 QYEEETEAKAELQRVLSKANSEvaqWRTKYET--DAIQR--------TEELEEAKLQDAEEAVEAVNA---KCSSLEKTK 1414
Cdd:PRK04863 1007 QLRQAQAQLAQYNQVLASLKSS---YDAKRQMlqELKQElqdlgvpaDSGAEERARARRDELHARLSAnrsRRNQLEKQL 1083
|
650
....*....|
gi 431907173 1415 HRLQNEIEDL 1424
Cdd:PRK04863 1084 TFCEAEMDNL 1093
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1986-2233 |
6.32e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 61.88 E-value: 6.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1986 LPAGPTPKPSlsqvPPAEPGSPYPAPEhsnedqEVYVVPPPAR---PCLTSESPAGPCLPSP-DPIYKVPRGSGTQPATP 2061
Cdd:PHA03247 2750 TPGGPARPAR----PPTTAGPPAPAPP------AAPAAGPPRRltrPAVASLSESRESLPSPwDPADPPAAVLAPAAALP 2819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2062 GDALEVYDVPP--AALRVSASGPYDTPASFSHLLARVAP-----------QPPGEDEAPYDVPL------APKPPSELEP 2122
Cdd:PHA03247 2820 PAASPAGPLPPptSAQPTAPPPPPGPPPPSLPLGGSVAPggdvrrrppsrSPAAKPAAPARPPVrrlarpAVSRSTESFA 2899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2123 DLEWEGGREPGPPLYAAPSNLKRASAllnlyeAPEELLADGEEGGSDegiydvPLLGPETPPSPEPLGALASNDPDTLAL 2202
Cdd:PHA03247 2900 LPPDQPERPPQPQAPPPPQPQPQPPP------PPQPQPPPPPPPRPQ------PPLAPTTDPAGAGEPSGAVPQPWLGAL 2967
|
250 260 270
....*....|....*....|....*....|.
gi 431907173 2203 LLARSPPPshRPRLPSaeslsrrPLPALPVP 2233
Cdd:PHA03247 2968 VPGRVAVP--RFRVPQ-------PAPSREAP 2989
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
931-1420 |
6.70e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 6.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 931 EEEMNAELTAKKRKLEDECSELKRDIDDLElTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALqEAHQQALD 1010
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1011 DLQAEEDKVNTLTKSKVKLEQqvddlegsLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDK-LQLEEKLKKKEFDI 1089
Cdd:COG4717 130 LYQELEALEAELAELPERLEE--------LEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1090 SQQNSKIEDEQALALQLQKKLKENQARIEELeeeleaertaraKVEKLRSDLSRELEEISERLeeAGGATSVQIEMNKKR 1169
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQL------------ENELEAAALEERLKEARLLL--LIAAALLALLGLGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1170 EAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVK----QKLEKEKSEFKLELDDVTSNMEQIIKAKA 1245
Cdd:COG4717 268 LLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEeleeEELEELLAALGLPPDLSPEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1246 NLEKVSRTLEDQANEYRTKLEEAQRSlNDFTTQQAKLQTENGELARQLEEKEALISQLtrgklsytqqtEDLKRQLEEEG 1325
Cdd:COG4717 348 ELQELLREAEELEEELQLEELEQEIA-ALLAEAGVEDEEELRAALEQAEEYQELKEEL-----------EELEEQLEELL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1326 KAKNALAHALQSARHDCDL--LREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKLQDAEEAVEAV 1403
Cdd:COG4717 416 GELEELLEALDEEELEEELeeLEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAAL 495
|
490
....*....|....*..
gi 431907173 1404 NAKCSSLEKTKHRLQNE 1420
Cdd:COG4717 496 KLALELLEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1642-1893 |
8.06e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 8.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1642 AQAHLKDTQLQMDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQllhsqntSLIN 1721
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1722 QKKKMESDLTQLQSEVEEAVqecRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQI-- 1799
Cdd:COG4942 91 EIAELRAELEAQKEELAELL---RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALra 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1800 ALKGGKKQLQKLEARVRELENELEAEQKRNAESVKgmrKSERRIKELTYQTEEDKKNLLRLQDLVDKLQlkvkayKRQAE 1879
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLE------AEAAA 238
|
250
....*....|....
gi 431907173 1880 EAEEQANTNLSKFR 1893
Cdd:COG4942 239 AAERTPAAGFAALK 252
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
2000-2231 |
8.84e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 61.49 E-value: 8.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2000 PPAEPGSPYPAPEHSnedqevyvVPPPaRPcltSESPAGPCLPSPDPIYKVPRGSgTQPATPGDAlevYDVPPAALRVSA 2079
Cdd:PHA03247 2553 PPLPPAAPPAAPDRS--------VPPP-RP---APRPSEPAVTSRARRPDAPPQS-ARPRAPVDD---RGDPRGPAPPSP 2616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2080 SGPYDTPASfshllarvaPQPPGEDEAPYDVP---LAPKPPSElEPDLEWEGGREPGPPLYAAPSNLKRASAllnlyeap 2156
Cdd:PHA03247 2617 LPPDTHAPD---------PPPPSPSPAANEPDphpPPTVPPPE-RPRDDPAPGRVSRPRRARRLGRAAQASS-------- 2678
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 2157 eelladgeeggsdegiydvPLLGPETPPSPEPLGALASndpdtlallLARSPPPSHRPRLPSAESLSRRPLPALP 2231
Cdd:PHA03247 2679 -------------------PPQRPRRRAARPTVGSLTS---------LADPPPPPPTPEPAPHALVSATPLPPGP 2725
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
862-1691 |
1.24e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.74 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 862 KETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQliKNKI-QLEAKVKEMNERLEDEE-------E 933
Cdd:PRK04863 299 RRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQ--QEKIeRYQADLEELEERLEEQNevveeadE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 934 MNAELTAKKRKLEDECSELKRDIDDL-------------------------------ELTLAKVEKEKHATENKVKNLTE 982
Cdd:PRK04863 377 QQEENEARAEAAEEEVDELKSQLADYqqaldvqqtraiqyqqavqalerakqlcglpDLTADNAEDWLEEFQAKEQEATE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 983 EMAGL-------DEIIAKLTKEKKALQ---------EAHQQALDDL-QAEEDKVntLTKSKVKLEQQVDDLEGSLEQEKk 1045
Cdd:PRK04863 457 ELLSLeqklsvaQAAHSQFEQAYQLVRkiagevsrsEAWDVARELLrRLREQRH--LAEQLQQLRMRLSELEQRLRQQQ- 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1046 vrmDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKkkefDISQQnskIEDEQALALQLQKKLKENQARIEELEEELE 1125
Cdd:PRK04863 534 ---RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLE----SLSES---VSEARERRMALRQQLEQLQARIQRLAARAP 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1126 AERTARAKVEKLRSDLSRELEEiSERLEEAggatsVQIEMNKKREAEFQK-----MRRDLEE--ATLQHEATAAALRKKH 1198
Cdd:PRK04863 604 AWLAAQDALARLREQSGEEFED-SQDVTEY-----MQQLLERERELTVERdelaaRKQALDEeiERLSQPGGSEDPRLNA 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1199 -AD-----SVAELGEQI---------------------DNLQRVKQKLEKEksEFKLE-----------LDDVTSNMEQI 1240
Cdd:PRK04863 678 lAErfggvLLSEIYDDVsledapyfsalygparhaivvPDLSDAAEQLAGL--EDCPEdlyliegdpdsFDDSVFSVEEL 755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1241 IKAKANLE-----KVSR-----TLEDQANEYRtkLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISqltrGKLSY 1310
Cdd:PRK04863 756 EKAVVVKIadrqwRYSRfpevpLFGRAAREKR--IEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIG----SHLAV 829
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1311 T------QQTEDLKRQLEEEGKAKNALAHALQSArhdcdllREQYEEETEAKAELQRVLSKANsevaqwrTKYETDAIQR 1384
Cdd:PRK04863 830 AfeadpeAELRQLNRRRVELERALADHESQEQQQ-------RSQLEQAKEGLSALNRLLPRLN-------LLADETLADR 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1385 TEELEEaKLQDAEEAVEAVNAKCSSLEKtkhrlqneIEDLmvdversnaaAAALDKKQRNFDKIlaewKQKYEESQSELE 1464
Cdd:PRK04863 896 VEEIRE-QLDEAEEAKRFVQQHGNALAQ--------LEPI----------VSVLQSDPEQFEQL----KQDYQQAQQTQR 952
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1465 SSQKEARSLsTELFKLKN--AYEESLEHLetfkrenknlqEEISDLTEQLgeggknvheleKVR-KQLEAEKLELQSALE 1541
Cdd:PRK04863 953 DAKQQAFAL-TEVVQRRAhfSYEDAAEML-----------AKNSDLNEKL-----------RQRlEQAEQERTRAREQLR 1009
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1542 EAEAslEHEEGKILRAQLE-----FNQIKAEIERKLAE----KDEEMEQAKRNHLrvvDSLQTSLDAETRSRNEALRVKK 1612
Cdd:PRK04863 1010 QAQA--QLAQYNQVLASLKssydaKRQMLQELKQELQDlgvpADSGAEERARARR---DELHARLSANRSRRNQLEKQLT 1084
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1613 KMEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQlqmdDAVRANDdlkeniaiVERRnnLLQAEL-----EELRAV 1687
Cdd:PRK04863 1085 FCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVL----RLVKDNG--------VERR--LHRRELaylsaDELRSM 1150
|
....
gi 431907173 1688 VEQT 1691
Cdd:PRK04863 1151 SDKA 1154
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1141-1787 |
1.29e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 60.61 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1141 LSRELEEISERLEEaggaTSVQIEMNKKR-EAEFQKMRRDLEeaTLQHEATAAALRKKHADSVAELGE---QIDNLQRVK 1216
Cdd:pfam10174 128 QAKELFLLRKTLEE----MELRIETQKQTlGARDESIKKLLE--MLQSKGLPKKSGEEDWERTRRIAEaemQLGHLEVLL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1217 QKLEKEKSEFKLEL---------DDVTSNMEQIIKAK----ANLEKVSRTLEDQANEYRT-------------KLEEAQR 1270
Cdd:pfam10174 202 DQKEKENIHLREELhrrnqlqpdPAKTKALQTVIEMKdtkiSSLERNIRDLEDEVQMLKTngllhtedreeeiKQMEVYK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1271 SLNDFttqqakLQTENGELARQLEEKEALISQLTRGKLSYTQQTEDLKRQLE---EEGKAKNALAHALQSarhDCDLLRE 1347
Cdd:pfam10174 282 SHSKF------MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEvlkESLTAKEQRAAILQT---EVDALRL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1348 QYEEEteakaelQRVLSKANSEVAQWRTKYETDA-----IQRTEELEEAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIE 1422
Cdd:pfam10174 353 RLEEK-------ESFLNKKTKQLQDLTEEKSTLAgeirdLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVK 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1423 DLMVDVERSNAAAAALDKKQRNFDKILaewkqkyeesqseleSSQKEARSLSTElfklknayeESLEHLETFKRENKNLQ 1502
Cdd:pfam10174 426 SLQTDSSNTDTALTTLEEALSEKERII---------------ERLKEQREREDR---------ERLEELESLKKENKDLK 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1503 EEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEASLEH--EEGKILRAQLefnqikaeierklaEKDEEME 1580
Cdd:pfam10174 482 EKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQkkEECSKLENQL--------------KKAHNAE 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1581 QAKRNHLRVVDSLQTsLDAE-TRSRNEA----------LRVKKKMEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDT 1649
Cdd:pfam10174 548 EAVRTNPEINDRIRL-LEQEvARYKEESgkaqaeverlLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHG 626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1650 QLQM--------DDAVRANDDLKENIAiverrnnllQAELEELRAVVEQTersrklaEQELIETSERV----QLLHSQNT 1717
Cdd:pfam10174 627 QQEMkkkgaqllEEARRREDNLADNSQ---------QLQLEELMGALEKT-------RQELDATKARLsstqQSLAEKDG 690
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1718 SLIN----QKKKMEsdltqlqsEVEEAVQECRNAEEKAKKA-ITDAAMMAEELKKEQDTSAHLERMKKNMEQTIK 1787
Cdd:pfam10174 691 HLTNlraeRRKQLE--------EILEMKQEALLAAISEKDAnIALLELSSSKKKKTQEEVMALKREKDRLVHQLK 757
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1537-1951 |
1.31e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.44 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1537 QSALEEAEASLEHEEGKILRAQLefnqikAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLD--AETRSRNEALRVkkkM 1614
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEKDLHERL------NGLESELAELDEEIERYEEQREQARETRDEADEvlEEHEERREELET---L 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1615 EGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERS 1694
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1695 RKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVE---EAVQECRNAEEKAKKAITDAAmmaEELKKEQDT 1771
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEdrrEEIEELEEEIEELRERFGDAP---VDLGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1772 SAHLERMKKNMEQTIKDLqhrldEAEqialkggkkqLQKLEARVRELENELEA-------EQKRNAESVKGMRKSERRIK 1844
Cdd:PRK02224 414 LEELREERDELREREAEL-----EAT----------LRTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVE 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1845 ELTYQTEEDKKNLLRLQDLVDKLQLKVKAyKRQAEEAEEQANtNLSKFRKVQHE-LDEAEERADIAESQVNKLRAKSRDI 1923
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERRE-DLEELIAERREtIEEKRERAEELRERAAELEAEAEEK 556
|
410 420
....*....|....*....|....*...
gi 431907173 1924 GAKAQLARALYDNTAESPQELSFRRGDV 1951
Cdd:PRK02224 557 REAAAEAEEEAEEAREEVAELNSKLAEL 584
|
|
| SH3_Abi |
cd11826 |
Src homology 3 domain of Abl Interactor proteins; Abl interactor (Abi) proteins are adaptor ... |
1931-1983 |
1.39e-08 |
|
Src homology 3 domain of Abl Interactor proteins; Abl interactor (Abi) proteins are adaptor proteins serving as binding partners and substrates of Abl tyrosine kinases. They are involved in regulating actin cytoskeletal reorganization and play important roles in membrane-ruffling, endocytosis, cell motility, and cell migration. They localize to sites of actin polymerization in epithelial adherens junction and immune synapses, as well as to the leading edge of lamellipodia. Vertebrates contain two Abi proteins, Abi1 and Abi2. Abi1 displays a wide expression pattern while Abi2 is highly expressed in the eye and brain. Abi proteins contain a homeobox homology domain, a proline-rich region, and a SH3 domain. The SH3 domain of Abi binds to a PxxP motif in Abl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212760 [Multi-domain] Cd Length: 52 Bit Score: 52.71 E-value: 1.39e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSLHGQQGIVPANRV 1983
Cdd:cd11826 3 VALYDYTADKDDELSFQEGDIIYVTKKND----DGWYEGVLNGVTGLFPGNYV 51
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1602-1890 |
1.72e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.03 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1602 RSRNEALRVKKKMEGDLNEMEIQLSQaNRTASEAQKHLKIAQAhlKDTQL-----QMDDAVRA------------NDDLK 1664
Cdd:COG3206 91 KSRPVLERVVDKLNLDEDPLGEEASR-EAAIERLRKNLTVEPV--KGSNVieisyTSPDPELAaavanalaeaylEQNLE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1665 ENIAIVERRNNLLQAELEELRAVVEQTERSRK--LAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEeAVQ 1742
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA-ALR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1743 ECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK----------KNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLE 1812
Cdd:COG3206 247 AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQ 326
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1813 ARVRELENELEAEQKRnaesVKGMRKSERRIKELTYQTEEDKKNllrLQDLVDKLQlkvkaykrQAEEAEEQANTNLS 1890
Cdd:COG3206 327 AREASLQAQLAQLEAR----LAELPELEAELRRLEREVEVAREL---YESLLQRLE--------EARLAEALTVGNVR 389
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
863-1095 |
2.03e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 863 ETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKK 942
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 943 RKLEDECSELKRDIddleltlakvekEKHATENKVKNLT-----EEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEED 1017
Cdd:COG4942 100 EAQKEELAELLRAL------------YRLGRQPPLALLLspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1018 KVNTLTKSKVKLEQQVDDLEGSLEQEKKVRmdlERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSK 1095
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1047-1282 |
2.03e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1047 RMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEA 1126
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1127 ERTARAKVEKLRSDLSR--ELEEI--SERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEatlqheatAAALRKKHADSV 1202
Cdd:COG4942 102 QKEELAELLRALYRLGRqpPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE--------LAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1203 AELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSL--NDFTTQQA 1280
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTpaAGFAALKG 253
|
..
gi 431907173 1281 KL 1282
Cdd:COG4942 254 KL 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
841-1057 |
2.12e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 841 LLKSAETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAK 920
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 921 VKEMNERLEDEEEMNAELTAKKRKLEDECS-------------------------ELKRDIDDLELTLAKVEKEKHATEN 975
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPlalllspedfldavrrlqylkylapARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 976 KVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQ--EKKVRMDLERA 1053
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAaaERTPAAGFAAL 251
|
....
gi 431907173 1054 KRKL 1057
Cdd:COG4942 252 KGKL 255
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
845-1015 |
2.37e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 57.24 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 845 AETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKiQLEAKVKEM 924
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-EYEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 925 nerledeeemnAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKhatENKVKNLTEEMAGLDEIIAKLTKEKKALQEA 1004
Cdd:COG1579 99 -----------ESLKRRISDLEDEILELMERIEELEEELAELEAEL---AELEAELEEKKAELDEELAELEAELEELEAE 164
|
170
....*....|.
gi 431907173 1005 HQQALDDLQAE 1015
Cdd:COG1579 165 REELAAKIPPE 175
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1987-2282 |
2.72e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 59.95 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1987 PAGPTPKPSLSQV--PPAEPGSPYPAPEHSnedqeVYVVP-PPARPCLTSESPAGPCLPSPDPIYKVPRGSGTQPATPGD 2063
Cdd:PHA03247 2686 RAARPTVGSLTSLadPPPPPPTPEPAPHAL-----VSATPlPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARP 2760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2064 ALEVYDVPPAALRVSASGPYDT---PASFSHLLAR-VAPQPPgedeAPYDVPLAPKPPSELEPDLEWEGGREPgPPLYAA 2139
Cdd:PHA03247 2761 PTTAGPPAPAPPAAPAAGPPRRltrPAVASLSESReSLPSPW----DPADPPAAVLAPAAALPPAASPAGPLP-PPTSAQ 2835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2140 PSNLKRASALLNLYEAPEELLADGEEGgSDEGIYDVPLLGPETPPSPePLGALASNDPDTLALLLARSPPPSHRPRLPSA 2219
Cdd:PHA03247 2836 PTAPPPPPGPPPPSLPLGGSVAPGGDV-RRRPPSRSPAAKPAAPARP-PVRRLARPAVSRSTESFALPPDQPERPPQPQA 2913
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 431907173 2220 ESlsrRPLPAlPVPEAPSPSPVPSPAPGRKGSiqdrplpPPPPRLPGYGGPKVEGGHHNEYEG 2282
Cdd:PHA03247 2914 PP---PPQPQ-PQPPPPPQPQPPPPPPPRPQP-------PLAPTTDPAGAGEPSGAVPQPWLG 2965
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1499-1923 |
3.13e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 59.07 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1499 KNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALE-EAEASLEHEEGKILRAQLEFNQIK-AEIERKLAEKD 1576
Cdd:pfam10174 174 KKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHrRNQLQPDPAKTKALQTVIEMKDTKiSSLERNIRDLE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1577 EEmeqakrnhlrvVDSLQTSLDAETRSRNEALrvkKKMEGDLNE---MEIQLSQANRTASEAQKHLKIAQAHLKDTQLQM 1653
Cdd:pfam10174 254 DE-----------VQMLKTNGLLHTEDREEEI---KQMEVYKSHskfMKNKIDQLKQELSKKESELLALQTKLETLTNQN 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1654 DDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQ-----TERSRKLAE---------------QELIETSER-VQLL 1712
Cdd:pfam10174 320 SDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEkesflNKKTKQLQDlteekstlageirdlKDMLDVKERkINVL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1713 HSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNaeekakkaiTDAAMMA-EELKKEQDTSahLERMKknmEQTIKDLQH 1791
Cdd:pfam10174 400 QKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSN---------TDTALTTlEEALSEKERI--IERLK---EQREREDRE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1792 RLDEAEQI--ALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDlvdklQL 1869
Cdd:pfam10174 466 RLEELESLkkENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLEN-----QL 540
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1870 KvkaykrQAEEAEEQANTN---LSKFRKVQHELDEAEERADIAESQVNKLRAKSRDI 1923
Cdd:pfam10174 541 K------KAHNAEEAVRTNpeiNDRIRLLEQEVARYKEESGKAQAEVERLLGILREV 591
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
859-1430 |
3.16e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 59.14 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 859 GRLKETLEKSEARRKELEEKMVSL--LQEKNDLQLQV----QAEQDNLNDAEERC----DQLIKNKIQLEAKVKEMNERL 928
Cdd:PRK01156 138 GEMDSLISGDPAQRKKILDEILEInsLERNYDKLKDVidmlRAEISNIDYLEEKLkssnLELENIKKQIADDEKSHSITL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 929 EDEEEMNAELTAKKRKLEDECSELKR------DIDDLELTLAKVEKEKHATE---NKVKNLTEEMAGLD--------EII 991
Cdd:PRK01156 218 KEIERLSIEYNNAMDDYNNLKSALNElssledMKNRYESEIKTAESDLSMELeknNYYKELEERHMKIIndpvyknrNYI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 992 AKLTKEKKALqEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEgsleqEKKVRM-DLERAKRKLEGDLKLTQESIMD 1070
Cdd:PRK01156 298 NDYFKYKNDI-ENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYI-----KKKSRYdDLNNQILELEGYEMDYNSYLKS 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1071 LENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEaerTARAKVEKLRSDLSrELEEISE 1150
Cdd:PRK01156 372 IESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS---SLNQRIRALRENLD-ELSRNME 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1151 RLEEAG-----GATSVQIEMNKKREAEFQKMRRdLEEATLQHEATAAALRKKHADSVAEL----GEQIDNLQRVKQKLEK 1221
Cdd:PRK01156 448 MLNGQSvcpvcGTTLGEEKSNHIINHYNEKKSR-LEEKIREIEIEVKDIDEKIVDLKKRKeyleSEEINKSINEYNKIES 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1222 EKSEFKLELDDVTSNMEQIIKAKANLEKV-SRTLEDQANEYRTKLEE-AQRSLNDFTTqqakLQTENGELARQLEEKEAL 1299
Cdd:PRK01156 527 ARADLEDIKIKINELKDKHDKYEEIKNRYkSLKLEDLDSKRTSWLNAlAVISLIDIET----NRSRSNEIKKQLNDLESR 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1300 ISQLTRGKLSYTQQTEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQ---YEEETEAKAELQRVLSKANSEVAQWRT- 1375
Cdd:PRK01156 603 LQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKidnYKKQIAEIDSIIPDLKEITSRINDIEDn 682
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1376 -KYETDAIQRT-------EELEEAKLQDAEEAVEAVNAKCSSLEKTKhrlqnEIEDLMVDVER 1430
Cdd:PRK01156 683 lKKSRKALDDAkanrarlESTIEILRTRINELSDRINDINETLESMK-----KIKKAIGDLKR 740
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
982-1864 |
3.60e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 982 EEMAGLDEIIAKLTKEK---KALQEAHQQALDDLQAEEDkvnTLTKSKVKLEQQVDDLEGSL----------EQEKKVRM 1048
Cdd:PRK04863 279 NERRVHLEEALELRRELytsRRQLAAEQYRLVEMARELA---ELNEAESDLEQDYQAASDHLnlvqtalrqqEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1049 DLERAKRKLEGDLKLTQESimdlENDKLQLEEKLKKKEFDISQQNSKIED-EQALALQLQKKLKENQARieeleeeleae 1127
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEA----DEQQEENEARAEAAEEEVDELKSQLADyQQALDVQQTRAIQYQQAV----------- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1128 rTARAKVEKLRSDLSRELEEISERLEEAggATSVQIEMNKKREAEfQKMRrDLEEATLQHEATAAALRKkhadsvaeLGE 1207
Cdd:PRK04863 421 -QALERAKQLCGLPDLTADNAEDWLEEF--QAKEQEATEELLSLE-QKLS-VAQAAHSQFEQAYQLVRK--------IAG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1208 QID--NLQRVKQKLEKEKSEFKLELddvtsnmEQIIKAKANLEKVSRTLEDQANeyrtkleeAQRSLNDFTTQQAKLQTE 1285
Cdd:PRK04863 488 EVSrsEAWDVARELLRRLREQRHLA-------EQLQQLRMRLSELEQRLRQQQR--------AERLLAEFCKRLGKNLDD 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1286 NGELARQLEEKEALISQLTRGKLSYTQQTEDLKRQLEEegkaknalahalqsarhdcdlLREQYEE-ETEAKAELQrvls 1364
Cdd:PRK04863 553 EDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ---------------------LQARIQRlAARAPAWLA---- 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1365 kANSEVAQWRTKYEtDAIQRTEELEEAKLQDAEEAVEAVNAKcSSLEKTKHRLQNEIEDLmvdverSNAAAAALDKKQRn 1444
Cdd:PRK04863 608 -AQDALARLREQSG-EEFEDSQDVTEYMQQLLERERELTVER-DELAARKQALDEEIERL------SQPGGSEDPRLNA- 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1445 fdkiLAEwkqkyeesqselessqKEARSLSTELFK---LKNA-YEESL----------EHLETFKRENKNLQEEISDL-- 1508
Cdd:PRK04863 678 ----LAE----------------RFGGVLLSEIYDdvsLEDApYFSALygparhaivvPDLSDAAEQLAGLEDCPEDLyl 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1509 ----TEQLGEGGKNVHELEK----------VR----------------KQLEAEKLELQSaLEEAEASLEHEEGKILRAQ 1558
Cdd:PRK04863 738 iegdPDSFDDSVFSVEELEKavvvkiadrqWRysrfpevplfgraareKRIEQLRAEREE-LAERYATLSFDVQKLQRLH 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1559 LEFNQIkaeIERKLA---EKDEEMEQAKRNhlrvvdslqtsldaetRSRNEALRVKKKMEGDLNEMEIQLSQANRTASEA 1635
Cdd:PRK04863 817 QAFSRF---IGSHLAvafEADPEAELRQLN----------------RRRVELERALADHESQEQQQRSQLEQAKEGLSAL 877
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1636 QKHLK----IAQAHLKD----TQLQMDDAVRANDDLKEN---IAIVERRNNLLQA---ELEELRAVVEQTERSRKLAEQE 1701
Cdd:PRK04863 878 NRLLPrlnlLADETLADrveeIREQLDEAEEAKRFVQQHgnaLAQLEPIVSVLQSdpeQFEQLKQDYQQAQQTQRDAKQQ 957
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1702 LIETSERVQLLH----SQNTSLINQkkkmESDLT-QLQSEVEEAVQECRNAEEKAKKA---ITDAAMMAEELKKEQDTsa 1773
Cdd:PRK04863 958 AFALTEVVQRRAhfsyEDAAEMLAK----NSDLNeKLRQRLEQAEQERTRAREQLRQAqaqLAQYNQVLASLKSSYDA-- 1031
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1774 hLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAE---QKRNAES-VKGMRKSERRIKELTYQ 1849
Cdd:PRK04863 1032 -KRQMLQELKQELQDLGVPADSGAEERARARRDELHARLSANRSRRNQLEKQltfCEAEMDNlTKKLRKLERDYHEMREQ 1110
|
970
....*....|....*
gi 431907173 1850 TEEDKKNLLRLQDLV 1864
Cdd:PRK04863 1111 VVNAKAGWCAVLRLV 1125
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1378-1957 |
3.65e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 59.14 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1378 ETDAIQRTEELEEAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEwKQKYE 1457
Cdd:PRK01156 198 ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEK-NNYYK 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1458 ESQSELESSQKEA----RSLSTELFKLKNayeesleHLETFKRENKNLQEEISDLTEQLgeggKNVHELEKVRKQLEAEK 1533
Cdd:PRK01156 277 ELEERHMKIINDPvyknRNYINDYFKYKN-------DIENKKQILSNIDAEINKYHAII----KKLSVLQKDYNDYIKKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1534 LELQSaLEEAEASLEHEEGKILRAQLEFNQIKAEIErklaEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKK 1613
Cdd:PRK01156 346 SRYDD-LNNQILELEGYEMDYNSYLKSIESLKKKIE----EYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQD 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1614 MEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLK----DTQLQMDDAVRanddlkeniaIVERRNNllqaELEELRAVVE 1689
Cdd:PRK01156 421 ISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcGTTLGEEKSNH----------IINHYNE----KKSRLEEKIR 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1690 QTERSRKLAEQELIETSERVQLLHSQNTS-LINQKKKMESDLTQLQsEVEEAVQECRNAEEKAKKAITDAAMMAEELKKE 1768
Cdd:PRK01156 487 EIEIEVKDIDEKIVDLKKRKEYLESEEINkSINEYNKIESARADLE-DIKIKINELKDKHDKYEEIKNRYKSLKLEDLDS 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1769 QDTSaHLERMKKNMEQTIKDLQHRLDEAeqialkggKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIkelty 1848
Cdd:PRK01156 566 KRTS-WLNALAVISLIDIETNRSRSNEI--------KKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNL----- 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1849 qteEDKKNLLR-LQDLVDKLQLKVKAYKRQaeeaeeqantnLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKA 1927
Cdd:PRK01156 632 ---NNKYNEIQeNKILIEKLRGKIDNYKKQ-----------IAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANR 697
|
570 580 590
....*....|....*....|....*....|
gi 431907173 1928 QLARALYDNTAESPQELSFRRGDVLRVLQR 1957
Cdd:PRK01156 698 ARLESTIEILRTRINELSDRINDINETLES 727
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
873-1225 |
3.72e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.99 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 873 KELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSEL 952
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 953 KRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQ 1032
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1033 VDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKE 1112
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1113 NQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAA 1192
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350
....*....|....*....|....*....|...
gi 431907173 1193 ALRKKHADSVAELGEQIDNLQRVKQKLEKEKSE 1225
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| SH3_Ysc84p_like |
cd11842 |
Src homology 3 domain of Ysc84p and similar fungal proteins; This family is composed of the ... |
1930-1985 |
4.02e-08 |
|
Src homology 3 domain of Ysc84p and similar fungal proteins; This family is composed of the Saccharomyces cerevisiae proteins, Ysc84p (also called LAS17-binding protein 4, Lsb4p) and Lsb3p, and similar fungal proteins. They contain an N-terminal SYLF domain (also called DUF500) and a C-terminal SH3 domain. Ysc84p localizes to actin patches and plays an important in actin polymerization during endocytosis. The N-terminal domain of both Ysc84p and Lsb3p can bind and bundle actin filaments. A study of the yeast SH3 domain interactome predicts that the SH3 domains of Lsb3p and Lsb4p may function as molecular hubs for the assembly of endocytic complexes. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212776 [Multi-domain] Cd Length: 55 Bit Score: 51.66 E-value: 4.02e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQRegAGGLDGWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd11842 2 AVALYDFAGEQPGDLAFQKGDIITILKK--SDSQNDWWTGRIGGREGIFPANYVEL 55
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1982-2225 |
4.43e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 59.18 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1982 RVKLLPAGPTPKPSLSQVPPAEPGSPYPAPEHSNEDQEVYVVPPPARPCLTSESPA---GPCLPSPDPiYKVPRGSGTQP 2058
Cdd:PHA03247 2882 PVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPrpqPPLAPTTDP-AGAGEPSGAVP 2960
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2059 ATPGDALEVYDVPPAALRVSASGPydtpasfshllARVAPQPPGEDEAPYDVPLAPKPPSELEPDLEweggREPGPplya 2138
Cdd:PHA03247 2961 QPWLGALVPGRVAVPRFRVPQPAP-----------SREAPASSTPPLTGHSLSRVSSWASSLALHEE----TDPPP---- 3021
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2139 apsnlkrASALLNLYEAPEELLADGEEG-GSDEGIYDVPLLGPETPPSPEPLGalASNDPDTLAlLLARSPPPSH--RPR 2215
Cdd:PHA03247 3022 -------VSLKQTLWPPDDTEDSDADSLfDSDSERSDLEALDPLPPEPHDPFA--HEPDPATPE-AGARESPSSQfgPPP 3091
|
250
....*....|
gi 431907173 2216 LPSAESLSRR 2225
Cdd:PHA03247 3092 LSANAALSRR 3101
|
|
| SH3_Nostrin |
cd11823 |
Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in ... |
1931-1983 |
6.21e-08 |
|
Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in endothelial and epithelial cells and is involved in the regulation, trafficking and targeting of endothelial NOS (eNOS). It facilitates the endocytosis of eNOS by coordinating the functions of dynamin and the Wiskott-Aldrich syndrome protein (WASP). Increased expression of Nostrin may be correlated to preeclampsia. Nostrin contains an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212757 [Multi-domain] Cd Length: 53 Bit Score: 51.19 E-value: 6.21e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSLHGQQGIVPANRV 1983
Cdd:cd11823 3 KALYSYTANREDELSLQPGDIIEVHEKQD----DGWWLGELNGKKGIFPATYV 51
|
|
| SH3_2 |
pfam07653 |
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ... |
1930-1986 |
6.46e-08 |
|
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.
Pssm-ID: 429575 [Multi-domain] Cd Length: 54 Bit Score: 51.06 E-value: 6.46e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSLHGQQGIVPANRVKLL 1986
Cdd:pfam07653 2 GRVIFDYVGTDKNGLTLKKGDVVKVLGKDN----DGWWEGETGGRVGLVPSTAVEEI 54
|
|
| SH3_DNMBP_C2_like |
cd11800 |
Second C-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba, and ... |
1932-1981 |
7.82e-08 |
|
Second C-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba, and similar domains; DNMBP or Tuba is a cdc42-specific guanine nucleotide exchange factor (GEF) that contains four N-terminal SH3 domains, a central RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. It provides a functional link between dynamin, Rho GTPase signaling, and actin dynamics. It plays an important role in regulating cell junction configuration. The C-terminal SH3 domains of DNMBP bind to N-WASP and Ena/VASP proteins, which are key regulatory proteins of the actin cytoskeleton. Also included in this subfamily is the second C-terminal SH3 domain of Rho guanine nucleotide exchange factor 37 (ARHGEF37), whose function is still unknown. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212734 [Multi-domain] Cd Length: 57 Bit Score: 50.83 E-value: 7.82e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQREGAGGLDGWCLCSLHGQQGIVPAN 1981
Cdd:cd11800 4 ALYTFEARSPGELSVTEGQVVTVLEKHDLKGNPEWWLVEDRGKQGYVPSN 53
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
1979-2209 |
9.14e-08 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 58.17 E-value: 9.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1979 PANRVKLLPAGPTPKPSLSQ-------VPPAEPGSPYPAPEHSNEDQEVYVVPPPARPCLTSESPAGPCLPSPDPIYKVP 2051
Cdd:PRK10263 336 PVEPVTQTPPVASVDVPPAQptvawqpVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQP 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2052 RGSGTQPATPGDALEVYDVPPAALRVSASGPYDTPASFSHLlarvAPQPPGEDEAPYDVPLAPKPPSELEPDLEWEGGRE 2131
Cdd:PRK10263 416 AQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTF----APQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVE 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 2132 PGPPLyaapSNLKRASALLNLYEAPEELLADGEEGgsdegiydvplLGPETPPSPEPLGALASNDPDTLALLLARSPP 2209
Cdd:PRK10263 492 PEPVV----EETKPARPPLYYFEEVEEKRAREREQ-----------LAAWYQPIPEPVKEPEPIKSSLKAPSVAAVPP 554
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
842-1058 |
9.74e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.72 E-value: 9.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 842 LKSAETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLlqeknDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKV 921
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 922 KEMNERLEDEEEMNAELTAkkrklEDECSELKRDIDDLELTLAkvEKEKHATEN--KVKNLTEEMAGLdeiiakltkeKK 999
Cdd:COG3206 243 AALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELA--ELSARYTPNhpDVIALRAQIAAL----------RA 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 431907173 1000 ALQEAHQQALDDLQAEedkVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLE 1058
Cdd:COG3206 306 QLQQEAQRILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| SH3_GRB2_like_N |
cd11804 |
N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related ... |
1930-1981 |
9.98e-08 |
|
N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related proteins; This family includes the adaptor protein GRB2 and related proteins including Drosophila melanogaster Downstream of receptor kinase (DRK), Caenorhabditis elegans Sex muscle abnormal protein 5 (Sem-5), GRB2-related adaptor protein (GRAP), GRAP2, and similar proteins. Family members contain an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. GRB2/Sem-5/DRK is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. GRAP2 plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. GRAP acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. The N-terminal SH3 domain of GRB2 binds to Sos and Sos-derived proline-rich peptides. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212738 [Multi-domain] Cd Length: 52 Bit Score: 50.43 E-value: 9.98e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGAgglDGWCLCSLHGQQGIVPAN 1981
Cdd:cd11804 2 AVAKHDFKATAEDELSFKKGSILKVLNMEDD---PNWYKAELDGKEGLIPKN 50
|
|
| SH3_OSTF1 |
cd11772 |
Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or ... |
1931-1983 |
1.02e-07 |
|
Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or SH3P2, is a signaling protein containing SH3 and ankyrin-repeat domains. It acts through a Src-related pathway to enhance the formation of osteoclasts and bone resorption. It also acts as a negative regulator of cell motility. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212706 [Multi-domain] Cd Length: 53 Bit Score: 50.38 E-value: 1.02e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSLHGQQGIVPANRV 1983
Cdd:cd11772 3 RALYDYEAQHPDELSFEEGDLLYISDKSD----PNWWKATCGGKTGLIPSNYV 51
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1468-1613 |
1.04e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 55.32 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1468 KEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDL-------TEQLGEGGKN------VHELEKVRKQ---LEA 1531
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVearikkyEEQLGNVRNNkeyealQKEIESLKRRisdLED 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1532 EKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNhlrvVDSLQTSLDAETRSRNEALRVK 1611
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE----REELAAKIPPELLALYERIRKR 186
|
..
gi 431907173 1612 KK 1613
Cdd:COG1579 187 KN 188
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1360-1929 |
1.17e-07 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 56.96 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1360 QRVLSKANSEVAQWRtkyetdaiQRTEELEEAKLQDAEEaveavnakcssLEKTKhrlqNEIEDLMVDVERsnaaaAALD 1439
Cdd:pfam05701 41 ELELEKVQEEIPEYK--------KQSEAAEAAKAQVLEE-----------LESTK----RLIEELKLNLER-----AQTE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1440 KKQRNFDKILAEWKQKyeesQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNV 1519
Cdd:pfam05701 93 EAQAKQDSELAKLRVE----EMEQGIADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1520 H-------ELEKVRKQLEAEKLELQSALEEAEAS-LEHEEGKIlRAQLEFNQIKAEIERKLAEKDEEMEQAkRNHLRVVD 1591
Cdd:pfam05701 169 EeavsaskEIEKTVEELTIELIATKESLESAHAAhLEAEEHRI-GAALAREQDKLNWEKELKQAEEELQRL-NQQLLSAK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1592 SLQTSLDAetrsrNEALRVKKK------MEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMDdavRANDDLKE 1665
Cdd:pfam05701 247 DLKSKLET-----ASALLLDLKaelaayMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIE---KAKDEVNC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1666 NIAIVERrnnlLQAELEELRAVVEQTERSRKLA-------EQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVE 1738
Cdd:pfam05701 319 LRVAAAS----LRSELEKEKAELASLRQREGMAsiavsslEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1739 EAVQECRNAEEKAKKAITDaammAEELKKEQDT-SAHLERMKKNMEQTIkdlqhrldEAEQIALkggkkqlqkleARVRE 1817
Cdd:pfam05701 395 EAKSLAQAAREELRKAKEE----AEQAKAAASTvESRLEAVLKEIEAAK--------ASEKLAL-----------AAIKA 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1818 LEnelEAEQKRNAESVKGMRKSerrikeLTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQH 1897
Cdd:pfam05701 452 LQ---ESESSAESTNQEDSPRG------VTLSLEEYYELSKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNR 522
|
570 580 590
....*....|....*....|....*....|..
gi 431907173 1898 ELDEAEERADIAESQVNKlrAKSRDIGAKAQL 1929
Cdd:pfam05701 523 EMEERKEALKIALEKAEK--AKEGKLAAEQEL 552
|
|
| SH3_PSTPIP1 |
cd11824 |
Src homology 3 domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; PSTPIP1, ... |
1930-1985 |
1.20e-07 |
|
Src homology 3 domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; PSTPIP1, also called CD2 Binding Protein 1 (CD2BP1), is mainly expressed in hematopoietic cells. It is a binding partner of the cell surface receptor CD2 and PTP-PEST, a tyrosine phosphatase which functions in cell motility and Rac1 regulation. It also plays a role in the activation of the Wiskott-Aldrich syndrome protein (WASP), which couples actin rearrangement and T cell activation. Mutations in the gene encoding PSTPIP1 cause the autoinflammatory disorder known as PAPA (pyogenic sterile arthritis, pyoderma gangrenosum, and acne) syndrome. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212758 [Multi-domain] Cd Length: 53 Bit Score: 50.06 E-value: 1.20e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd11824 2 YSVLYDYTAQEDDELSISKGDVVAVIEKGE----DGWWTVERNGQKGLVPGTYLEK 53
|
|
| SH3_GRAP2_N |
cd11947 |
N-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ... |
1930-1983 |
1.22e-07 |
|
N-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS (GRB2-related adapter downstream of Shc), GrpL, GRB2L, Mona, or GRID (Grb2-related protein with insert domain). It is expressed specifically in the hematopoietic system. It plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. It also have roles in antigen-receptor and tyrosine kinase mediated signaling. GRAP2 is unique from other GRB2-like adaptor proteins in that it can be regulated by caspase cleavage. It contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The N-terminal SH3 domain of the related protein GRB2 binds to Sos and Sos-derived proline-rich peptides. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212880 [Multi-domain] Cd Length: 52 Bit Score: 50.18 E-value: 1.22e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREgagglDGWCLCSLHGQQGIVPANRV 1983
Cdd:cd11947 2 ARGKFDFTASGEDELSFKKGDVLKILSSD-----DIWFKAELNGEEGYVPKNFV 50
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1986-2223 |
1.27e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 57.64 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1986 LPAGPTPKPSLSQVP---PAEPGSPYPAPehsnedqevyVVPPPARPCLTSESPAGPCLPSPDPI--YKVPRGSGTQPAT 2060
Cdd:PHA03247 2798 LPSPWDPADPPAAVLapaAALPPAASPAG----------PLPPPTSAQPTAPPPPPGPPPPSLPLggSVAPGGDVRRRPP 2867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2061 PGDALEVYDVP--PAALRVSASGPYDTPASFshllarvaPQPPGEDEAPYDVPLAPKP-PSELEPDLEWEGGREPGPPLY 2137
Cdd:PHA03247 2868 SRSPAAKPAAParPPVRRLARPAVSRSTESF--------ALPPDQPERPPQPQAPPPPqPQPQPPPPPQPQPPPPPPPRP 2939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2138 AAPSNLKRASALLNlyeAPEELLADGEEGGSDEGIYDVP--LLGPETPPSPEPlgalasndpdtlalllARSPPPSHR-- 2213
Cdd:PHA03247 2940 QPPLAPTTDPAGAG---EPSGAVPQPWLGALVPGRVAVPrfRVPQPAPSREAP----------------ASSTPPLTGhs 3000
|
250
....*....|..
gi 431907173 2214 -PRLPS-AESLS 2223
Cdd:PHA03247 3001 lSRVSSwASSLA 3012
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1469-1825 |
1.29e-07 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 56.61 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1469 EARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEASLE 1548
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1549 HEEGKILRAQLEFNQ---IKAEIERKLAEKDEEME------QAKRNHLRVVDSLQTSLDAETRSRNEALRV----KKKME 1615
Cdd:pfam19220 101 EAEAAKEELRIELRDktaQAEALERQLAAETEQNRaleeenKALREEAQAAEKALQRAEGELATARERLALleqeNRRLQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1616 GDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDAV----RANDDLKENIAIVERRNNLLQAELEELRAVVEQT 1691
Cdd:pfam19220 181 ALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQaereRAEAQLEEAVEAHRAERASLRMKLEALTARAAAT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1692 ERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQEcRNAEEKAKKAITD-AAMMAEELKkeqD 1770
Cdd:pfam19220 261 EQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQ-FQEMQRARAELEErAEMLTKALA---A 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1771 TSAHLERMkknmEQTIKDLQHRLDEAEQIALKggkkQLQKLEARVRELENELEAE 1825
Cdd:pfam19220 337 KDAALERA----EERIASLSDRIAELTKRFEV----ERAALEQANRRLKEELQRE 383
|
|
| SH3_MLK4 |
cd12058 |
Src Homology 3 domain of Mixed Lineage Kinase 4; MLK4 is a Serine/Threonine Kinase (STK), ... |
1929-1983 |
1.29e-07 |
|
Src Homology 3 domain of Mixed Lineage Kinase 4; MLK4 is a Serine/Threonine Kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. MLK4 contains an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212991 [Multi-domain] Cd Length: 58 Bit Score: 50.32 E-value: 1.29e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1929 LARALYDNTAESPQELSFRRGDVLRVLQREGA-GGLDGWCLCSLHGQQGIVPANRV 1983
Cdd:cd12058 1 LWTALYDYEASGEDELSLRRGDVVEVLSQDAAvSGDDGWWAGKIRHRLGIFPANYV 56
|
|
| SH3_PACSIN |
cd11843 |
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) ... |
1931-1983 |
1.39e-07 |
|
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins; PACSINs, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. They bind both dynamin and Wiskott-Aldrich syndrome protein (WASP), and may provide direct links between the actin cytoskeletal machinery through WASP and dynamin-dependent endocytosis. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212777 [Multi-domain] Cd Length: 53 Bit Score: 50.11 E-value: 1.39e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGAgglDGWCLCSLHGQQGIVPANRV 1983
Cdd:cd11843 3 RALYDYEGQESDELSFKAGDILTKLEEEDE---QGWCKGRLDGRVGLYPANYV 52
|
|
| SH3_GRAF-like |
cd11882 |
Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase and similar ... |
1930-1985 |
1.40e-07 |
|
Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase and similar proteins; This subfamily is composed of Rho GTPase activating proteins (GAPs) with similarity to GRAF. Members contain an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. Although vertebrates harbor four Rho GAPs in the GRAF subfamily including GRAF, GRAF2, GRAF3, and Oligophrenin-1 (OPHN1), only three are included in this model. OPHN1 contains the BAR, PH and GAP domains, but not the C-terminal SH3 domain. GRAF and GRAF2 show GAP activity towards RhoA and Cdc42. GRAF influences Rho-mediated cytoskeletal rearrangements and binds focal adhesion kinase. GRAF2 regulates caspase-activated p21-activated protein kinase-2. The SH3 domain of GRAF and GRAF2 binds PKNbeta, a target of the small GTPase Rho. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.
Pssm-ID: 212815 [Multi-domain] Cd Length: 54 Bit Score: 49.98 E-value: 1.40e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQ--REgagglDGWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd11882 2 ARALYACKAEDESELSFEPGQIITNVQpsDE-----PGWLEGTLNGRTGLIPENYVEF 54
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
971-1225 |
1.41e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 971 HATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQekkvrmdL 1050
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-------L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1051 ERAKRKLEGDLKLTQESIMDLeNDKLQLEEKLKKKEFDISQQNSkieDEQALALQLQKKLkeNQARieeleeeleaerta 1130
Cdd:COG4942 89 EKEIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLLSPEDF---LDAVRRLQYLKYL--APAR-------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1131 RAKVEKLRSDLsRELEEISERLEEaggatsvQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKK---HADSVAELGE 1207
Cdd:COG4942 149 REQAEELRADL-AELAALRAELEA-------ERAELEALLAELEEERAALEALKAERQKLLARLEKElaeLAAELAELQQ 220
|
250
....*....|....*...
gi 431907173 1208 QIDNLQRVKQKLEKEKSE 1225
Cdd:COG4942 221 EAEELEALIARLEAEAAA 238
|
|
| SH3_Bem1p_1 |
cd11878 |
First Src Homology 3 domain of Bud emergence protein 1 and similar domains; Members of this ... |
1931-1981 |
1.65e-07 |
|
First Src Homology 3 domain of Bud emergence protein 1 and similar domains; Members of this subfamily bear similarity to Saccharomyces cerevisiae Bem1p, containing two Src Homology 3 (SH3) domains at the N-terminus, a central PX domain, and a C-terminal PB1 domain. Bem1p is a scaffolding protein that is critical for proper Cdc42p activation during bud formation in yeast. During budding and mating, Bem1p migrates to the plasma membrane where it can serve as an adaptor for Cdc42p and some other proteins. Bem1p also functions as an effector of the G1 cyclin Cln3p and the cyclin-dependent kinase Cdc28p in promoting vacuolar fusion. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.
Pssm-ID: 212811 [Multi-domain] Cd Length: 54 Bit Score: 49.98 E-value: 1.65e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGAgglDGWCLCS--LHGQQGIVPAN 1981
Cdd:cd11878 3 RALYDYRAQTPGELSFSKGDFFHVIGEEDQ---GEWYEATnpVTGKRGLVPKS 52
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1050-1582 |
1.67e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.83 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1050 LERAKRKLEGDLKLTQESIMDLENdklqLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERT 1129
Cdd:PRK01156 164 LERNYDKLKDVIDMLRAEISNIDY----LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1130 A--------------RAKVEKLRSDLSRELEE---ISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAA 1192
Cdd:PRK01156 240 AlnelssledmknryESEIKTAESDLSMELEKnnyYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1193 ALRKKHAD--SVAELG---EQIDNLQRVKQKLEKEKSEFKLELDDVTS---NMEQIIKAKANLEK--------VSRTLED 1256
Cdd:PRK01156 320 EINKYHAIikKLSVLQkdyNDYIKKKSRYDDLNNQILELEGYEMDYNSylkSIESLKKKIEEYSKniermsafISEILKI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1257 Q---ANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLT-RGK---LSYTQQTEDLKRQLEEEGKAKN 1329
Cdd:PRK01156 400 QeidPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNgQSVcpvCGTTLGEEKSNHIINHYNEKKS 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1330 ALAHALQSARHDCDLLREQYEEETEAKAELQRvlSKANSEVAQWRTKYETDAIQRTEELEEAKLQDAEEAVEAVNAKCSS 1409
Cdd:PRK01156 480 RLEEKIREIEIEVKDIDEKIVDLKKRKEYLES--EEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKS 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1410 LEKTKHRLQNEiEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLE 1489
Cdd:PRK01156 558 LKLEDLDSKRT-SWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYN 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1490 HLETFKRENKNLQEEISDLTEQLGEggknVHELEKVRKQLEAEKLE-------LQSALEEAEASLEHEEG--KILRAQL- 1559
Cdd:PRK01156 637 EIQENKILIEKLRGKIDNYKKQIAE----IDSIIPDLKEITSRINDiednlkkSRKALDDAKANRARLEStiEILRTRIn 712
|
570 580
....*....|....*....|...
gi 431907173 1560 EFNQIKAEIERKLaEKDEEMEQA 1582
Cdd:PRK01156 713 ELSDRINDINETL-ESMKKIKKA 734
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1504-1896 |
1.90e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 56.90 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1504 EISDLTEQLG--EGGKNVHELEKVRKQLEAEKLELQSALEEAEASLEHEEgKILRAQLEFNQIKAEIERKLAEKDEEMEQ 1581
Cdd:pfam02463 120 EVAELLESQGisPEAYNFLVQGGKIEIIAMMKPERRLEIEEEAAGSRLKR-KKKEALKKLIEETENLAELIIDLEELKLQ 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1582 AKRNHLRVVDSLQTS-LDAETRSRNEALRVKKKMEgdLNEMEIQLSQANRTASeaQKHLKIAQAHLKDTQLQMDDAVRAN 1660
Cdd:pfam02463 199 ELKLKEQAKKALEYYqLKEKLELEEEYLLYLDYLK--LNEERIDLLQELLRDE--QEEIESSKQEIEKEEEKLAQVLKEN 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1661 DDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLhsqntslinQKKKMESDLTQLQSEVEEA 1740
Cdd:pfam02463 275 KEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA---------EKELKKEKEEIEELEKELK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1741 VQECRNAEEKAKKaitdAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELEN 1820
Cdd:pfam02463 346 ELEIKREAEEEEE----EELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLL 421
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1821 ELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQ 1896
Cdd:pfam02463 422 KEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEE 497
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1408-1918 |
2.09e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 56.29 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1408 SSLEKTKHRL-QNEIEDLMVDVERSNAAAAALDKKQRNFDKILAewKQKYEESQSELESSQKEARSLSTELFKLKNAYEE 1486
Cdd:pfam05557 9 ARLSQLQNEKkQMELEHKRARIELEKKASALKRQLDRESDRNQE--LQKRIRLLEKREAEAEEALREQAELNRLKKKYLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1487 SLEHLEtfkRENKNLQEEISDLTEQLGEggknvhELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQlEFNQIKA 1566
Cdd:pfam05557 87 ALNKKL---NEKESQLADAREVISCLKN------ELSELRRQIQRAELELQSTNSELEELQERLDLLKAKAS-EAEQLRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1567 EIERKLAEKDEEMEQAKrnHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANrTASEAQKHLKIAQAHL 1646
Cdd:pfam05557 157 NLEKQQSSLAEAEQRIK--ELEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLN-ENIENKLLLKEEVEDL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1647 KDTQLQMDDAvranddlKENIAIVERRNNLLQAELEELravvEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKM 1726
Cdd:pfam05557 234 KRKLEREEKY-------REEAATLELEKEKLEQELQSW----VKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1727 ESDLTQLQSEVEEAVQECRNAEEKakkaITDAAMMAEELK--------------KEQD-TSAHLERMKK--NMEQTIKDL 1789
Cdd:pfam05557 303 TSSARQLEKARRELEQELAQYLKK----IEDLNKKLKRHKalvrrlqrrvllltKERDgYRAILESYDKelTMSNYSPQL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1790 QHRLDEAEQIALKgGKKQLQKLEARVRELENELEAeQKRNAESVK---GMRKSERRIKELTYQTEEdkKNLLRLQdlVDK 1866
Cdd:pfam05557 379 LERIEEAEDMTQK-MQAHNEEMEAQLSVAEEELGG-YKQQAQTLErelQALRQQESLADPSYSKEE--VDSLRRK--LET 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 431907173 1867 LQLKVKAYKRQAEEAEE-------QANTNLSKFRKVQHELDEAEERADIAESQVNKLRA 1918
Cdd:pfam05557 453 LELERQRLREQKNELEMelerrclQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQA 511
|
|
| SH3_p47phox_like |
cd11856 |
Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This ... |
1931-1981 |
2.34e-07 |
|
Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This family is composed of the tandem SH3 domains of p47phox subunit of NADPH oxidase and Nox Organizing protein 1 (NoxO1), the four SH3 domains of Tks4 (Tyr kinase substrate with four SH3 domains), the five SH3 domains of Tks5, the SH3 domain of obscurin, Myosin-I, and similar domains. Most members of this group also contain Phox homology (PX) domains, except for obscurin and Myosin-I. p47phox and NoxO1 are regulators of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) and nonphagocytic NADPH oxidase Nox1, respectively. They play roles in the activation of their respective NADPH oxidase, which catalyzes the transfer of electrons from NADPH to molecular oxygen to form superoxide. Tks proteins are Src substrates and scaffolding proteins that play important roles in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. Obscurin is a giant muscle protein that plays important roles in the organization and assembly of the myofibril and the sarcoplasmic reticulum. Type I myosins (Myosin-I) are actin-dependent motors in endocytic actin structures and actin patches. They play roles in membrane traffic in endocytic and secretory pathways, cell motility, and mechanosensing. Myosin-I contains an N-terminal actin-activated ATPase, a phospholipid-binding TH1 (tail homology 1) domain, and a C-terminal extension which includes an F-actin-binding TH2 domain, an SH3 domain, and an acidic peptide that participates in activating the Arp2/3complex. The SH3 domain of myosin-I is required for myosin-I-induced actin polymerization. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212790 [Multi-domain] Cd Length: 53 Bit Score: 49.56 E-value: 2.34e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREgaggLDGWCLCSLHGQQGIVPAN 1981
Cdd:cd11856 3 VAIADYEAQGDDEISLQEGEVVEVLEKN----DSGWWYVRKGDKEGWVPAS 49
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1988-2232 |
2.35e-07 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 56.53 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1988 AGPTPKPSLSQVPPAEPGSPYPAPEHSNEDQEVYVVPPPARPcltSESPAGPCLPSPDPiykvprgsGTQPATPGDALEV 2067
Cdd:PRK07764 588 VGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAP---AGAAAAPAEASAAP--------APGVAAPEHHPKH 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2068 YDVPPAALRVSASGPYDTPAsfshllARVAPQPPGEDEAPydVPLAPKPPSELEPDLEWEGGREPGPPLYAAP-----SN 2142
Cdd:PRK07764 657 VAVPDASDGGDGWPAKAGGA------APAAPPPAPAPAAP--AAPAGAAPAQPAPAPAATPPAGQADDPAAQPpqaaqGA 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2143 LKRASALLNLYEAPEELLADGEEGGSDEGIYDVPLLGPETPPSPEPLGALASNDPDTLALLLARSPPPSHRPRLPSAESL 2222
Cdd:PRK07764 729 SAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEEVAMEL 808
|
250
....*....|
gi 431907173 2223 SRRPLPALPV 2232
Cdd:PRK07764 809 LEEELGAKKI 818
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1237-1446 |
2.38e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.18 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1237 MEQIIKAK-ANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQ--AKLQTENGELARQLEEKEALISQLTRGKLSYTQQ 1313
Cdd:COG3206 162 LEQNLELRrEEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1314 TEDLKRQLEEEGKAKNALAHALQSARhdcdlLREQYEEETEAKAELQRVLSKANSEVAQWRtkyetdaiQRTEELEEAKL 1393
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELEAELAELSARYTPNHPDVIALR--------AQIAALRAQLQ 308
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1394 QDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFD 1446
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| SH3_AHI-1 |
cd11812 |
Src Homology 3 domain of Abelson helper integration site-1 (AHI-1); AHI-1, also called ... |
1932-1983 |
2.61e-07 |
|
Src Homology 3 domain of Abelson helper integration site-1 (AHI-1); AHI-1, also called Jouberin, is expressed in high levels in the brain, gonad tissues, and skeletal muscle. It is an adaptor protein that interacts with the small GTPase Rab8a and regulates it distribution and function, affecting cilium formation and vesicle transport. Mutations in the AHI-1 gene can cause Joubert syndrome, a disorder characterized by brainstem malformations, cerebellar aplasia/hypoplasia, and retinal dystrophy. AHI-1 variation is also associated with susceptibility to schizophrenia and type 2 diabetes mellitus progression. AHI-1 contains WD40 and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212746 [Multi-domain] Cd Length: 52 Bit Score: 49.43 E-value: 2.61e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSL-HGQQGIVPANRV 1983
Cdd:cd11812 4 ALYDYTANRSDELTIHRGDIIRVLYKDN----DNWWFGSLvNGQQGYFPANYV 52
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1803-2231 |
3.21e-07 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 55.93 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1803 GGKKQLQKLEARVRELENELE---------AEQKRNAESVKGMRKSERRIKEltyqteedkknllrlqdlvdKLQLKVKA 1873
Cdd:pfam03154 20 GRKKQTASPDGRASPTNEDLRssgrnspsaASTSSNDSKAESMKKSSKKIKE--------------------EAPSPLKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1874 YKRQAE------EAEEQANTNLSKFRKVQ--HELDEAEERADIAESQVNKLRAKSRDIGAkaqlaralyDNTAESPQELS 1945
Cdd:pfam03154 80 AKRQREkgasdtEEPERATAKKSKTQEISrpNSPSEGEGESSDGRSVNDEGSSDPKDIDQ---------DNRSTSPSIPS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1946 FR--RGDVLRVLQREgaggldgwclcSLHGQQGIVPAnrvkllPAGPTPKPSLSQVPPAEPGSPYPAPEHSNEDQEVYvv 2023
Cdd:pfam03154 151 PQdnESDSDSSAQQQ-----------ILQTQPPVLQA------QSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGS-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2024 PPPARPCLTSESPAGPC-------------LPSPDPiykvPRGSGTQPATPgdalevydvppaalrvSASGPYDTPASFS 2090
Cdd:pfam03154 212 PATSQPPNQTQSTAAPHtliqqtptlhpqrLPSPHP----PLQPMTQPPPP----------------SQVSPQPLPQPSL 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2091 HllARVAPQPPGEDEAPYDVPlAPKPPSELEPDLEWEGGREPGPPLYAAPSNLKRASALlnlyeAPEElladgeeggsde 2170
Cdd:pfam03154 272 H--GQMPPMPHSLQTGPSHMQ-HPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHT-----PPSQ------------ 331
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 431907173 2171 giydvPLLGPETPPSPEPLgalasnDPDTLALLLARSPPPSHRPRLPSAESLSRRPLPALP 2231
Cdd:pfam03154 332 -----SQLQSQQPPREQPL------PPAPLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGP 381
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1393-1824 |
3.42e-07 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 55.47 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1393 LQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDkkqrNFDKILAEWKQKYEESQselessqKEARS 1472
Cdd:pfam05622 2 LSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLE----SGDDSGTPGGKKYLLLQ-------KQLEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1473 LSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLT-------------------------------------EQLGEG 1515
Cdd:pfam05622 71 LQEENFRLETARDDYRIKCEELEKEVLELQHRNEELTslaeeaqalkdemdilressdkvkkleatvetykkklEDLGDL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1516 GKNVHELEK---------------------VRKQLEAEKLELQsaleEAEASLEHEEGKILRAQLEFNQIKAEIERKLAE 1574
Cdd:pfam05622 151 RRQVKLLEErnaeymqrtlqleeelkkanaLRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKKLEEKLEALQKE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1575 KDEEMEQakRNHLRvvdslqtsldaETrsrNEALRVKKKMEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMD 1654
Cdd:pfam05622 227 KERLIIE--RDTLR-----------ET---NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1655 D-AVRANDDLKENIAIVErrnnlLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLH-------SQNTSLINQKKKM 1726
Cdd:pfam05622 291 NkMLRLGQEGSYRERLTE-----LQQLLEDANRRKNELETQNRLANQRILELQQQVEELQkalqeqgSKAEDSSLLKQKL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1727 ESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNMEQ---TIKDLQHRLDEAEQ 1798
Cdd:pfam05622 366 EEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKaksVIKTLDPKQNPASP 445
|
490 500
....*....|....*....|....*.
gi 431907173 1799 IALKGGKKQLQKLEARVRELENELEA 1824
Cdd:pfam05622 446 PEIQALKNQLLEKDKKIEHLERDFEK 471
|
|
| SH3_FCHSD1_2 |
cd11895 |
Second Src Homology 3 domain of FCH and double SH3 domains protein 1; FCHSD1 has a domain ... |
1929-1980 |
3.52e-07 |
|
Second Src Homology 3 domain of FCH and double SH3 domains protein 1; FCHSD1 has a domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. It has only been characterized in silico and its function is unknown. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212828 Cd Length: 58 Bit Score: 49.19 E-value: 3.52e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 431907173 1929 LARALYDNTAESPQELSFRRGDVLRVLQREGAGGLDGWCLCSLHGQQGIVPA 1980
Cdd:cd11895 1 LARALYSYTGQSPEELSFPEGALIRLLPRAQDGVDDGFWRGEFGGRVGVFPS 52
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1611-1832 |
3.99e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1611 KKKMEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQ 1690
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1691 TERSRKLAE--------QELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQEcrnaeekakkaitdaammA 1762
Cdd:COG3883 98 SGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE------------------L 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1763 EELKKEqdtsahLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEARVRELENELEAEQKRNAES 1832
Cdd:COG3883 160 EALKAE------LEAAKAELEAQQAEQEALLAQLSA--------EEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1353-1583 |
4.32e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1353 TEAKAELQRVLSKANSEVAQwrTKYETDAIQRTEELEEAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMvdvERSN 1432
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAE--LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE---KEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1433 AAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQL 1512
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 431907173 1513 GEGGKNVHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAK 1583
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1740-1946 |
4.92e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1740 AVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELE 1819
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ-ELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1820 NELEAEQKRNAESVKGMRKSERR---------------IKELTY----------QTEEDKKNLLRLQDLVDKLQLKVKAY 1874
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQpplalllspedfldaVRRLQYlkylaparreQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 431907173 1875 KRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKAQLARALYDNTAESPQELSF 1946
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
|
| SH3_Sorbs_1 |
cd11781 |
First Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) proteins and similar ... |
1930-1985 |
4.97e-07 |
|
First Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) proteins and similar domains; This family, also called the vinexin family, is composed predominantly of adaptor proteins containing one sorbin homology (SoHo) and three SH3 domains. Members include the first SH3 domains of Sorbs1 (or ponsin), Sorbs2 (or ArgBP2), Vinexin (or Sorbs3), and similar domains. They are involved in the regulation of cytoskeletal organization, cell adhesion, and growth factor signaling. Members of this family bind multiple partners including signaling molecules like c-Abl, c-Arg, Sos, and c-Cbl, as well as cytoskeletal molecules such as vinculin and afadin. They may have overlapping functions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212715 [Multi-domain] Cd Length: 53 Bit Score: 48.49 E-value: 4.97e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGAGGLDGwclcSLHGQQGIVPANRVKL 1985
Cdd:cd11781 2 ARALYPFKAQSAKELSLKKGDIIYIRRQIDKNWYEG----EHNGRVGIFPASYVEI 53
|
|
| SH3_SH3RF_1 |
cd11786 |
First Src Homology 3 domain of SH3 domain containing ring finger proteins; This model ... |
1930-1984 |
5.04e-07 |
|
First Src Homology 3 domain of SH3 domain containing ring finger proteins; This model represents the first SH3 domain of SH3RF1 (or POSH), SH3RF2 (or POSHER), SH3RF3 (POSH2), and similar domains. Members of this family are scaffold proteins that function as E3 ubiquitin-protein ligases. They all contain an N-terminal RING finger domain and multiple SH3 domains; SH3RF1 and SH3RF3 have four SH3 domains while SH3RF2 has three. SH3RF1 plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF3 interacts with p21-activated kinase 2 (PAK2) and GTP-loaded Rac1. It may play a role in regulating JNK mediated apoptosis in certain conditions. SH3RF2 acts as an anti-apoptotic regulator of the JNK pathway by binding to and promoting the degradation of SH3RF1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212720 [Multi-domain] Cd Length: 53 Bit Score: 48.51 E-value: 5.04e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQRegaggLD-GWCLCSLHGQQGIVPANRVK 1984
Cdd:cd11786 2 AKALYNYEGKEPGDLSFKKGDIILLRKR-----IDeNWYHGECNGKQGFFPASYVQ 52
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1369-1945 |
5.05e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 55.61 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1369 EVAQWRtkYETDAIQRTEEL--EEAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMvdvERSNAAAAALDKKQRNFD 1446
Cdd:pfam12128 222 QVEHWI--RDIQAIAGIMKIrpEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQ---EERQETSAELNQLLRTLD 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1447 KilaEWKQKYEEsqselessqkearsLSTELFKLKNAYEESLEHLETFKRENKNLQEEisdlteqlgeggknvhELEKVR 1526
Cdd:pfam12128 297 D---QWKEKRDE--------------LNGELSAADAAVAKDRSELEALEDQHGAFLDA----------------DIETAA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1527 KQLEAEKLeLQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEqakrnhlrvvDSLQTSLDAETRSRNE 1606
Cdd:pfam12128 344 ADQEQLPS-WQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIK----------DKLAKIREARDRQLAV 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1607 ALRVKKKMEGDLNEmeiQLSQANRTASEAQKHLKIAQAHLKdtqLQMDDAVrANDDLKENIAIVERRNNLLQAELEELRA 1686
Cdd:pfam12128 413 AEDDLQALESELRE---QLEAGKLEFNEEEYRLKSRLGELK---LRLNQAT-ATPELLLQLENFDERIERAREEQEAANA 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1687 VVEQTERSRKLAEQELIETSERVQLLHSQntslinqkkkmesdLTQLQSEVEEAVQEcrnaeekakkAITDAAMMAEELK 1766
Cdd:pfam12128 486 EVERLQSELRQARKRRDQASEALRQASRR--------------LEERQSALDELELQ----------LFPQAGTLLHFLR 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1767 KE-QDTSAHLERMKKnmeqtiKDLQHRLDeaeqialkggkkqlqklearvreLENELEAEQKRNAESVKGMRkserrike 1845
Cdd:pfam12128 542 KEaPDWEQSIGKVIS------PELLHRTD-----------------------LDPEVWDGSVGGELNLYGVK-------- 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1846 ltyqteedkknlLRLQdlvdklQLKVKAYKRQAEEAEEQANtnlskfrKVQHELDEAEERADIAESQVNKLRAKSRDIGA 1925
Cdd:pfam12128 585 ------------LDLK------RIDVPEWAASEEELRERLD-------KAEEALQSAREKQAAAEEQLVQANGELEKASR 639
|
570 580
....*....|....*....|
gi 431907173 1926 KAQLARALYDNTAESPQELS 1945
Cdd:pfam12128 640 EETFARTALKNARLDLRRLF 659
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1196-1696 |
5.15e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 55.29 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1196 KKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVtsnMEQIIKAKANLEKVSrTLEDQANEYRTKLEEAQRSLNDF 1275
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNA---MDDYNNLKSALNELS-SLEDMKNRYESEIKTAESDLSME 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1276 TTQQAKLQTENGELARQLEEKEALISQLTRGKLSYTQQTEDLKRQLE----EEGKAKNALAHA--LQSARHDCDLLREQY 1349
Cdd:PRK01156 269 LEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSnidaEINKYHAIIKKLsvLQKDYNDYIKKKSRY 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1350 EEETEAKAELQRVLSKANSEV------AQWRTKYE------TDAIQRTEELEE-------AKLQDAEEAVEAVNAKCSSL 1410
Cdd:PRK01156 349 DDLNNQILELEGYEMDYNSYLksieslKKKIEEYSkniermSAFISEILKIQEidpdaikKELNEINVKLQDISSKVSSL 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1411 EKTKHRLQNEIEDLMVDVE----RSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYE- 1485
Cdd:PRK01156 429 NQRIRALRENLDELSRNMEmlngQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEy 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1486 ---ESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLE-----------------------LQSA 1539
Cdd:PRK01156 509 lesEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEdldskrtswlnalavislidietNRSR 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1540 LEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEME--QAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGD 1617
Cdd:PRK01156 589 SNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANnlNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPD 668
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 431907173 1618 LNEMEIQLSQANrtaseaqkhlkiaqAHLKDTQLQMDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRK 1696
Cdd:PRK01156 669 LKEITSRINDIE--------------DNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKK 733
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1216-1417 |
5.47e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1216 KQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEE 1295
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1296 KEALISQLTR-----GKLSYT---------------------------QQTEDLKRQLEEEGKAKNALAHALQSARHDCD 1343
Cdd:COG4942 102 QKEELAELLRalyrlGRQPPLalllspedfldavrrlqylkylaparrEQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1344 LLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKLQDAEEAVEAVNAKCSSLEKTKHRL 1417
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1989-2232 |
5.98e-07 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 54.88 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1989 GPTPKPSLSQVPPAEPGSPYPAPEhsnedqevYVVPPPARPCLTSESPAGPCLPSPdpiykVPRGSGTQPATPGDALEVY 2068
Cdd:PRK12323 370 GGAGPATAAAAPVAQPAPAAAAPA--------AAAPAPAAPPAAPAAAPAAAAAAR-----AVAAAPARRSPAPEALAAA 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2069 DVPPAALRVSASGPYDTPASfshllARVAPQPPGEDEAPYDVPLAPKPPSELEPDLEWEGGREPGPPLYAAPSNLkrasA 2148
Cdd:PRK12323 437 RQASARGPGGAPAPAPAPAA-----APAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEF----A 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2149 LLNLYEAPEELLADGEEGGSDEGIYDVPllGPETPPSPEPLGALASNDPDTLALLLARSPPPSHRPRLPSAESLSRRPLP 2228
Cdd:PRK12323 508 SPAPAQPDAAPAGWVAESIPDPATADPD--DAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGDWPALA 585
|
....*
gi 431907173 2229 A-LPV 2232
Cdd:PRK12323 586 ArLPV 590
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
870-1035 |
7.16e-07 |
|
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
Pssm-ID: 318204 [Multi-domain] Cd Length: 234 Bit Score: 52.66 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 870 ARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQL---------------IKNKI--------QLEAKVKEMNE 926
Cdd:pfam15934 41 ENKNEQEQQLKEFTVQNQRLACQIDNLHETLKDRDHQIKQLqsmitgysdisennrLKEEIhdlkqkncVQARVVRKMGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 927 RLEDEEEMNAELTAKKRKL----EDECSELK---RDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLdeiiakltKEKK 999
Cdd:pfam15934 121 ELKGQEEQRVELCDKYESLlgsfEEQCQELKranRRVQSLQTRLSQVEKLQEELRTERKILREEVIAL--------KEKD 192
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 431907173 1000 ALQEAHQQALDD----LQAEEDKVNTLTKsKVKLEQQVDD 1035
Cdd:pfam15934 193 AKSNGRERALQDqlkcCQTEIEKSRTLIR-NMQSHLQLED 231
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1428-1830 |
7.19e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 7.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1428 VERSNAAAAALDKKQRNFDKILAEwKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEhLETFKRENKNLQEEISD 1507
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQLLPLYQE-LEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1508 LTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHL 1587
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1588 RVVDSLQTSLDAETRSRNE----------ALRVKKKMEGDLNEM--------------EIQLSQANRTASEAQKHLKIAQ 1643
Cdd:COG4717 231 QLENELEAAALEERLKEARlllliaaallALLGLGGSLLSLILTiagvlflvlgllalLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1644 AHLKDTQLQMDDAVRANDDLKENIAIVERRNNLLQ-AELEELRAVVEQTERSRKLAEQElietSERVQLLHSQNTSLIN- 1721
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRiEELQELLREAEELEEELQLEELE----QEIAALLAEAGVEDEEe 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1722 --QKKKMESDLTQLQSEVEEAVQECRNA--EEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAE 1797
Cdd:COG4717 387 lrAALEQAEEYQELKEELEELEEQLEELlgELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
410 420 430
....*....|....*....|....*....|...
gi 431907173 1798 qialkgGKKQLQKLEARVRELENELEAEQKRNA 1830
Cdd:COG4717 467 ------EDGELAELLQELEELKAELRELAEEWA 493
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1979-2257 |
7.55e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.94 E-value: 7.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1979 PANRVKLLPAGPTPKpSLSQVPPAEPGSPYPAPEHSNEDQEVYVVPPPARPcltseSPAGPCLPSPdpiykvPRG--SGT 2056
Cdd:PHA03247 2712 PHALVSATPLPPGPA-AARQASPALPAAPAPPAVPAGPATPGGPARPARPP-----TTAGPPAPAP------PAApaAGP 2779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2057 QPATPGDALevydVPPAALRVSASGPYDTPASFSHLLARVAPQPPGEDEA------PYDVPLAPKPPSE-LEPDLEWEGG 2129
Cdd:PHA03247 2780 PRRLTRPAV----ASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAgplpppTSAQPTAPPPPPGpPPPSLPLGGS 2855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2130 REPGPPLYAAPSNLKRASALLNLYEAPEELLADGEEGGSDEGiYDVPLLGPETPPSPEPLGALASNDPDTLALLLARSPP 2209
Cdd:PHA03247 2856 VAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTES-FALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPP 2934
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 431907173 2210 PSHRPRLPSAESL----SRRPLPALPVPEAPSPSPVPSPAPGRKGS--IQDRPL 2257
Cdd:PHA03247 2935 PPPRPQPPLAPTTdpagAGEPSGAVPQPWLGALVPGRVAVPRFRVPqpAPSREA 2988
|
|
| SH3_Eve1_4 |
cd11817 |
Fourth Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 ... |
1930-1981 |
7.60e-07 |
|
Fourth Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 domain-containing protein 19 (SH3D19) or EEN-binding protein (EBP), exists in multiple alternatively spliced isoforms. The longest isoform contains five SH3 domain in the C-terminal region and seven proline-rich motifs in the N-terminal region. It is abundantly expressed in skeletal muscle and heart, and may be involved in regulating the activity of ADAMs (A disintegrin and metalloproteases). Eve-1 interacts with EEN, an endophilin involved in endocytosis and may be the target of the MLL-EEN fusion protein that is implicated in leukemogenesis. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212751 [Multi-domain] Cd Length: 50 Bit Score: 47.86 E-value: 7.60e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQRegaggLDG-WCLCSLHGQQGIVPAN 1981
Cdd:cd11817 2 AVALYDFTGETEEDLSFQRGDRILVTEH-----LDAeWSRGRLNGREGIFPRA 49
|
|
| SH3_GRAP2_C |
cd11950 |
C-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ... |
1930-1984 |
8.23e-07 |
|
C-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS (GRB2-related adapter downstream of Shc), GrpL, GRB2L, Mona, or GRID (Grb2-related protein with insert domain). It is expressed specifically in the hematopoietic system. It plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. It also has roles in antigen-receptor and tyrosine kinase mediated signaling. GRAP2 is unique from other GRB2-like adaptor proteins in that it can be regulated by caspase cleavage. It contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domain of GRAP2 binds to different motifs found in substrate peptides including the typical PxxP motif in hematopoietic progenitor kinase 1 (HPK1), the RxxK motif in SLP-76 and HPK1, and the RxxxxK motif in phosphatase-like protein HD-PTP. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212883 [Multi-domain] Cd Length: 53 Bit Score: 47.90 E-value: 8.23e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGAggldGWCLCSLHGQQGIVPANRVK 1984
Cdd:cd11950 2 VRALYDFEALEDDELGFNSGDVIEVLDSSNP----SWWKGRLHGKLGLFPANYVA 52
|
|
| SH3_SKAP1-like |
cd11866 |
Src Homology 3 domain of Src Kinase-Associated Phosphoprotein 1 and similar proteins; This ... |
1931-1979 |
9.00e-07 |
|
Src Homology 3 domain of Src Kinase-Associated Phosphoprotein 1 and similar proteins; This subfamily is composed of SKAP1, SKAP2, and similar proteins. SKAP1 and SKAP2 are immune cell-specific adaptor proteins that play roles in T- and B-cell adhesion, respectively, and are thus important in the migration of T- and B-cells to sites of inflammation and for movement during T-cell conjugation with antigen-presenting cells. Both SKAP1 and SKAP2 bind to ADAP (adhesion and degranulation-promoting adaptor protein), among many other binding partners. They contain a pleckstrin homology (PH) domain, a C-terminal SH3 domain, and several tyrosine phosphorylation sites. The SH3 domain of SKAP1 is necessary for its ability to regulate T-cell conjugation with antigen-presenting cells and the formation of LFA-1 clusters. SKAP1 binds primarily to a proline-rich region of ADAP through its SH3 domain; its degradation is regulated by ADAP. A secondary interaction occurs via the ADAP SH3 domain and the RKxxYxxY motif in SKAP1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212800 Cd Length: 53 Bit Score: 47.81 E-value: 9.00e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGAGglDGWCLCSLHGQQGIVP 1979
Cdd:cd11866 3 MGLWDCSGNEPDELSFKRGDLIYIISKEYDS--FGWWVGELNGKVGLVP 49
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
852-1175 |
9.12e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.75 E-value: 9.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 852 ANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNERLEDE 931
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 932 EEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAH-QQALD 1010
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1011 DLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDIS 1090
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1091 QQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKRE 1170
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
....*
gi 431907173 1171 AEFQK 1175
Cdd:COG4372 347 LVGLL 351
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1489-1933 |
9.19e-07 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 54.14 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1489 EHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSAL--------EEAEASLEHEEGKILRAQLE 1560
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIalrragglEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1561 FNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRTASEAQKHLK 1640
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1641 IAQAHLKDTQLQMDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLI 1720
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1721 NQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIA 1800
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1801 LKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEE 1880
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1881 AEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKAQLARAL 1933
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASA 528
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
845-1698 |
9.78e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.57 E-value: 9.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 845 AETEKEMANMKEEFGRLKETLEKSEARRKELEEKmvslLQEKND-LQLQVQAEQdnLNDAEERCdqliknkiqlEAKVKE 923
Cdd:COG3096 295 FGARRQLAEEQYRLVEMARELEELSARESDLEQD----YQAASDhLNLVQTALR--QQEKIERY----------QEDLEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 924 MNERLEDEEEMNAELT-------AKKRKLEDECSELKRDIDDL-------------------------------ELTLAK 965
Cdd:COG3096 359 LTERLEEQEEVVEEAAeqlaeaeARLEAAEEEVDSLKSQLADYqqaldvqqtraiqyqqavqalekaralcglpDLTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 966 VEKEKHATENKVKNLTEEMAGLDE--IIAKLTKEK--KALQ------------EAHQQALD------DLQAEEDKVNTlt 1023
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQklSVADAARRQfeKAYElvckiageversQAWQTAREllrryrSQQALAQRLQQ-- 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1024 kskvkLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLkltqESIMDLENDKLQLEEKLKkkefDISQQnskIEDEQALA 1103
Cdd:COG3096 517 -----LRAQLAELEQRLRQQQNAERLLEEFCQRIGQQL----DAAEELEELLAELEAQLE----ELEEQ---AAEAVEQR 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1104 LQLQKKLKENQARIEELEEELEAERTARAKVEKLRsdlsrelEEISERLEEAGGATS-VQIEMNKKREAEFQKmrrdlEE 1182
Cdd:COG3096 581 SELRQQLEQLRARIKELAARAPAWLAAQDALERLR-------EQSGEALADSQEVTAaMQQLLEREREATVER-----DE 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1183 ATLQHEATAAALRKKHADSVAELGEqidnLQRVKQKLEKE-KSEFkleLDDVTSNMEQIIKAK---ANLEKVSRTLEDqa 1258
Cdd:COG3096 649 LAARKQALESQIERLSQPGGAEDPR----LLALAERLGGVlLSEI---YDDVTLEDAPYFSALygpARHAIVVPDLSA-- 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1259 neYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLTRGKLSYT--------------QQTEDLKRQLEE- 1323
Cdd:COG3096 720 --VKEQLAGLEDCPEDLYLIEGDPDSFDDSVFDAEELEDAVVVKLSDRQWRYSrfpevplfgraareKRLEELRAERDEl 797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1324 -EGKAKNA--------LAHALQS--ARHDCDLLREQYEEE----TEAKAELQRVLSKANSEVAQWRTKY----------- 1377
Cdd:COG3096 798 aEQYAKASfdvqklqrLHQAFSQfvGGHLAVAFAPDPEAElaalRQRRSELERELAQHRAQEQQLRQQLdqlkeqlqlln 877
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1378 ----------ETDAIQRTEELEEaKLQDAEEAVEAVNAKCSSLEktkhrlqnEIEDLmvdversnaaAAALDKKQRNFDk 1447
Cdd:COG3096 878 kllpqanllaDETLADRLEELRE-ELDAAQEAQAFIQQHGKALA--------QLEPL----------VAVLQSDPEQFE- 937
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1448 ilaEWKQKYEESQSELESSQKEARSLsTELFKLKN--AYEESLEHLetfkrenknlqEEISDLTEQLGEggknvhELEkv 1525
Cdd:COG3096 938 ---QLQADYLQAKEQQRRLKQQIFAL-SEVVQRRPhfSYEDAVGLL-----------GENSDLNEKLRA------RLE-- 994
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1526 rkQLEAEKLELQSALEEAEAslEHEEGKILRAQLEF-----NQIKAEIERKLAE----KDEEMEQAKRNHlrvVDSLQTS 1596
Cdd:COG3096 995 --QAEEARREAREQLRQAQA--QYSQYNQVLASLKSsrdakQQTLQELEQELEElgvqADAEAEERARIR---RDELHEE 1067
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1597 LDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLkDTQLQMddaVRANDdlkeniaiVERRNN- 1675
Cdd:COG3096 1068 LSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGW-CAVLRL---ARDND--------VERRLHr 1135
|
970 980
....*....|....*....|....*
gi 431907173 1676 --LLQAELEELRAVVEQTERSRKLA 1698
Cdd:COG3096 1136 reLAYLSADELRSMSDKALGALRLA 1160
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1282-1574 |
1.02e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 53.00 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1282 LQTENGELARQLEEKEALIS-QLTRGKLSYTQQTEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEE----TEAK 1356
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDElnlrTSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1357 AE---LQRVLSKANSEVAQWRTKYETdaiqRTEELEEAKLQDAEEAVEavnakcsslektkhrLQNEIEDLMVDVERSNA 1433
Cdd:pfam00038 103 NDlvgLRKDLDEATLARVDLEAKIES----LKEELAFLKKNHEEEVRE---------------LQAQVSDTQVNVEMDAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1434 aaaaldkKQRNFDKILAEWKQKYEEsqselessqkearslstelfkLKNAYEESLEhlETFKRENKNLQEEISDLTEQLG 1513
Cdd:pfam00038 164 -------RKLDLTSALAEIRAQYEE---------------------IAAKNREEAE--EWYQSKLEELQQAAARNGDALR 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 431907173 1514 EGGKNVHELEKVRKQLEAE-------KLELQSALEEAEASLEHE----EGKILRAQLEFNQIKAEIERKLAE 1574
Cdd:pfam00038 214 SAKEEITELRRTIQSLEIElqslkkqKASLERQLAETEERYELQladyQELISELEAELQETRQEMARQLRE 285
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
845-1251 |
1.07e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 53.75 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 845 AETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEM 924
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 925 NERLEdeeemnaELTAKKRKLEDECSelkrdidDLELTLAKVEKEKHatenkvknlteemagldeiiaKLTKEKKALQEA 1004
Cdd:pfam07888 156 KERAK-------KAGAQRKEEEAERK-------QLQAKLQQTEEELR---------------------SLSKEFQELRNS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1005 HQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGdlkLTQE-SIMDLENDKLQLEekLK 1083
Cdd:pfam07888 201 LAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEG---LGEElSSMAAQRDRTQAE--LH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1084 KKEFDISQQNSKIEDeqaLALQLqkklkenqarieeleeeleaeRTARAKVEKLRSDLSRELEEISERLEeaggatsvqi 1163
Cdd:pfam07888 276 QARLQAAQLTLQLAD---ASLAL---------------------REGRARWAQERETLQQSAEADKDRIE---------- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1164 emnkKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKL---EKEKSEFKLELDDVtsnMEQI 1240
Cdd:pfam07888 322 ----KLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLrvaQKEKEQLQAEKQEL---LEYI 394
|
410
....*....|.
gi 431907173 1241 IKAKANLEKVS 1251
Cdd:pfam07888 395 RQLEQRLETVA 405
|
|
| SH3_SNX9_like |
cd11763 |
Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox ... |
1929-1983 |
1.09e-06 |
|
Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. This subfamily consists of SH3 domain containing SNXs including SNX9, SNX18, SNX33, and similar proteins. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis, while SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212697 [Multi-domain] Cd Length: 55 Bit Score: 47.71 E-value: 1.09e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1929 LARALYDNTAESPQELSFRRGDVLRVLqREGAGglDGWCL-CSLHGQQGIVPANRV 1983
Cdd:cd11763 1 KVRALYDFDSQPSGELSLRAGEVLTIT-RQDVG--DGWLEgRNSRGEVGLFPSSYV 53
|
|
| SH3_Sla1p_3 |
cd11775 |
Third Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates ... |
1930-1985 |
1.12e-06 |
|
Third Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates endocytosis by playing a role as an adaptor protein in coupling components of the actin cytoskeleton to the endocytic machinery. It interacts with Abp1p, Las17p and Pan1p, which are activator proteins of actin-related protein 2/3 (Arp2/3). Sla1p contains multiple domains including three SH3 domains, a SAM (sterile alpha motif) domain, and a Sla1 homology domain 1 (SHD1), which binds to the NPFXD motif that is found in many integral membrane proteins such as the Golgi-localized Arf-binding protein Lsb5p and the P4-ATPases, Drs2p and Dnf1p. The third SH3 domain of Sla1p can bind ubiquitin while retaining the ability to bind proline-rich ligands; monoubiquitination of target proteins signals internalization and sorting through the endocytic pathway. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212709 [Multi-domain] Cd Length: 57 Bit Score: 47.70 E-value: 1.12e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGAgglDGWCLCSL--HGQQGIVPANRVKL 1985
Cdd:cd11775 3 GKVLYDFDAQSDDELTVKEGDVVYILDDKKS---KDWWMVENvsTGKEGVVPASYIEI 57
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1317-1643 |
1.21e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 53.75 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1317 LKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEA----KAELQRVLSKANSEVAQWRtkyetdaiQRTEELEEaK 1392
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQwerqRRELESRVAELKEELRQSR--------EKHEELEE-K 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1393 LQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDV----ERSNAAAAALDKKQRNFDKILAEWKQKYEESQ---SELES 1465
Cdd:pfam07888 103 YKELSASSEELSEEKDALLAQRAAHEARIRELEEDIktltQRVLERETELERMKERAKKAGAQRKEEEAERKqlqAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1466 SQKEARSLSTELFKLKNAYEESLEHLETfkrenknLQEEISDLTEQLGEGGKNVHELEKVRKQLEA--EKLE-------- 1535
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITTLTQKLTTAHRKEAENEALLEELRSlqERLNaserkveg 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1536 LQSALEEAEASLEHEEGKILRAQLEfnqiKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDA---------------- 1599
Cdd:pfam07888 256 LGEELSSMAAQRDRTQAELHQARLQ----AAQLTLQLADASLALREGRARWAQERETLQQSAEAdkdrieklsaelqrle 331
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 431907173 1600 ----ETRSRNEALRVKKKMEGDLNemEIQLSQANRTASEAQKHLKIAQ 1643
Cdd:pfam07888 332 erlqEERMEREKLEVELGREKDCN--RVQLSESRRELQELKASLRVAQ 377
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1256-1487 |
1.42e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1256 DQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLTRGKLSYTQQTEDLKRQLEEEGKAKNALAHAL 1335
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1336 QSARHD-CDLLREQYEEETEAKAELqrVLSKANSEVAQWRTKYETDAIQRTEELEEAKLQDAEEaveavnakcssLEKTK 1414
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-----------LAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1415 HRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEES 1487
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1155-1384 |
1.43e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1155 AGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAAlRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVT 1234
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1235 SNMEQIIKA----KANLEKVSRTLEDQANEYRTKL-------EEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQL 1303
Cdd:COG4942 90 KEIAELRAEleaqKEELAELLRALYRLGRQPPLALllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1304 TRGKLSYTQQTEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQ 1383
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
.
gi 431907173 1384 R 1384
Cdd:COG4942 250 A 250
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1387-1701 |
1.53e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 53.42 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1387 ELEEAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIedlmvdVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESS 1466
Cdd:COG5185 242 ESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAES------SKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1467 QKEARslstelFKLKNAYEESLEHLETfkrENKNLQEEISDLTEQLGEGgknvheLEKVRKqlEAEKLELQSALEEAEAS 1546
Cdd:COG5185 316 EQLAA------AEAEQELEESKRETET---GIQNLTAEIEQGQESLTEN------LEAIKE--EIENIVGEVELSKSSEE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1547 LEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEiQLS 1626
Cdd:COG5185 379 LDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVM-REA 457
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1627 QANRTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQE 1701
Cdd:COG5185 458 DEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRA 532
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1234-1584 |
1.64e-06 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 53.48 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1234 TSNMEQIIKAKaNLEKVSRTLEDQANEYRTKLEEAQRSLN-DFTTQQAKLQTENGELARQLEEK-EALISQLTRGKL--S 1309
Cdd:NF033838 48 VTSSGNESQKE-HAKEVESHLEKILSEIQKSLDKRKHTQNvALNKKLSDIKTEYLYELNVLKEKsEAELTSKTKKELdaA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1310 YTQQTEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRvlskANSEVAQWRTKYETDAIQRTEELE 1389
Cdd:NF033838 127 FEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNTYKTLELEI----AESDVEVKKAELELVKEEAKEPRD 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1390 EAKLQDAEEAVEAVNAKCSSLEKTK-HRLQNEIE-DLMVDVERSNAAAAALDKKQRnfDKILAEWKQKYEESQSELESSQ 1467
Cdd:NF033838 203 EEKIKQAKAKVESKKAEATRLEKIKtDREKAEEEaKRRADAKLKEAVEKNVATSEQ--DKPKRRAKRGVLGEPATPDKKE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1468 KEARS---------LSTELFKLKNAYEESLEHLETFKRENKNLQEEisdlteqlgeggKNVHELEKVRKQLEAEKLELQS 1538
Cdd:NF033838 281 NDAKSsdssvgeetLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEE------------DRRNYPTNTYKTLELEIAESDV 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1539 ALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAE----------KDEEMEQAKR 1584
Cdd:NF033838 349 KVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEatrlekiktdRKKAEEEAKR 404
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1473-1691 |
1.78e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1473 LSTELFKLKNAYEESLEHLETFKRENK--NLQEEISDLTEQLGEggknvheLEKVRKQLEAEKLELQSALEEAEASLEHE 1550
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSE-------LESQLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1551 EGKI--LRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVdSLQTSLDA-ETRSRNEALRVKKKMEGDLNEMEIQLSQ 1627
Cdd:COG3206 253 PDALpeLLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVI-ALRAQIAAlRAQLQQEAQRILASLEAELEALQAREAS 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1628 ANRTASEAQKhlKIAQAHLKDTQLQmddavrandDLKENIAIVERRNNLLQAELEELRAVVEQT 1691
Cdd:COG3206 332 LQAQLAQLEA--RLAELPELEAELR---------RLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1205-1949 |
1.97e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 53.90 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1205 LGEQIDnlQRVKQKLEKE-KSEFKLELDDVTSNMEQIIKAKANLEkvsrtledQANEYRTKLEeaqRSLNDFTTQQAKLQ 1283
Cdd:TIGR01612 526 IGFDID--QNIKAKLYKEiEAGLKESYELAKNWKKLIHEIKKELE--------EENEDSIHLE---KEIKDLFDKYLEID 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1284 TEN---GELARQLEEKEALISQltrgKLSYTQQTEDLKR------------------QLEEEGKAKNALAHALQSA---- 1338
Cdd:TIGR01612 593 DEIiyiNKLKLELKEKIKNISD----KNEYIKKAIDLKKiiennnayidelakispyQVPEHLKNKDKIYSTIKSElski 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1339 -RHDCDLL--------REQYEEETEAKAELQRVLSKANSEVAQWR-----------TKYETDAIQRTEELEEAKLQDAEE 1398
Cdd:TIGR01612 669 yEDDIDALynelssivKENAIDNTEDKAKLDDLKSKIDKEYDKIQnmetatvelhlSNIENKKNELLDIIVEIKKHIHGE 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1399 AVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDK------KQRNFDKILAE-WKQKYEESQSELESSQKEAR 1471
Cdd:TIGR01612 749 INKDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEiknhynDQINIDNIKDEdAKQNYDKSKEYIKTISIKED 828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1472 SLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEggknvhELEKVRKQLEAEKLEL--------QSALEEA 1543
Cdd:TIGR01612 829 EIFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAE------LTNKIKAEISDDKLNDyekkfndsKSLINEI 902
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1544 EASLEHEEGKIlraqlefNQIKAEIER-KLAEKDEEMEQAKRNHLRVV-DSLQTSLDAETRSRNEALRVKKKMEGDLNEM 1621
Cdd:TIGR01612 903 NKSIEEEYQNI-------NTLKKVDEYiKICENTKESIEKFHNKQNILkEILNKNIDTIKESNLIEKSYKDKFDNTLIDK 975
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1622 EIQLSQANRTASeaqkhlkiaqahLKDTQLQMDDAVRANDDLKENIAivERRNNLLQAELEElravveqtersRKLAEQE 1701
Cdd:TIGR01612 976 INELDKAFKDAS------------LNDYEAKNNELIKYFNDLKANLG--KNKENMLYHQFDE-----------KEKATND 1030
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1702 LIETSERVqllhsqNTSLINQKKKMESDLTQLQSEVEEAVQ---ECRNAE--EKAKKAITDAAMMAEELK--------KE 1768
Cdd:TIGR01612 1031 IEQKIEDA------NKNIPNIEIAIHTSIYNIIDEIEKEIGkniELLNKEilEEAEINITNFNEIKEKLKhynfddfgKE 1104
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1769 QDT--SAHLERMKKNMEQTIKDLQHRLDEAEQIALKgGKKQLQKLEARVRELENelEAEQKRNAESVKGMRKSERRIkel 1846
Cdd:TIGR01612 1105 ENIkyADEINKIKDDIKNLDQKIDHHIKALEEIKKK-SENYIDEIKAQINDLED--VADKAISNDDPEEIEKKIENI--- 1178
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1847 tyQTEEDKKNllRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHE-LDEAEERADIAESQVNKLRAKSRDIga 1925
Cdd:TIGR01612 1179 --VTKIDKKK--NIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLfLEKIDEEKKKSEHMIKAMEAYIEDL-- 1252
|
810 820
....*....|....*....|....
gi 431907173 1926 kaqlaralyDNTAESPQELSFRRG 1949
Cdd:TIGR01612 1253 ---------DEIKEKSPEIENEMG 1267
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1974-2231 |
2.03e-06 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 53.62 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1974 QQGIVPANRVKLLPAGPTPKPSlsQVP-PAEPGSPYPAPehsnedqevyvvPPPARPCLTSESPA---GPCLPSPDPIYK 2049
Cdd:pfam03154 219 NQTQSTAAPHTLIQQTPTLHPQ--RLPsPHPPLQPMTQP------------PPPSQVSPQPLPQPslhGQMPPMPHSLQT 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2050 ----VPRGSGTQPATPGDALEVYDVPP---AALRVSASGPYDTPASFSHLlarVAPQPPGEDE---APYDVPLAPKPPSE 2119
Cdd:pfam03154 285 gpshMQHPVPPQPFPLTPQSSQSQVPPgpsPAAPGQSQQRIHTPPSQSQL---QSQQPPREQPlppAPLSMPHIKPPPTT 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2120 LEPDL-EWEGGREP----GPPLYAAPSNLKRASALLNL-----------YEAPEELLADGEEggsdegiydvplLGPetP 2183
Cdd:pfam03154 362 PIPQLpNPQSHKHPphlsGPSPFQMNSNLPPPPALKPLsslsthhppsaHPPPLQLMPQSQQ------------LPP--P 427
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 431907173 2184 PSPEPLGALASNDPDTLAlllaRSPPPSHRPRLPSAESLSRRP-LPALP 2231
Cdd:pfam03154 428 PAQPPVLTQSQSLPPPAA----SHPPTSGLHQVPSQSPFPQHPfVPGGP 472
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1975-2225 |
2.04e-06 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 53.64 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1975 QGIVPA--NRVKLLPAGPTPKPSLSQVPPAEPGS---PYPAPEHSNEDQEVyvVPPPARPCLTSESPAGPCLPSPDPiyK 2049
Cdd:PHA03307 761 PSLVPAklAEALALLEPAEPQRGAGSSPPVRAEAafrRPGRLRRSGPAADA--ASRTASKRKSRSHTPDGGSESSGP--A 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2050 VPRGSGTQPAtPGDALEVYDVPPAALRVSASGPYDTPASFSHLLAR---VAPQPPGEDEAPYDVPLAPKPPSELEPDL-- 2124
Cdd:PHA03307 837 RPPGAAARPP-PARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRArpgAAAPPKAAAAAPPAGAPAPRPRPAPRVKLgp 915
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2125 -------EWEGGRE--PGPPLYAAPSnlkrASAlLNLYEAPE---ELLadgeeggsdegiyDVPLLgpetppsPEPLGAL 2192
Cdd:PHA03307 916 mppggpdPRGGFRRvpPGDLHTPAPS----AAA-LAAYCPPEvvaELV-------------DHPLF-------PEPWRPA 970
|
250 260 270
....*....|....*....|....*....|....*...
gi 431907173 2193 ASNDPDTLALLLARSPPPSHRPR-----LPSAESLSRR 2225
Cdd:PHA03307 971 LAFDPEALAEIAARCGGPPPRSGsafgpLRASGPLRRR 1008
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
869-1336 |
2.10e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 53.22 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 869 EARRKELEEKMVSLLQEKNDLQLQVQAEQDNLndaeercdQLIKNKIQLEAkvKEMNERLEDEEEMNAELTAKKRKLede 948
Cdd:pfam07111 241 ELERQELLDTMQHLQEDRADLQATVELLQVRV--------QSLTHMLALQE--EELTRKIQPSDSLEPEFPKKCRSL--- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 949 cseLKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTL------ 1022
Cdd:pfam07111 308 ---LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLqmelsr 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1023 -TKSKVKLEQQVDDLEgslEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKefdisqqnskiedeQA 1101
Cdd:pfam07111 385 aQEARRRQQQQTASAE---EQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKV--------------HT 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1102 LALQLQKKLKENQARIEELEEELEAertarakvEKLRSDLSRELEEISE---RL--EEAGGATSVQIEMNKKREaEFQKM 1176
Cdd:pfam07111 448 IKGLMARKVALAQLRQESCPPPPPA--------PPVDADLSLELEQLREernRLdaELQLSAHLIQQEVGRARE-QGEAE 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1177 RRDLEEATLQHEATAaalrKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELddvtsNMEQIIKAKANLEKVSRTled 1256
Cdd:pfam07111 519 RQQLSEVAQQLEQEL----QRAQESLASVGQQLEVARQGQQESTEEAASLRQEL-----TQQQEIYGQALQEKVAEV--- 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1257 qANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLTR-GKLSYTQQTEDLKRQLEEEGKAKNALAHAL 1335
Cdd:pfam07111 587 -ETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRlQDEARKEEGQRLARRVQELERDKNLMLATL 665
|
.
gi 431907173 1336 Q 1336
Cdd:pfam07111 666 Q 666
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
837-1091 |
2.14e-06 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 52.76 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 837 KIKPL----LKSAETEKEMANMKEEFGRLKETLEKSEARRKELEEKM-----VSLL----QEKNDLQLQVQAEQDNLNDA 903
Cdd:pfam15742 91 KIRELelevLKQAQSIKSQNSLQEKLAQEKSRVADAEEKILELQQKLehahkVCLTdtciLEKKQLEERIKEASENEAKL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 904 EERCDQLIKNKIQLEAKVKEMNERLEDeeemnaeLTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEe 983
Cdd:pfam15742 171 KQQYQEEQQKRKLLDQNVNELQQQVRS-------LQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQE- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 984 magLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNtltkskvkleqqvddlEGSLEQEKKVRmdleRAKRKLEGDLKL 1063
Cdd:pfam15742 243 ---LSEKLSSLQQEKEALQEELQQVLKQLDVHVRKYN----------------EKHHHHKAKLR----RAKDRLVHEVEQ 299
|
250 260
....*....|....*....|....*...
gi 431907173 1064 TQESIMDLENDKLQLEEKLKKKEFDISQ 1091
Cdd:pfam15742 300 RDERIKQLENEIGILQQQSEKEKAFQKQ 327
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1258-1927 |
2.26e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1258 ANEYRTKLEEA---QRSLNDFTTQQAKLQTENGELARQLEEKEALISQLTrgklsytQQTEDLKRQLEeegKAKNALAHA 1334
Cdd:PRK04863 278 ANERRVHLEEAlelRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLE-------QDYQAASDHLN---LVQTALRQQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1335 LQSARHDCDL--LREQYEEETEA-------KAELQRVLSKANSEVAQWRTKYeTDAIQRTEELEEAKLQ--DAEEAVEAV 1403
Cdd:PRK04863 348 EKIERYQADLeeLEERLEEQNEVveeadeqQEENEARAEAAEEEVDELKSQL-ADYQQALDVQQTRAIQyqQAVQALERA 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1404 NAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKE-----ARSLSTELF 1478
Cdd:PRK04863 427 KQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSeawdvARELLRRLR 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1479 KLKN------AYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAeasleHEEG 1552
Cdd:PRK04863 507 EQRHlaeqlqQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEA-----RERR 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1553 KILRAQLEfnQIKAEIERKLAEKDEEME-QAKRNHLR------------VVDSLQTSLDAE---TRSRNEALRVKKKMEG 1616
Cdd:PRK04863 582 MALRQQLE--QLQARIQRLAARAPAWLAaQDALARLReqsgeefedsqdVTEYMQQLLERErelTVERDELAARKQALDE 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1617 DLNEmeiqLSQANRTASEAQKHLK-----IAQAHLKDtQLQMDDA---------------VR----------ANDDLKEN 1666
Cdd:PRK04863 660 EIER----LSQPGGSEDPRLNALAerfggVLLSEIYD-DVSLEDApyfsalygparhaivVPdlsdaaeqlaGLEDCPED 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1667 IAIVER-----RNNLLQAELEElRAVV----------------------------EQTERSRKLAEQELIETSERVQL-- 1711
Cdd:PRK04863 735 LYLIEGdpdsfDDSVFSVEELE-KAVVvkiadrqwrysrfpevplfgraarekriEQLRAEREELAERYATLSFDVQKlq 813
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1712 -LHSQNTSLINQKKKM------ESDLTQLQ---SEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERmkKN 1781
Cdd:PRK04863 814 rLHQAFSRFIGSHLAVafeadpEAELRQLNrrrVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLAD--ET 891
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1782 MEQTIKDLQHRLDEAEQ----IALKGGK-KQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTE----- 1851
Cdd:PRK04863 892 LADRVEEIREQLDEAEEakrfVQQHGNAlAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahf 971
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 431907173 1852 --EDKKNLL-RLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKA 1927
Cdd:PRK04863 972 syEDAAEMLaKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPA 1050
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
653-677 |
2.31e-06 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 50.04 E-value: 2.31e-06
10 20
....*....|....*....|....*
gi 431907173 653 HRENLNKLMTNLKTTHPHFVRCIIP 677
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
900-1904 |
2.41e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 53.30 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 900 LNDAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLElTLAKVEKE----KHATEN 975
Cdd:PTZ00440 493 DSNYQEKVDELLQIINSIKEKNNIVNNNFKNIEDYYITIEGLKNEIEGLIELIKYYLQSIE-TLIKDEKLkrsmKNDIKN 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 976 KVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEgsleqekkvrmdlerakr 1055
Cdd:PTZ00440 572 KIKYIEENVDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFY------------------ 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1056 klEGDLKLtqesimdLENDKLQLEEKLKkkefDISQQNSKIEDEQalalQLQKKLKENQarieeleeeleaertarAKVE 1135
Cdd:PTZ00440 634 --KGDLQE-------LLDELSHFLDDHK----YLYHEAKSKEDLQ----TLLNTSKNEY-----------------EKLE 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1136 KLRSDlsrELEEISERLE-EAGGATSVQIEMNKKreaEFQKMRRDLEEATLQHEATAAALRKkhadSVAELGEQIDNLQR 1214
Cdd:PTZ00440 680 FMKSD---NIDNIIKNLKkELQNLLSLKENIIKK---QLNNIEQDISNSLNQYTIKYNDLKS----SIEEYKEEEEKLEV 749
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1215 VKQKLEKEKSEFKLELD-------DVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENG 1287
Cdd:PTZ00440 750 YKHQIINRKNEFILHLYendkdlpDGKNTYEEFLQYKDTILNKENKISNDINILKENKKNNQDLLNSYNILIQKLEAHTE 829
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1288 ELARQL---------EEKEALISQLTRGKLSYTQQTEDLKRQLEEEGKAKNALaHALQSARHDCDLLREQYEEETEAKAE 1358
Cdd:PTZ00440 830 KNDEELkqllqkfptEDENLNLKELEKEFNENNQIVDNIIKDIENMNKNINII-KTLNIAINRSNSNKQLVEHLLNNKID 908
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1359 LQRVLSKANSEVaqwrTKYETDAIQRTEELEeaklqdaeeaveavnakcSSLEKTKHRLQNEIEDlmvdvERSNAAAAAL 1438
Cdd:PTZ00440 909 LKNKLEQHMKII----NTDNIIQKNEKLNLL------------------NNLNKEKEKIEKQLSD-----TKINNLKMQI 961
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1439 DKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNlqeEISDLTEQLGEG-GK 1517
Cdd:PTZ00440 962 EKTLEYYDKSKENINGNDGTHLEKLDKEKDEWEHFKSEIDKLNVNYNILNKKIDDLIKKQHD---DIIELIDKLIKEkGK 1038
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1518 NVHE-LEKVRKQLEAEKLELQSaLEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHlrvvDSLQTS 1596
Cdd:PTZ00440 1039 EIEEkVDQYISLLEKMKTKLSS-FHFNIDIKKYKNPKIKEEIKLLEEKVEALLKKIDENKNKLIEIKNKS----HEHVVN 1113
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1597 LDAETRSRNEALRVKKKMEGDLNE-MEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDavranddlkeniaIVERRNN 1675
Cdd:PTZ00440 1114 ADKEKNKQTEHYNKKKKSLEKIYKqMEKTLKELENMNLEDITLNEVNEIEIEYERILIDH-------------IVEQINN 1180
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1676 llqaELEELRAVVEQTERSRKLAEQelietservqllhsqntSLINQKKKMESDLTQLqsEVEEAVQECRNAEEKAKKAI 1755
Cdd:PTZ00440 1181 ----EAKKSKTIMEEIESYKKDIDQ-----------------VKKNMSKERNDHLTTF--EYNAYYDKATASYENIEELT 1237
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1756 TDaammAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEqialkggkkqlqKLEARVRELENELEAEQKRNAESV-K 1834
Cdd:PTZ00440 1238 TE----AKGLKGEANRSTNVDELKEIKLQVFSYLQQVIKENN------------KMENALHEIKNMYEFLISIDSEKIlK 1301
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1835 GMRKSERRIKELTYQTeedKKNLLRLQDLVDKLQLKV---KAYKRQAEEAEE--QANTNLSKFRKVQHELDEAEE 1904
Cdd:PTZ00440 1302 EILNSTKKAEEFSNDA---KKELEKTDNLIKQVEAKIeqaKEHKNKIYGSLEdkQIDDEIKKIEQIKEEISNKRK 1373
|
|
| SH3_GRB2_C |
cd11949 |
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical ... |
1930-1984 |
2.72e-06 |
|
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. It is ubiquitously expressed in all tissues throughout development and is important in cell cycle progression, motility, morphogenesis, and angiogenesis. In lymphocytes, GRB2 is associated with antigen receptor signaling components. GRB2 contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domain of GRB2 binds to Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, as well as to the proline-rich C-terminus of FGRF2. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212882 [Multi-domain] Cd Length: 53 Bit Score: 46.37 E-value: 2.72e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGAGGLDGWClcslHGQQGIVPANRVK 1984
Cdd:cd11949 2 VQALFDFDPQEDGELGFRRGDFIEVMDNSDPNWWKGAC----HGQTGMFPRNYVT 52
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1574-1958 |
3.11e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.20 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1574 EKDEEMEQAKRNHLRVVDS---LQTSLDAETRSRNEALR----VKKKMEGDLNEMEIQLSQANRTASEAQKH---LKIAQ 1643
Cdd:pfam07888 10 EEESHGEEGGTDMLLVVPRaelLQNRLEECLQERAELLQaqeaANRQREKEKERYKRDREQWERQRRELESRvaeLKEEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1644 AHLKDTQLQMDDAVRANDDLKENIAivERRNNLLQAELEELRAVVEQTERSRKLAEQELiETSERVQLLHSQNTSLINQK 1723
Cdd:pfam07888 90 RQSREKHEELEEKYKELSASSEELS--EEKDALLAQRAAHEARIRELEEDIKTLTQRVL-ERETELERMKERAKKAGAQR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1724 KKMESDLTQLQSEVEEAVQECRNaeekakkaitdaamMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQ--IAL 1801
Cdd:pfam07888 167 KEEEAERKQLQAKLQQTEEELRS--------------LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRkeAEN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1802 KGGKKQLQKLEARVRELENELEAeQKRNAESVKGMRksERRIKELTYQTEEDKKNLLRLQDLvdKLQLKVKAYKRQAEEA 1881
Cdd:pfam07888 233 EALLEELRSLQERLNASERKVEG-LGEELSSMAAQR--DRTQAELHQARLQAAQLTLQLADA--SLALREGRARWAQERE 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 431907173 1882 EEQANTNLSKFR--KVQHELDEAEERADIAESQVNKLRAksrDIGAKAQLARALYDNTAESPQELSfrrgDVLRVLQRE 1958
Cdd:pfam07888 308 TLQQSAEADKDRieKLSAELQRLEERLQEERMEREKLEV---ELGREKDCNRVQLSESRRELQELK----ASLRVAQKE 379
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
893-1115 |
3.21e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 893 VQAEqDNLNDAEERCDQLIKNKIQLEAKVKEMNERLEdeeemnaELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHA 972
Cdd:COG3883 12 AFAD-PQIQAKQKELSELQAELEAAQAELDALQAELE-------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 973 TENKVKNLTEEM----------------AGLDEIIAKLTKEKKaLQEAHQQALDDLQAEedkvntltksKVKLEQQVDDL 1036
Cdd:COG3883 84 RREELGERARALyrsggsvsyldvllgsESFSDFLDRLSALSK-IADADADLLEELKAD----------KAELEAKKAEL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 431907173 1037 EGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQA 1115
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1130-1363 |
3.23e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 51.46 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1130 ARAKVEKLRSDLSRELEEISERLEEaggatsvqiEMNKKR--EAEFQKMRRDLEEATLQH---EATA-------AALRKK 1197
Cdd:pfam00038 69 ERARLQLELDNLRLAAEDFRQKYED---------ELNLRTsaENDLVGLRKDLDEATLARvdlEAKIeslkeelAFLKKN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1198 HADSVAELGEQIDNLQRVkqklekeksefkLELDDVTS-NMEQIIK-AKANLEKVSRTLEDQANE-YRTKLEEAQRSLND 1274
Cdd:pfam00038 140 HEEEVRELQAQVSDTQVN------------VEMDAARKlDLTSALAeIRAQYEEIAAKNREEAEEwYQSKLEELQQAAAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1275 FTTQQAKLQTENGELARQLEEKEALISQLTRgklsytqQTEDLKRQLEEegkAKNALAHALQSARhdcDLLREQYEEETE 1354
Cdd:pfam00038 208 NGDALRSAKEEITELRRTIQSLEIELQSLKK-------QKASLERQLAE---TEERYELQLADYQ---ELISELEAELQE 274
|
....*....
gi 431907173 1355 AKAELQRVL 1363
Cdd:pfam00038 275 TRQEMARQL 283
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
861-1096 |
3.64e-06 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 52.47 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 861 LKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAeqdnlNDAEERCDQLIKNKIQLEAKVKEMNERLEDeeeMNAELTA 940
Cdd:pfam18971 619 LEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQA-----NSQKDEIFALINKEANRDARAIAYTQNLKG---IKRELSD 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 941 KKRKLEDECSELKRDIDDLE----LTLAKVEKEKHATENKVKNLteemaGLD-EIIAKLTKEKKALQEAHQQALDDL--- 1012
Cdd:pfam18971 691 KLEKISKDLKDFSKSFDEFKngknKDFSKAEETLKALKGSVKDL-----GINpEWISKVENLNAALNEFKNGKNKDFskv 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1013 -QAEEDKVNTLtkSKVKLEQQVDDLEGSLEQEKKVrmdlerakRKLEGDLKLTQESIMDLEN-DKLQLEEKLKKKEFDIS 1090
Cdd:pfam18971 766 tQAKSDLENSV--KDVIINQKVTDKVDNLNQAVSV--------AKAMGDFSRVEQVLADLKNfSKEQLAQQAQKNEDFNT 835
|
....*.
gi 431907173 1091 QQNSKI 1096
Cdd:pfam18971 836 GKNSEL 841
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
843-1086 |
4.15e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.06 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 843 KSAETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKN-------KI 915
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKvkelkeeRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 916 QLEAKVKEMNERLEDEEEMNAELTAKKRKLEdecsELKRDIDDLE-----------------LTLAKVEKEKHATE---- 974
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGGSID----KLRKEIERLEwrqqtevlspeeekelvEKIKELEKELEKAKkale 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 975 --NKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDL-----QAEE--DKVNTLTKSKVKLEQQVDDLEGSL-EQEK 1044
Cdd:COG1340 158 knEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMielykEADElrKEADELHKEIVEAQEKADELHEEIiELQK 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 431907173 1045 KVR--MDLERAKRKLEGDLKLTQESiMDLENDKLQLEEKLKKKE 1086
Cdd:COG1340 238 ELRelRKELKKLRKKQRALKREKEK-EELEEKAEEIFEKLKKGE 280
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1022-1444 |
4.59e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 52.05 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1022 LTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEfdisqqnskiedeqa 1101
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAE--------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1102 laLQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGAtsvQIEMNKKR-EAEFQKMRRDL 1180
Cdd:pfam05557 69 --EALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA---ELELQSTNsELEELQERLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1181 EEATLQ-HEATAAALRKKHaDSVAELGEQIDNLQRVKQKLEKEKSEFK------LELDDVTSNMEQIIKAKANLEKVSRT 1253
Cdd:pfam05557 144 LKAKASeAEQLRQNLEKQQ-SSLAEAEQRIKELEFEIQSQEQDSEIVKnskselARIPELEKELERLREHNKHLNENIEN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1254 ---LEDQANEYRTKLEEAQrslnDFTTQQAKLQTENGELARQLEEKEAL-----------------ISQLTRGKLSYTQQ 1313
Cdd:pfam05557 223 kllLKEEVEDLKRKLEREE----KYREEAATLELEKEKLEQELQSWVKLaqdtglnlrspedlsrrIEQLQQREIVLKEE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1314 TEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYET-DAIQRTEELEEAK 1392
Cdd:pfam05557 299 NSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESyDKELTMSNYSPQL 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 431907173 1393 LQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRN 1444
Cdd:pfam05557 379 LERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQ 430
|
|
| SH3_SPIN90 |
cd11849 |
Src homology 3 domain of SH3 protein interacting with Nck, 90 kDa (SPIN90); SPIN90 is also ... |
1931-1984 |
4.83e-06 |
|
Src homology 3 domain of SH3 protein interacting with Nck, 90 kDa (SPIN90); SPIN90 is also called NCK interacting protein with SH3 domain (NCKIPSD), Dia-interacting protein (DIP), 54 kDa vimentin-interacting protein (VIP54), or WASP-interacting SH3-domain protein (WISH). It is an F-actin binding protein that regulates actin polymerization and endocytosis. It associates with the Arp2/3 complex near actin filaments and determines filament localization at the leading edge of lamellipodia. SPIN90 is expressed in the early stages of neuronal differentiation and plays a role in regulating growth cone dynamics and neurite outgrowth. It also interacts with IRSp53 and regulates cell motility by playing a role in the formation of membrane protrusions. SPIN90 contains an N-terminal SH3 domain, a proline-rich domain, and a C-terminal VCA (verprolin-homology and cofilin-like acidic) domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212783 [Multi-domain] Cd Length: 53 Bit Score: 45.77 E-value: 4.83e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGAggldGWCLCSLH-GQQGIVPANRVK 1984
Cdd:cd11849 3 RALYDFKSAEPNTLSFSEGETFLLLERSNA----HWWLVTNHsGETGYVPANYVK 53
|
|
| SH3_DNMBP_C2 |
cd12141 |
Second C-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba, and ... |
1932-1981 |
4.85e-06 |
|
Second C-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba, and similar domains; DNMBP or Tuba is a cdc42-specific guanine nucleotide exchange factor (GEF) that contains four N-terminal SH3 domains, a central RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. It provides a functional link between dynamin, Rho GTPase signaling, and actin dynamics. It plays an important role in regulating cell junction configuration. The C-terminal SH3 domains of DNMBP bind to N-WASP and Ena/VASP proteins, which are key regulatory proteins of the actin cytoskeleton. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 213017 [Multi-domain] Cd Length: 57 Bit Score: 45.95 E-value: 4.85e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQREGAGGLDGWCLCSLHGQQGIVPAN 1981
Cdd:cd12141 4 AVYTFKARSPNELSVSANQRVRILEFSDLTGNKEWWLAEANGQKGYVPSN 53
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1973-2174 |
5.16e-06 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 51.91 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1973 GQQGIVPANRVKLLPAGPTPKPSLSQVPPAEPGSPYPAPEHSNEDQEVYVVPPPARPCLTSESPAGPCLPSPDPIYKVPR 2052
Cdd:PRK07764 594 AAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKA 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2053 GSGTQPATPGDALEVYDVPPA--ALRVSASGPYDTPASFSHLLARVAPQPPGEDEAP------YDVPLAPKPPSELEPDL 2124
Cdd:PRK07764 674 GGAAPAAPPPAPAPAAPAAPAgaAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASApspaadDPVPLPPEPDDPPDPAG 753
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 431907173 2125 EWEGGR-EPGPPLYAAPSNLKRASALlnlyEAPEELLADGEEGGSDEGIYD 2174
Cdd:PRK07764 754 APAQPPpPPAPAPAAAPAAAPPPSPP----SEEEEMAEDDAPSMDDEDRRD 800
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1521-1737 |
5.24e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 5.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1521 ELEKVRKQLEAEKLELQSALEEAEASLEH-----------EEGKILRAQLefnqikAEIERKLAEKDEEMEQAKRNhlrv 1589
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlsEEAKLLLQQL------SELESQLAEARAELAEAEAR---- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1590 VDSLQTSLDAETRSRNEALR--VKKKMEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDAV-RANDDLKEN 1666
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAqRILASLEAE 321
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 431907173 1667 IAIVERRNNLLQAELEELRAVVEQTERsrklAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEV 1737
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| SH3_Endophilin_A |
cd11803 |
Src homology 3 domain of Endophilin-A; Endophilins play roles in synaptic vesicle formation, ... |
1930-1986 |
5.44e-06 |
|
Src homology 3 domain of Endophilin-A; Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms (A1, A2, and A3). Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. They tubulate membranes and regulate calcium influx into neurons to trigger the activation of the endocytic machinery. They are also involved in the sorting of plasma membrane proteins, actin filament assembly, and the uncoating of clathrin-coated vesicles for fusion with endosomes. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212737 [Multi-domain] Cd Length: 55 Bit Score: 45.71 E-value: 5.44e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQRegaggLD-GWCLCSLHGQQGIVPANRVKLL 1986
Cdd:cd11803 3 CRALYDFEPENEGELGFKEGDIITLTNQ-----IDeNWYEGMVNGQSGFFPVNYVEVL 55
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1003-1187 |
5.67e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1003 EAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQekkvrmdLERAKRKLEGDLKLTQESIMDLENDKLQLEEKL 1082
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1083 KKKEfdiSQQNSKIEDEQALALQ-----LQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGG 1157
Cdd:COG1579 76 KKYE---EQLGNVRNNKEYEALQkeiesLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170 180 190
....*....|....*....|....*....|
gi 431907173 1158 ATSVQIEmnkKREAEFQKMRRDLEEATLQH 1187
Cdd:COG1579 153 ELEAELE---ELEAEREELAAKIPPELLAL 179
|
|
| SH3_RUSC2 |
cd11957 |
Src homology 3 domain of RUN and SH3 domain-containing protein 2; RUSC2, also called Iporin or ... |
1931-1979 |
5.69e-06 |
|
Src homology 3 domain of RUN and SH3 domain-containing protein 2; RUSC2, also called Iporin or Interacting protein of Rab1, is expressed ubiquitously with highest amounts in the brain and testis. It interacts with the small GTPase Rab1 and the Golgi matrix protein GM130, and may function in linking GTPases to certain intracellular signaling pathways. RUSC proteins are adaptor proteins consisting of RUN, leucine zipper, and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212890 Cd Length: 52 Bit Score: 45.68 E-value: 5.69e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGAggldGWCLCSLHGQQGIVP 1979
Cdd:cd11957 3 KALCHHIATEPGQLSFNKGDILQVLSRADG----DWLRCSLGPDSGLVP 47
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
846-1929 |
5.87e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 52.14 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 846 ETEKEMANMKEEfgrLKETLEKSEarrkELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMN 925
Cdd:PTZ00440 557 KDEKLKRSMKND---IKNKIKYIE----ENVDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYIL 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 926 ERLEdeeemnaeltakKRKLEDECSELKRDIDDLEltlaKVEKEKHATENkVKNLteemagLDEIIAKLTKEKKALQEAH 1005
Cdd:PTZ00440 630 NKFY------------KGDLQELLDELSHFLDDHK----YLYHEAKSKED-LQTL------LNTSKNEYEKLEFMKSDNI 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1006 QQALDDLQAEEDKVNTL----------------TKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKltqESIM 1069
Cdd:PTZ00440 687 DNIIKNLKKELQNLLSLkeniikkqlnnieqdiSNSLNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKN---EFIL 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1070 DL-ENDKLQLEEKLKKKEF-----DISQQNSKIEDEqalALQLQKKLKENQARIEELEEELEAERT----ARAKVEKLRS 1139
Cdd:PTZ00440 764 HLyENDKDLPDGKNTYEEFlqykdTILNKENKISND---INILKENKKNNQDLLNSYNILIQKLEAhtekNDEELKQLLQ 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1140 DLSRELEEISERLEEAGGATSVQI---------EMNKKREA----EFQKMRRDLEEATLQHEAT-AAALRKKHADSVAEL 1205
Cdd:PTZ00440 841 KFPTEDENLNLKELEKEFNENNQIvdniikdieNMNKNINIiktlNIAINRSNSNKQLVEHLLNnKIDLKNKLEQHMKII 920
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1206 GE----QIDNLQRVKQKLEKEKSEFKLELDDVTSN---------MEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSL 1272
Cdd:PTZ00440 921 NTdniiQKNEKLNLLNNLNKEKEKIEKQLSDTKINnlkmqiektLEYYDKSKENINGNDGTHLEKLDKEKDEWEHFKSEI 1000
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1273 NDFTTQQAKLQTE-NGELARQLEEKEALISQLTRGKLSYTQQTEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEE 1351
Cdd:PTZ00440 1001 DKLNVNYNILNKKiDDLIKKQHDDIIELIDKLIKEKGKEIEEKVDQYISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIK 1080
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1352 ETEAKAE-LQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKlqdaeeavEAVNAKCSSLEKTKHRLQNEIEDLmVDVER 1430
Cdd:PTZ00440 1081 LLEEKVEaLLKKIDENKNKLIEIKNKSHEHVVNADKEKNKQT--------EHYNKKKKSLEKIYKQMEKTLKEL-ENMNL 1151
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1431 SNAAAAALDKKQRNFDKILaewkqkyeesqselessqkearslstelfklknaYEESLEHLETFKRENKNLQEEISDLTE 1510
Cdd:PTZ00440 1152 EDITLNEVNEIEIEYERIL----------------------------------IDHIVEQINNEAKKSKTIMEEIESYKK 1197
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1511 QLGEGGKNVHElekvrkqleaeklELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVV 1590
Cdd:PTZ00440 1198 DIDQVKKNMSK-------------ERNDHLTTFEYNAYYDKATASYENIEELTTEAKGLKGEANRSTNVDELKEIKLQVF 1264
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1591 DSLQTSLDaETRSRNEALRVKKKMEGDLnemeiQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKENIAIV 1670
Cdd:PTZ00440 1265 SYLQQVIK-ENNKMENALHEIKNMYEFL-----ISIDSEKILKEILNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQA 1338
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1671 ERRNNLLQAELEElravvEQTErsrklaeqelietsERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEk 1750
Cdd:PTZ00440 1339 KEHKNKIYGSLED-----KQID--------------DEIKKIEQIKEEISNKRKEINKYLSNIKSNKEKCDLHVRNASR- 1398
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1751 aKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKggKKQLQKLEarvRELENELeaeqkrNA 1830
Cdd:PTZ00440 1399 -GKDKIDFLNKHEAIEPSNSKEVNIIKITDNINKCKQYSNEAMETENKADEN--NDSIIKYE---KEITNIL------NN 1466
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1831 ESVKGMR-KSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQA--EEAEEQANTNLSK---------FRKVQHE 1898
Cdd:PTZ00440 1467 SSILGKKtKLEKKKKEATNIMDDINGEHSIIKTKLTKSSEKLNQLNEQPniKREGDVLNNDKSTiayetiqynLGRVKHN 1546
|
1130 1140 1150
....*....|....*....|....*....|.
gi 431907173 1899 LDEAEERADIAESQVNKLRAKSRDIGAKAQL 1929
Cdd:PTZ00440 1547 LLNILNIKDEIETILNKAQDLMRDISKISKI 1577
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1079-1330 |
6.27e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1079 EEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEEleeeleaertARAKVEKLRsdlsRELEEISERLEEAgga 1158
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE----------LQAELEALQ----AEIDKLQAEIAEA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1159 tsvQIEMNKKREaEFQKMRRDLEEATLQHEATAAALrkkHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNME 1238
Cdd:COG3883 78 ---EAEIEERRE-ELGERARALYRSGGSVSYLDVLL---GSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1239 QIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLTRGKLSYTQQTEDLK 1318
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250
....*....|..
gi 431907173 1319 RQLEEEGKAKNA 1330
Cdd:COG3883 231 AAAAAAAAAAAA 242
|
|
| SH3_ASPP |
cd11807 |
Src homology 3 domain of Apoptosis Stimulating of p53 proteins (ASPP); The ASPP family of ... |
1932-1981 |
6.36e-06 |
|
Src homology 3 domain of Apoptosis Stimulating of p53 proteins (ASPP); The ASPP family of proteins bind to important regulators of apoptosis (p53, Bcl-2, and RelA) and cell growth (APCL, PP1). They share similarity at their C-termini, where they harbor a proline-rich region, four ankyrin (ANK) repeats, and an SH3 domain. Vertebrates contain three members of the family: ASPP1, ASPP2, and iASPP. ASPP1 and ASPP2 activate the apoptotic function of the p53 family of tumor suppressors (p53, p63, and p73), while iASPP is an oncoprotein that specifically inhibits p53-induced apoptosis. The expression of ASPP proteins is altered in tumors; ASPP1 and ASPP2 are downregulated whereas iASPP is upregulated is some cancer types. ASPP proteins also bind and regulate protein phosphatase 1 (PP1), and this binding is competitive with p53 binding. The SH3 domain and the ANK repeats of ASPP contribute to the p53 binding site; they bind to the DNA binding domain of p53. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212741 [Multi-domain] Cd Length: 57 Bit Score: 45.45 E-value: 6.36e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQREGAGGLDgWCLCSLHGQQGIVPAN 1981
Cdd:cd11807 5 ALFDYEAENGDELSFREGDELTVLRKGDDDETE-WWWARLNDKEGYVPRN 53
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1591-1803 |
6.74e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1591 DSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKENIAIV 1670
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1671 ER------RNNLLQ--------AELEELRAVVEQTERSRKLAEQELIETSERvqlLHSQNTSLINQKKKMESDLTQLQSE 1736
Cdd:COG4942 110 LRalyrlgRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAE---LAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1737 ---VEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQHRLDEAEQIALKG 1803
Cdd:COG4942 187 raaLEALKAERQKLLARLEKELAELAAELAELQQEAEE---LEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
767-1112 |
7.23e-06 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 51.49 E-value: 7.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 767 FKAGLLGLLEEMR---------DERLSRIITRIQaqargqlmRIEFKKMVERRDALLVIQWNIRAFMGVKNWPWMKLYF- 836
Cdd:pfam15818 5 FKTSLLEALEELRmrreaetqyEEQIGKIIVETQ--------ELKWQKETLQNQKETLAKQHKEAMAVFKKQLQMKMCAl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 837 ---KIKPLLKSAETEKEMANmkeefgrLKETLEKSEARRKELEEKmVSLLQEKndLQLQVQAEQD---NLNDAEeRCDQL 910
Cdd:pfam15818 77 eeeKGKYQLATEIKEKEIEG-------LKETLKALQVSKYSLQKK-VSEMEQK--LQLHLLAKEDhhkQLNEIE-KYYAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 911 IKNKIQLeakVKEMNERLE----DEEEMNAELTAKKRKLEDECSELKRDIDDL--ELTLAKVE-KEKHATEN-------- 975
Cdd:pfam15818 146 ITGQFGL---VKENHGKLEqnvqEAIQLNKRLSALNKKQESEICSLKKELKKVtsDLIKSKVTcQYKMGEENinltikeq 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 976 KVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEgslEQEKKVRMDLERAKR 1055
Cdd:pfam15818 223 KFQELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALK---ENNQTLERDNELQRE 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1056 KLegdlKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKE 1112
Cdd:pfam15818 300 KV----KENEEKFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQE 352
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
848-1641 |
7.55e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 51.76 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 848 EKEMAN----MKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKE 923
Cdd:PTZ00440 716 EQDISNslnqYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNKENK 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 924 MN------------------------ERLEDEEEMNAE-------------LTAKKRKLEDECSELKRDID----DLEL- 961
Cdd:PTZ00440 796 ISndinilkenkknnqdllnsyniliQKLEAHTEKNDEelkqllqkfptedENLNLKELEKEFNENNQIVDniikDIENm 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 962 -----TLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQ-------EAHQQALDDLQAEEDKVNT------LT 1023
Cdd:PTZ00440 876 nkninIIKTLNIAINRSNSNKQLVEHLLNNKIDLKNKLEQHMKIINtdniiqkNEKLNLLNNLNKEKEKIEKqlsdtkIN 955
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1024 KSKVKLEQQVD-----------DLEGSLEQEKKVRMDLERAKRKLEG---DLKLTQESIMDL----ENDKLQLEEKL-KK 1084
Cdd:PTZ00440 956 NLKMQIEKTLEyydkskeningNDGTHLEKLDKEKDEWEHFKSEIDKlnvNYNILNKKIDDLikkqHDDIIELIDKLiKE 1035
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1085 KEFDIsqqNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEE-----AGGAT 1159
Cdd:PTZ00440 1036 KGKEI---EEKVDQYISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEALLKKIDENKNKLIEiknksHEHVV 1112
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1160 SVQIEMNKKREAeFQKMRRDLEEATLQHEATAAALRKKH-----ADSVAELGEQIDNL--QRVKQKLEKEKSEFKLELDD 1232
Cdd:PTZ00440 1113 NADKEKNKQTEH-YNKKKKSLEKIYKQMEKTLKELENMNleditLNEVNEIEIEYERIliDHIVEQINNEAKKSKTIMEE 1191
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1233 VTSNMEQIIKAKANL--EKVSRTLEDQANEYRTKLEEAQRSLNDFTTqQAKLQTENGELARQLEEKEALISQLTRGKLSY 1310
Cdd:PTZ00440 1192 IESYKKDIDQVKKNMskERNDHLTTFEYNAYYDKATASYENIEELTT-EAKGLKGEANRSTNVDELKEIKLQVFSYLQQV 1270
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1311 TQQTEDLKRQLEE-------------EGKAKNALAHALQSARHDCDLLREqYEEETEAKAELQRVLSKANSEVAQWRTKY 1377
Cdd:PTZ00440 1271 IKENNKMENALHEiknmyeflisidsEKILKEILNSTKKAEEFSNDAKKE-LEKTDNLIKQVEAKIEQAKEHKNKIYGSL 1349
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1378 ETDAIQRTEELEEAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEdlmvDVERSNAAAAALDKKQRNFDKILAEWK-QKY 1456
Cdd:PTZ00440 1350 EDKQIDDEIKKIEQIKEEISNKRKEINKYLSNIKSNKEKCDLHVR----NASRGKDKIDFLNKHEAIEPSNSKEVNiIKI 1425
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1457 EESQSELESSQKEARSLSTELFKLKNA---YEESLEH-------------LETFKRENKNLQEEI----SDLTEQLGEGG 1516
Cdd:PTZ00440 1426 TDNINKCKQYSNEAMETENKADENNDSiikYEKEITNilnnssilgkktkLEKKKKEATNIMDDIngehSIIKTKLTKSS 1505
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1517 KNVHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTS 1596
Cdd:PTZ00440 1506 EKLNQLNEQPNIKREGDVLNNDKSTIAYETIQYNLGRVKHNLLNILNIKDEIETILNKAQDLMRDISKISKIVENKNLEN 1585
|
890 900 910 920
....*....|....*....|....*....|....*....|....*....
gi 431907173 1597 LDAETRSRNEALR----VKKKMEGDLNEMEIQLSQANRTASEAQKHLKI 1641
Cdd:PTZ00440 1586 LNDKEADYVKYLDnilkEKQLMEAEYKKLNEIYSDVDNIEKELKKHKKN 1634
|
|
| SH3_Eve1_5 |
cd11818 |
Fifth Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 ... |
1930-1981 |
7.68e-06 |
|
Fifth Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 domain-containing protein 19 (SH3D19) or EEN-binding protein (EBP), exists in multiple alternatively spliced isoforms. The longest isoform contains five SH3 domain in the C-terminal region and seven proline-rich motifs in the N-terminal region. It is abundantly expressed in skeletal muscle and heart, and may be involved in regulating the activity of ADAMs (A disintegrin and metalloproteases). Eve-1 interacts with EEN, an endophilin involved in endocytosis and may be the target of the MLL-EEN fusion protein that is implicated in leukemogenesis. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212752 [Multi-domain] Cd Length: 50 Bit Score: 45.17 E-value: 7.68e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSLHGQQGIVPAN 1981
Cdd:cd11818 2 ARALYDFTGENEDELSFKAGDIITELESID----EEWMSGELRGKSGIFPKN 49
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
846-1154 |
7.80e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 846 ETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMN 925
Cdd:COG4372 56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 926 ERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLE-----LTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKA 1000
Cdd:COG4372 136 AQIAELQSEIAEREEELKELEEQLESLQEELAALEqelqaLSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1001 LQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEE 1080
Cdd:COG4372 216 LAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALEL 295
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1081 KLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEE 1154
Cdd:COG4372 296 KLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| SH3_srGAP |
cd11809 |
Src homology 3 domain of Slit-Robo GTPase Activating Proteins; Slit-Robo GTPase Activating ... |
1929-1979 |
8.44e-06 |
|
Src homology 3 domain of Slit-Robo GTPase Activating Proteins; Slit-Robo GTPase Activating Proteins (srGAPs) are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. Vertebrates contain three isoforms of srGAPs (srGAP1-3), all of which are expressed during embryonic and early development in the nervous system but with different localization and timing. A fourth member has also been reported (srGAP4, also called ARHGAP4). srGAPs contain an N-terminal F-BAR domain, a Rho GAP domain, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212743 [Multi-domain] Cd Length: 53 Bit Score: 45.08 E-value: 8.44e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 431907173 1929 LARALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSLHGQQGIVP 1979
Cdd:cd11809 1 EATAQFDYTGRSERELSFKKGDSLTLYRQVS----DDWWRGQLNGQDGLVP 47
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
926-1232 |
9.09e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.91 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 926 ERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL----DEIIAKLTKEKKAL 1001
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELrekrDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1002 QEAHQQALDdlqaeedkvntltkskvkLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDK------ 1075
Cdd:COG1340 81 DELNEKLNE------------------LREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKelveki 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1076 LQLEEKLKKKEfDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEA 1155
Cdd:COG1340 143 KELEKELEKAK-KALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEA 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1156 ggatSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAElgeqidnlQRVKQKLEKEKSEFKLELDD 1232
Cdd:COG1340 222 ----QEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE--------EKAEEIFEKLKKGEKLTTEE 286
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1261-1943 |
9.53e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 51.23 E-value: 9.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1261 YRTKLEEAQRSLNDFTTQQaklqteNGELARQLEEKEALISQ--LTRGKLSYTQQTEDLKRQLEEEGKAKNALAHALQsa 1338
Cdd:COG5022 760 LRRRYLQALKRIKKIQVIQ------HGFRLRRLVDYELKWRLfiKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKK-- 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1339 rhdcdlLREQYEEETEAKAE--LQRVLSKANSEVAQWRTKYETDAIQRTEELEEAK-----LQDAEEAVEAVNAKCSSLE 1411
Cdd:COG5022 832 ------LRETEEVEFSLKAEvlIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAErqlqeLKIDVKSISSLKLVNLELE 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1412 KTKHRLQNEIE-DLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKeaRSLSTELFKLKNAYEESLEH 1490
Cdd:COG5022 906 SEIIELKKSLSsDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVE--SKLKETSEEYEDLLKKSTIL 983
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1491 LETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVrKQLEAEKLELQSAleEAEASLEHEEGKILR--AQLEFNQIKAei 1568
Cdd:COG5022 984 VREGNKANSELKNFKKELAELSKQYGALQESTKQL-KELPVEVAELQSA--SKIISSESTELSILKplQKLKGLLLLE-- 1058
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1569 ERKLAEKDEEMEQAKRNHLRvvDSLQTSLDAETRSRNEALRVKKKMEGDLNEMeiQLSQANRTASEAQKHLKIAQahlkd 1648
Cdd:COG5022 1059 NNQLQARYKALKLRRENSLL--DDKQLYQLESTENLLKTINVKDLEVTNRNLV--KPANVLQFIVAQMIKLNLLQ----- 1129
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1649 tqlQMDDAVRANDDlkeNIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERvqllhsQNTSLINQKKKMES 1728
Cdd:COG5022 1130 ---EISKFLSQLVN---TLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLY------QSALYDEKSKLSSS 1197
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1729 DLTQLQSEVEEAVQECRNAEEKA---KKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIaLKGGK 1805
Cdd:COG5022 1198 EVNDLKNELIALFSKIFSGWPRGdklKKLISEGWVPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNL-LSSYK 1276
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1806 KQLQKLEARVRELENELEAEQ------KRNAESVKGMRKSERRIKEL-----TYQTEEDKKNLLRLQDLVDKLQLKVKAY 1874
Cdd:COG5022 1277 LEEEVLPATINSLLQYINVGLfnalrtKASSLRWKSATEVNYNSEELddwcrEFEISDVDEELEELIQAVKVLQLLKDDL 1356
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 431907173 1875 KRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSrdIGAKAQLARALYDNTAESPQE 1943
Cdd:COG5022 1357 NKLDELLDACYSLNPAEIQNLKSRYDPADKENNLPKEILKKIEALL--IKQELQLSLEGKDETEVHLSE 1423
|
|
| SH3_Eps8 |
cd11764 |
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar ... |
1929-1981 |
9.73e-06 |
|
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar proteins; This group is composed of Eps8 and Eps8-like proteins including Eps8-like 1-3, among others. These proteins contain N-terminal Phosphotyrosine-binding (PTB), central SH3, and C-terminal effector domains. Eps8 binds either Abi1 (also called E3b1) or Rab5 GTPase activating protein RN-tre through its SH3 domain. With Abi1 and Sos1, it becomes part of a trimeric complex that is required to activate Rac. Together with RN-tre, it inhibits the internalization of EGFR. The SH3 domains of Eps8 and similar proteins recognize peptides containing a PxxDY motif, instead of the classical PxxP motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212698 [Multi-domain] Cd Length: 54 Bit Score: 44.94 E-value: 9.73e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1929 LARALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSLHGQQGIVPAN 1981
Cdd:cd11764 1 YVRVLYDFTARNSKELSVLKGEYLEVLDDSR----QWWKVRNSRGQVGYVPHN 49
|
|
| SH3_MLK1-3 |
cd12059 |
Src Homology 3 domain of Mixed Lineage Kinases 1, 2, and 3; MLKs 1, 2, and 3 are Serine ... |
1932-1983 |
9.99e-06 |
|
Src Homology 3 domain of Mixed Lineage Kinases 1, 2, and 3; MLKs 1, 2, and 3 are Serine/Threonine Kinases (STKs), catalyzing the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. Little is known about the specific function of MLK1, also called MAP3K9. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. MLK2, also called MAP3K10, is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK3, also called MAP3K11, is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. It also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and thus, impacts inflammation and immunity. MLKs contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212992 [Multi-domain] Cd Length: 58 Bit Score: 45.14 E-value: 9.99e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQREGA-GGLDGWCLCSLHGQQGIVPANRV 1983
Cdd:cd12059 4 AVFDYEASAEDELTLRRGDRVEVLSKDSAvSGDEGWWTGKINDRVGIFPSNYV 56
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
889-1095 |
1.01e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.78 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 889 LQLQVQAEQDNLNDAEER--------CDQLIKN-KIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDL 959
Cdd:PHA02562 160 LDISVLSEMDKLNKDKIRelnqqiqtLDMKIDHiQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 960 ELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAH-----QQALDD----LQAEEDKVNTLTKSKVKLE 1030
Cdd:PHA02562 240 TDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGvcptcTQQISEgpdrITKIKDKLKELQHSLEKLD 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 431907173 1031 QQVDDLEGSL----EQEKKVRmDLERAKRKLEGDLKLTQESIMDLEN--DKLQLEEKLKKKEFDISQQNSK 1095
Cdd:PHA02562 320 TAIDELEEIMdefnEQSKKLL-ELKNKISTNKQSLITLVDKAKKVKAaiEELQAEFVDNAEELAKLQDELD 389
|
|
| SH3_Fus1p |
cd11854 |
Src homology 3 domain of yeast cell fusion protein Fus1p; Fus1p is required at the cell ... |
1929-1980 |
1.30e-05 |
|
Src homology 3 domain of yeast cell fusion protein Fus1p; Fus1p is required at the cell surface for cell fusion during the mating response in yeast. It requires Bch1p and Bud7p, which are Chs5p-Arf1p binding proteins, for localization to the plasma membrane. It acts as a scaffold protein to assemble a cell surface complex which is involved in septum degradation and inhibition of the NOG pathway to promote cell fusion. The SH3 domain of Fus1p interacts with Bin1p, a formin that controls the assembly of actin cables in response to Cdc42 signaling. It has been shown to bind the motif, R(S/T)(S/T)SL, instead of PxxP motifs. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212788 [Multi-domain] Cd Length: 56 Bit Score: 44.62 E-value: 1.30e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1929 LARALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLC----SLHGQQGIVPA 1980
Cdd:cd11854 1 LMTVISTFEPSLDDELLIKVGETVRVLAEYD----DGWCLVeradGLNGDRGMVPG 52
|
|
| SH3_SH3YL1_like |
cd11841 |
Src homology 3 domain of SH3 domain containing Ysc84-like 1 (SH3YL1) protein; SH3YL1 localizes ... |
1930-1984 |
1.34e-05 |
|
Src homology 3 domain of SH3 domain containing Ysc84-like 1 (SH3YL1) protein; SH3YL1 localizes to the plasma membrane and is required for dorsal ruffle formation. It binds phosphoinositides (PIs) with high affinity through its N-terminal SYLF domain (also called DUF500). In addition, SH3YL1 contains a C-terminal SH3 domain which has been reported to bind to N-WASP, dynamin 2, and SHIP2 (a PI 5-phosphatase). SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212775 Cd Length: 54 Bit Score: 44.31 E-value: 1.34e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGAGglDGWCLCSLHGQQGIVPANRVK 1984
Cdd:cd11841 2 VTALYSFEGQQPCDLSFQAGDRITVLTRTDSQ--FDWWEGRLRGRVGIFPANYVS 54
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1128-1918 |
1.35e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 50.98 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1128 RTARAKVEKLRSdlsrELEEISERLEEAGgatsvqiemnKKREAEFQKMRRDLEEATLQHEATAAALRkkhADSVAElGE 1207
Cdd:NF041483 400 REAEAEADRLRG----EAADQAEQLKGAA----------KDDTKEYRAKTVELQEEARRLRGEAEQLR---AEAVAE-GE 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1208 QIDNLQR---VKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKV-------SRTLEDQANEY--RTKlEEAQRSLNDF 1275
Cdd:NF041483 462 RIRGEARreaVQQIEEAARTAEELLTKAKADADELRSTATAESERVrteaierATTLRRQAEETleRTR-AEAERLRAEA 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1276 TTQQAKLQTENGELARQL-EEKEALISQltrgklSYTQQTEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETE 1354
Cdd:NF041483 541 EEQAEEVRAAAERAARELrEETERAIAA------RQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETE 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1355 ----AKAELQRVL-SKANSEVAQWRTKYETDAIQRTEELEEAKLQ-DAEEAVEAvnakcsslektkHRLQNEIEDlMVDV 1428
Cdd:NF041483 615 rlrtEAAERIRTLqAQAEQEAERLRTEAAADASAARAEGENVAVRlRSEAAAEA------------ERLKSEAQE-SADR 681
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1429 ERSNAAAAA----------LDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELF-----KLKNAYEESLEHLET 1493
Cdd:NF041483 682 VRAEAAAAAervgteaaeaLAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLasarkRVEEAQAEAQRLVEE 761
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1494 FKRENKNL-----------QEEISDLTEQLGE---GGKNV--HELEKVRKQLEAEKLELQS-ALEEAEASLEHEEGKILR 1556
Cdd:NF041483 762 ADRRATELvsaaeqtaqqvRDSVAGLQEQAEEeiaGLRSAaeHAAERTRTEAQEEADRVRSdAYAERERASEDANRLRRE 841
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1557 AQLEFNQIKAEIERKLAEKDEE--------MEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDlnemeiQLSQA 1628
Cdd:NF041483 842 AQEETEAAKALAERTVSEAIAEaerlrsdaSEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSD------AAAQA 915
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1629 NRTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLK--ENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETS 1706
Cdd:NF041483 916 DRLIGEATSEAERLTAEARAEAERLRDEARAEAERVraDAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTEA 995
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1707 ERVQLLHSQNTSLINQKKKMESDLTqLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAhLERMKKNMEQTI 1786
Cdd:NF041483 996 ERVKAEAAAEAERLRTEAREEADRT-LDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEA-LRTTTEAEAQAD 1073
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1787 KDLQHRLDEAEQIALKGGKKQLQKLEaRVRELENELEAEQKRNAESVKGmRKSERR------IKELTYQTEEDKKNLLRL 1860
Cdd:NF041483 1074 TMVGAARKEAERIVAEATVEGNSLVE-KARTDADELLVGARRDATAIRE-RAEELRdritgeIEELHERARRESAEQMKS 1151
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 431907173 1861 Q-DLVDKLqlkVKAYKRQAEEAEEQ-------ANTNLSKFR-----KVQHELDEAEERADIAESQVNKLRA 1918
Cdd:NF041483 1152 AgERCDAL---VKAAEEQLAEAEAKakelvsdANSEASKVRiaavkKAEGLLKEAEQKKAELVREAEKIKA 1219
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
842-1153 |
1.39e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 842 LKSAETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLqlqvQAEQDNLNDAEERCDQLIKNKIQLEAKV 921
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSEL----EQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 922 KEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKE---- 997
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAeaeq 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 998 --KKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDK 1075
Cdd:COG4372 184 alDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1076 LQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLE 1153
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1503-1926 |
1.45e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 50.34 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1503 EEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELqsALEEAEASLEHEEGKILRAQLEFNQIKAEI-ERKLAEKDEEMEQ 1581
Cdd:COG5185 118 ILISLLYLYKSEIVALKDELIKVEKLDEIADIEA--SYGEVETGIIKDIFGKLTQELNQNLKKLEIfGLTLGLLKGISEL 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1582 AKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDAVRAND 1661
Cdd:COG5185 196 KKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1662 DLKEniaiVERRNNLLQAELEELRAVVEQTERSRKLAeqelIETSERVQLLHSQ--NTSLINQKKKMESDLTQLQSEVEE 1739
Cdd:COG5185 276 SSKR----LNENANNLIKQFENTKEKIAEYTKSIDIK----KATESLEEQLAAAeaEQELEESKRETETGIQNLTAEIEQ 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1740 AVQECRNAEEKAKKAItdaammaEELKKEQDTSaHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELE 1819
Cdd:COG5185 348 GQESLTENLEAIKEEI-------ENIVGEVELS-KSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAD 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1820 NELEaeqkrnaesvkgmrKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVkaykrQAEEAEEQANTNLSKFRKVQHEL 1899
Cdd:COG5185 420 RQIE--------------ELQRQIEQATSSNEEVSKLLNELISELNKVMREA-----DEESQSRLEEAYDEINRSVRSKK 480
|
410 420
....*....|....*....|....*..
gi 431907173 1900 DEAEERADIAESQVNKLRAKSRDIGAK 1926
Cdd:COG5185 481 EDLNEELTQIESRVSTLKATLEKLRAK 507
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1523-1960 |
1.45e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1523 EKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAeierklAEKDEEME-QAKRNHLRVVdslqtsldaet 1601
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNE------AESDLEQDyQAASDHLNLV----------- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1602 rsrNEALRVKKKME---GDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMddavranDDLKENIAIVERRNNLLQ 1678
Cdd:PRK04863 341 ---QTALRQQEKIEryqADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEV-------DELKSQLADYQQALDVQQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1679 aeleelravveqterSRKLAEQELIETSERV-QLLHSQNTSLinqkKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITD 1757
Cdd:PRK04863 411 ---------------TRAIQYQQAVQALERAkQLCGLPDLTA----DNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAA 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1758 AAMMAEELKKEQDTSAHLERmkKNMEQTIKDLQHRLDEAEQIAlkggkKQLQKLEARVRELENELeaEQKRNAESvkgMR 1837
Cdd:PRK04863 472 HSQFEQAYQLVRKIAGEVSR--SEAWDVARELLRRLREQRHLA-----EQLQQLRMRLSELEQRL--RQQQRAER---LL 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1838 KSERRIKELTYQTEEDkknllrLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADI---AESQVN 1914
Cdd:PRK04863 540 AEFCKRLGKNLDDEDE------LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALA 613
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1915 KLRAKSRDIGAKAQLARALYDNTAESPQELSFRR-----------GDVLRVLQREGA 1960
Cdd:PRK04863 614 RLREQSGEEFEDSQDVTEYMQQLLERERELTVERdelaarkqaldEEIERLSQPGGS 670
|
|
| SH3_CD2AP-like_3 |
cd11875 |
Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This ... |
1930-1985 |
1.46e-05 |
|
Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This subfamily is composed of the third SH3 domain (SH3C) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3C of both proteins have been shown to bind to ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212808 [Multi-domain] Cd Length: 55 Bit Score: 44.26 E-value: 1.46e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREgaGGLDGWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd11875 2 ARVLFDYEAENEDELTLREGDIVTILSKD--CEDKGWWKGELNGKRGVFPDNFVEP 55
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1669-1907 |
1.47e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.60 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1669 IVERRNNLLQAELEELRAVVEQTERSRKLAEQELIEtserVQLLHSQNTSLinqKKKMESDLTQLQSEVEEAVQEcrnAE 1748
Cdd:PRK00409 503 IIEEAKKLIGEDKEKLNELIASLEELERELEQKAEE----AEALLKEAEKL---KEELEEKKEKLQEEEDKLLEE---AE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1749 EKAKKAItdaammaEELKKEQDtsahlermkknmeQTIKDLQHRLD-EAEQIALKGGKKQLQKLEARVRELENELEAEQK 1827
Cdd:PRK00409 573 KEAQQAI-------KEAKKEAD-------------EIIKELRQLQKgGYASVKAHELIEARKRLNKANEKKEKKKKKQKE 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1828 RNAESVKGMrkserRIKELTYQT-----EEDKKNLLRLQDLVDKLQLK---VKAYKRQAEEAEEQANTNLSKFRKVQHEL 1899
Cdd:PRK00409 633 KQEELKVGD-----EVKYLSLGQkgevlSIPDDKEAIVQAGIMKMKVPlsdLEKIQKPKKKKKKKPKTVKPKPRTVSLEL 707
|
250
....*....|....*
gi 431907173 1900 D-------EAEERAD 1907
Cdd:PRK00409 708 DlrgmryeEALERLD 722
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
849-1045 |
1.51e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 48.87 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 849 KEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEM---- 924
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESergr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 925 ----NERLEDEEEMN---AELTAKKRKLED---ECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKL 994
Cdd:pfam00261 81 kvleNRALKDEEKMEileAQLKEAKEIAEEadrKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 995 -TKEKKALQ------EAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKK 1045
Cdd:pfam00261 161 eASEEKASEredkyeEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKE 218
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
845-1016 |
1.55e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 845 AETEKEMANMKEEfgrLKETLEKSEARRKELEEKMVSLLQEKNDLQ-LQVQAEQDNLNDAEERCDQLikNKIqleakVKE 923
Cdd:COG3883 61 EALQAEIDKLQAE---IAEAEAEIEERREELGERARALYRSGGSVSyLDVLLGSESFSDFLDRLSAL--SKI-----ADA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 924 MNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQE 1003
Cdd:COG3883 131 DADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
170
....*....|...
gi 431907173 1004 AHQQALDDLQAEE 1016
Cdd:COG3883 211 AAAAAAAAAAAAA 223
|
|
| SH3_Sorbs_2 |
cd11782 |
Second Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) proteins and similar ... |
1930-1984 |
1.61e-05 |
|
Second Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) proteins and similar domains; This family, also called the vinexin family, is composed predominantly of adaptor proteins containing one sorbin homology (SoHo) and three SH3 domains. Members include the second SH3 domains of Sorbs1 (or ponsin), Sorbs2 (or ArgBP2), Vinexin (or Sorbs3), and similar domains. They are involved in the regulation of cytoskeletal organization, cell adhesion, and growth factor signaling. Members of this family bind multiple partners including signaling molecules like c-Abl, c-Arg, Sos, and c-Cbl, as well as cytoskeletal molecules such as vinculin and afadin. They may have overlapping functions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212716 [Multi-domain] Cd Length: 53 Bit Score: 44.26 E-value: 1.61e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSLHGQQGIVPANRVK 1984
Cdd:cd11782 2 ARAKYNFNADTGVELSFRKGDVITLTRRVD----ENWYEGRIGGRQGIFPVSYVQ 52
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1677-1933 |
1.66e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1677 LQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAIT 1756
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1757 DAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGM 1836
Cdd:COG4372 123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEEL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1837 RKSERRIKELtyQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKL 1916
Cdd:COG4372 203 AEAEKLIESL--PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250
....*....|....*..
gi 431907173 1917 RAKSRDIGAKAQLARAL 1933
Cdd:COG4372 281 AALELEALEEAALELKL 297
|
|
| SH3_PACSIN_like |
cd11999 |
Src homology 3 domain of an unknown subfamily of proteins with similarity to Protein kinase C ... |
1928-1983 |
1.81e-05 |
|
Src homology 3 domain of an unknown subfamily of proteins with similarity to Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins; PACSINs, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. They bind both dynamin and Wiskott-Aldrich syndrome protein (WASP), and may provide direct links between the actin cytoskeletal machinery through WASP and dynamin-dependent endocytosis. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212932 [Multi-domain] Cd Length: 56 Bit Score: 44.16 E-value: 1.81e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1928 QLARALYDNTAESPQELSFRRGDVLRVLQREGAgglDGWCL-CSLHGQQGIVPANRV 1983
Cdd:cd11999 2 VRVRAVYDYTGQEPDELSFKAGEELLKVEDEDE---QGWCKgVTDGGAVGLYPANYV 55
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1988-2229 |
2.08e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 50.17 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1988 AGPTPKPSLSQVPPAEPGSPYPAPEHSnedqevyVVPPPARPCLTSESPAgpclpspdpiykvPRGSGTQPATPGDAlev 2067
Cdd:PHA03307 59 AAACDRFEPPTGPPPGPGTEAPANESR-------STPTWSLSTLAPASPA-------------REGSPTPPGPSSPD--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2068 ydvPPAALRVSASGPYDTPASFSHLLARVAPQPPGEDEAPYDVPLAPKPPSElepdleweGGREPGPPLYAAPSnlkras 2147
Cdd:PHA03307 116 ---PPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVAS--------DAASSRQAALPLSS------ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2148 allnlyeaPEElladgeeggsdegiydvpllgPETPPSPEPlgalASNDPDTLALLLARSPPPSHRPRlpSAESLSRRPL 2227
Cdd:PHA03307 179 --------PEE---------------------TARAPSSPP----AEPPPSTPPAAASPRPPRRSSPI--SASASSPAPA 223
|
..
gi 431907173 2228 PA 2229
Cdd:PHA03307 224 PG 225
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
936-1160 |
2.08e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 936 AELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAE 1015
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1016 EDKVNTLT-----KSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDIS 1090
Cdd:COG3883 99 GGSVSYLDvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1091 QQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATS 1160
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| SH3_ARHGEF37_C2 |
cd11941 |
Second C-terminal Src homology 3 domain of Rho guanine nucleotide exchange factor 37; ARHGEF37 ... |
1932-1981 |
2.24e-05 |
|
Second C-terminal Src homology 3 domain of Rho guanine nucleotide exchange factor 37; ARHGEF37 contains a RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. Its specific function is unknown. Its domain architecture is similar to the C-terminal half of DNMBP or Tuba, a cdc42-specific GEF that provides a functional link between dynamin, Rho GTPase signaling, and actin dynamics, and plays an important role in regulating cell junction configuration. GEFs activate small GTPases by exchanging bound GDP for free GTP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212874 Cd Length: 57 Bit Score: 44.13 E-value: 2.24e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQREGAGGLDGWCLCSLHGQQGIVPAN 1981
Cdd:cd11941 4 AAYPFTARSKHEVSLQAGQPVTVLEPHDKKGSPEWSLVEVNGQRGYVPSS 53
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1433-1673 |
2.24e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1433 AAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQl 1512
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1513 geggknvheLEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQI--KAEIERKLAEKDEEMEQAKRNHLRVV 1590
Cdd:COG4942 92 ---------IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAvrRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1591 DSLQTSLDAEtrsrnealrvKKKMEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKENIAIV 1670
Cdd:COG4942 163 AALRAELEAE----------RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
...
gi 431907173 1671 ERR 1673
Cdd:COG4942 233 EAE 235
|
|
| SH3_Nck_2 |
cd11766 |
Second Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin ... |
1930-1983 |
2.31e-05 |
|
Second Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4), which show partly overlapping functions but also bind distinct targets. Their SH3 domains are involved in recruiting downstream effector molecules, such as the N-WASP/Arp2/3 complex, which when activated induces actin polymerization that results in the production of pedestals, or protrusions of the plasma membrane. The second SH3 domain of Nck appears to prefer ligands containing the APxxPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212700 [Multi-domain] Cd Length: 53 Bit Score: 43.79 E-value: 2.31e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSLHGQQGIVPANRV 1983
Cdd:cd11766 2 AVVKFNYEAQREDELSLRKGDRVLVLEKSS----DGWWRGECNGQVGWFPSNYV 51
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1228-1405 |
2.37e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1228 LELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLTRGK 1307
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1308 lsytqQTEDLKRQLEEEGKAKNALAHALQSarhdcdlLREQYEEETEAKAELQRVLSKANSEVAQWRTKYEtDAIQRTEE 1387
Cdd:COG1579 90 -----EYEALQKEIESLKRRISDLEDEILE-------LMERIEELEEELAELEAELAELEAELEEKKAELD-EELAELEA 156
|
170
....*....|....*...
gi 431907173 1388 LEEAKLQDAEEAVEAVNA 1405
Cdd:COG1579 157 ELEELEAEREELAAKIPP 174
|
|
| SH3_MyoIe_If_like |
cd11827 |
Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If ... |
1930-1983 |
2.49e-05 |
|
Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If (MyoIf) are nonmuscle, unconventional, long tailed, class I myosins containing an N-terminal motor domain and a myosin tail with TH1, TH2, and SH3 domains. MyoIe interacts with the endocytic proteins, dynamin and synaptojanin-1, through its SH3 domain; it may play a role in clathrin-dependent endocytosis. In the kidney, MyoIe is critical for podocyte function and normal glomerular filtration. Mutations in MyoIe is associated with focal segmental glomerulosclerosis, a disease characterized by massive proteinuria and progression to end-stage kidney disease. MyoIf is predominantly expressed in the immune system; it plays a role in immune cell motility and innate immunity. Mutations in MyoIf may be associated with the loss of hearing. The MyoIf gene has also been found to be fused to the MLL (Mixed lineage leukemia) gene in infant acute myeloid leukemias (AML). SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212761 [Multi-domain] Cd Length: 53 Bit Score: 43.56 E-value: 2.49e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGAggldGWCLCSLHGQQGIVPANRV 1983
Cdd:cd11827 2 CKALYAYDAQDTDELSFNEGDIIEILKEDPS----GWWTGRLRGKEGLFPGNYV 51
|
|
| SH3_VAV1_2 |
cd11976 |
C-terminal (or second) Src homology 3 domain of VAV1 protein; VAV1 is expressed predominantly ... |
1930-1984 |
2.61e-05 |
|
C-terminal (or second) Src homology 3 domain of VAV1 protein; VAV1 is expressed predominantly in the hematopoietic system and it plays an important role in the development and activation of B and T cells. It is activated by tyrosine phosphorylation to function as a guanine nucleotide exchange factor (GEF) for Rho GTPases following cell surface receptor activation, triggering various effects such as cytoskeletal reorganization, transcription regulation, cell cycle progression, and calcium mobilization. It also serves as a scaffold protein and has been shown to interact with Ku70, Socs1, Janus kinase 2, SIAH2, S100B, Abl gene, ZAP-70, SLP76, and Syk, among others. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The C-terminal SH3 domain of Vav1 interacts with a wide variety of proteins including cytoskeletal regulators (zyxin), RNA-binding proteins (Sam68), transcriptional regulators, viral proteins, and dynamin 2. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212909 [Multi-domain] Cd Length: 54 Bit Score: 43.78 E-value: 2.61e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGAgglDGWCLCSLHGQQGIVPANRVK 1984
Cdd:cd11976 2 AKARYDFCARDRSELSLKEGDIIKILNKKGQ---QGWWRGEIYGRVGWFPANYVE 53
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1006-1853 |
2.74e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.95 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1006 QQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAkrklEGDLKLTQESimdlendkLQLEEKLKKK 1085
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAA----SDHLNLVQTA--------LRQQEKIERY 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1086 EFDISQQNSKIEDEQALALQLQKKLKENQARieeleeeleaERTARAKVEKLRSDLSReleeiserLEEAggatsvqIEM 1165
Cdd:COG3096 353 QEDLEELTERLEEQEEVVEEAAEQLAEAEAR----------LEAAEEEVDSLKSQLAD--------YQQA-------LDV 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1166 NKKREAEFQKMRRDLEEATLQHEA---TAAALRKKHADSVAELGEQIDNLQRVKQKL---EKEKSEFK--LEL----DDV 1233
Cdd:COG3096 408 QQTRAIQYQQAVQALEKARALCGLpdlTPENAEDYLAAFRAKEQQATEEVLELEQKLsvaDAARRQFEkaYELvckiAGE 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1234 TSNMEQIIKAKANLEKVS--RTLEDQANEYRTKL----------EEAQRSLNDFTTQQAKLQTENGELARQLEEKEALIS 1301
Cdd:COG3096 488 VERSQAWQTARELLRRYRsqQALAQRLQQLRAQLaeleqrlrqqQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLE 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1302 QLT------RGKLSYTQQTEDLKRQLEEEGKAKNALAHALQSARHDcdlLREQYEEETEAKAELQ----------RVLSK 1365
Cdd:COG3096 568 ELEeqaaeaVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALER---LREQSGEALADSQEVTaamqqllereREATV 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1366 ANSEVAQWRTKYEtDAIQR------------------------TEELEEAKLQDAEE-------AVEA-VNAKCSSLEKT 1413
Cdd:COG3096 645 ERDELAARKQALE-SQIERlsqpggaedprllalaerlggvllSEIYDDVTLEDAPYfsalygpARHAiVVPDLSAVKEQ 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1414 KHRLQNEIEDLMVdVERS-NAAAAALDKKQRNFDKILAEWKQKyeesqselesSQKEARSLSTELFKLKnAYEESLEhle 1492
Cdd:COG3096 724 LAGLEDCPEDLYL-IEGDpDSFDDSVFDAEELEDAVVVKLSDR----------QWRYSRFPEVPLFGRA-AREKRLE--- 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1493 tfkrenkNLQEEISDLTEQLGEGGKNVHELEKVRKQL----------------EAEKLELQSALEEAEASLEHEEGKILR 1556
Cdd:COG3096 789 -------ELRAERDELAEQYAKASFDVQKLQRLHQAFsqfvgghlavafapdpEAELAALRQRRSELERELAQHRAQEQQ 861
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1557 AQLEFNQIKAEIE--RKLAE-----KDEEMEQakrnhlRVVDslqtsLDAETRSRNEALRVKKKMEGDLNEMEIQLSqAN 1629
Cdd:COG3096 862 LRQQLDQLKEQLQllNKLLPqanllADETLAD------RLEE-----LREELDAAQEAQAFIQQHGKALAQLEPLVA-VL 929
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1630 RTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLkeniaiVERRNNLLQAE----LEELRAVVEQTERSRKLAEQELIET 1705
Cdd:COG3096 930 QSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEV------VQRRPHFSYEDavglLGENSDLNEKLRARLEQAEEARREA 1003
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1706 SERVQLLHSQNTSLiNQKkkmesdLTQLQSEVEEAVQECRNAEEKAK----KAITDAAMMAEELKKEQDTSAHLERMKKN 1781
Cdd:COG3096 1004 REQLRQAQAQYSQY-NQV------LASLKSSRDAKQQTLQELEQELEelgvQADAEAEERARIRRDELHEELSQNRSRRS 1076
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1782 meQTIKDLQHRldEAEQialkggkKQLQKleaRVRELENELEAEQKRNAESVKG----MRKS-----ERRI--KELTYQT 1850
Cdd:COG3096 1077 --QLEKQLTRC--EAEM-------DSLQK---RLRKAERDYKQEREQVVQAKAGwcavLRLArdndvERRLhrRELAYLS 1142
|
...
gi 431907173 1851 EED 1853
Cdd:COG3096 1143 ADE 1145
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1390-1584 |
2.78e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1390 EAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKE 1469
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1470 ARSLSTELFKLKNA-----------YEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQS 1538
Cdd:COG4942 106 LAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 431907173 1539 ALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKR 1584
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| SH3_CD2AP-like_1 |
cd11873 |
First Src Homology 3 domain (SH3A) of CD2-associated protein and similar proteins; This ... |
1930-1984 |
2.81e-05 |
|
First Src Homology 3 domain (SH3A) of CD2-associated protein and similar proteins; This subfamily is composed of the first SH3 domain (SH3A) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3A of both proteins bind to an atypical PXXXPR motif at the C-terminus of Cbl and the cytoplasmic domain of the cell adhesion protein CD2. CIN85 SH3A binds to internal proline-rich motifs within the proline-rich region; this intramolecular interaction serves as a regulatory mechanism to keep CIN85 in a closed conformation, preventing the recruitment of other proteins. CIN85 SH3A has also been shown to bind ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212806 [Multi-domain] Cd Length: 53 Bit Score: 43.41 E-value: 2.81e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLR-VLQREGaggldGWCLCSLHGQQGIVPANRVK 1984
Cdd:cd11873 2 VIVEFDYDAEEPDELTLKVGDIITnVKKMEE-----GWWEGTLNGKRGMFPDNFVK 52
|
|
| SH3_SKAP1 |
cd12044 |
Src Homology 3 domain of Src Kinase-Associated Phosphoprotein 1; SKAP1, also called SKAP55 ... |
1931-1979 |
2.84e-05 |
|
Src Homology 3 domain of Src Kinase-Associated Phosphoprotein 1; SKAP1, also called SKAP55 (Src kinase-associated protein of 55kDa), is an immune cell-specific adaptor protein that plays an important role in T-cell adhesion, migration, and integrin clustering. It is expressed exclusively in T-lymphocytes, mast cells, and macrophages. Binding partners include ADAP (adhesion and degranulation-promoting adaptor protein), Fyn, Riam, RapL, and RasGRP. It contains a pleckstrin homology (PH) domain, a C-terminal SH3 domain, and several tyrosine phosphorylation sites. The SH3 domain of SKAP1 is necessary for its ability to regulate T-cell conjugation with antigen-presenting cells and the formation of LFA-1 clusters. SKAP1 binds primarily to a proline-rich region of ADAP through its SH3 domain; its degradation is regulated by ADAP. A secondary interaction occurs via the ADAP SH3 domain and the RKxxYxxY motif in SKAP1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212977 Cd Length: 53 Bit Score: 43.69 E-value: 2.84e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREgaGGLDGWCLCSLHGQQGIVP 1979
Cdd:cd12044 3 QGLWDCFGDNPDELSFQRGDLIYILSKE--YNMYGWWVGELNGIVGIVP 49
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
983-1154 |
2.95e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 983 EMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQekkVRMDLERAKRKLEG--- 1059
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEE---VEARIKKYEEQLGNvrn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1060 --DLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIeeleeeleaeRTARAKVEKL 1137
Cdd:COG1579 88 nkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL----------DEELAELEAE 157
|
170
....*....|....*..
gi 431907173 1138 RSDLSRELEEISERLEE 1154
Cdd:COG1579 158 LEELEAEREELAAKIPP 174
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1254-1880 |
2.98e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.80 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1254 LEDQANEYRTKLEEAQRSLNDFTTQQAKLQTenGELARQLEEKEALISQLTRGKLSYTQQTEDLKRQLEEEGKAKNALAH 1333
Cdd:PRK10246 255 LQQEASRRQQALQQALAAEEKAQPQLAALSL--AQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRH 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1334 alqSARHDCDLLREQYEEETEAKAELQRvLSKANSEVAQWRTKYetdaiqrteeleeAKLQDAEEAVEAVNAKCSSLEKT 1413
Cdd:PRK10246 333 ---HAAKQSAELQAQQQSLNTWLAEHDR-FRQWNNELAGWRAQF-------------SQQTSDREQLRQWQQQLTHAEQK 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1414 KHRLQNEIEDLMVDverSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKnayeeslEHLET 1493
Cdd:PRK10246 396 LNALPAITLTLTAD---EVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRN-------AALNE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1494 FKRENKNLQEEISDLteqlgeggKNVHELEKVRKQLEAEKLELQS-------------------------------ALEE 1542
Cdd:PRK10246 466 MRQRYKEKTQQLADV--------KTICEQEARIKDLEAQRAQLQAgqpcplcgstshpaveayqalepgvnqsrldALEK 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1543 AEASLEhEEGKILRAQLE--FNQIK---------AEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNE--ALR 1609
Cdd:PRK10246 538 EVKKLG-EEGAALRGQLDalTKQLQrdeseaqslRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQlrLLS 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1610 VKKKMEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKENIAIVERRNN---LLQAELEELRA 1686
Cdd:PRK10246 617 QRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQSWQQRQNeltALQNRIQQLTP 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1687 VVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEK---AKKAITDAAMMAE 1763
Cdd:PRK10246 697 LLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQAsvfDDQQAFLAALLDE 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1764 ElkkeqdTSAHLERMKKNMEQTIKDLQHRLDEAEQialkggkKQLQKLEARVRELENELEAE--QKRNAESVKGMRKSER 1841
Cdd:PRK10246 777 E------TLTQLEQLKQNLENQRQQAQTLVTQTAQ-------ALAQHQQHRPDGLDLTVTVEqiQQELAQLAQQLRENTT 843
|
650 660 670
....*....|....*....|....*....|....*....
gi 431907173 1842 RIKELTYQTEEDKKNLLRLQDLVdklqLKVKAYKRQAEE 1880
Cdd:PRK10246 844 RQGEIRQQLKQDADNRQQQQALM----QQIAQATQQVED 878
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1221-1584 |
3.08e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.57 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1221 KEKSEFKLELD-DVTSNMEQIIKAKANLEKVSRTLEDQaNEYRTKLEEAQRSLNDF-------TTQQAKL---QTENGEL 1289
Cdd:COG3096 281 RELSERALELRrELFGARRQLAEEQYRLVEMARELEEL-SARESDLEQDYQAASDHlnlvqtaLRQQEKIeryQEDLEEL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1290 ARQLEEKEALISQLTRGKlsytQQTEDLKRQLEEEGK-AKNALAHaLQSArhdCDLLRE---QYEEETEAKAELQRVLSK 1365
Cdd:COG3096 360 TERLEEQEEVVEEAAEQL----AEAEARLEAAEEEVDsLKSQLAD-YQQA---LDVQQTraiQYQQAVQALEKARALCGL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1366 AN---SEVAQWRTKYETDAIQRTEELEEA--KLQDAEEAveavnakcssleKTKHRLQNEIEDLMVD-VERSNA--AAAA 1437
Cdd:COG3096 432 PDltpENAEDYLAAFRAKEQQATEEVLELeqKLSVADAA------------RRQFEKAYELVCKIAGeVERSQAwqTARE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1438 LDKKQRNFdKILAE----WKQKYEESQSELESSqKEARSLSTELFKLKNAYEESLEHLETFKREnknLQEEISDLTEQLG 1513
Cdd:COG3096 500 LLRRYRSQ-QALAQrlqqLRAQLAELEQRLRQQ-QNAERLLEEFCQRIGQQLDAAEELEELLAE---LEAQLEELEEQAA 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1514 EGGKNVHELEKVRKQLEAEKLELQS------ALEEAEASLEHEEGKIL---RAQLEFNQIKAEIERKLAEKDEEMEQAKR 1584
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKELAArapawlAAQDALERLREQSGEALadsQEVTAAMQQLLEREREATVERDELAARKQ 654
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
971-1338 |
3.20e-05 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 49.24 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 971 HATENKVKNLTEEMAGLDEIiakLTKEKKALQEAHQQALDDLQAEEDK---------VNTLTKSKVKLEQQVDDLEGSLE 1041
Cdd:NF033838 36 HAEEVRGGNNPTVTSSGNES---QKEHAKEVESHLEKILSEIQKSLDKrkhtqnvalNKKLSDIKTEYLYELNVLKEKSE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1042 QE--KKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKK---------------------EFDISQQNSKIED 1098
Cdd:NF033838 113 AEltSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQkeedrrnyptntyktleleiaESDVEVKKAELEL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1099 EQALALQLQKKLKENQARIEELEEELEAERTARAKVEKlrsdlsrelEEISERLEEAGGATSVQIEMNKKREAEFQKMRR 1178
Cdd:NF033838 193 VKEEAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDR---------EKAEEEAKRRADAKLKEAVEKNVATSEQDKPKR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1179 DLEEATLQHEATAAALRKKHADSVAELGEQidNLQRVKQKLEKEKSEFKLELDDVTSnmeqiiKAKANLEKVSR------ 1252
Cdd:NF033838 264 RAKRGVLGEPATPDKKENDAKSSDSSVGEE--TLPSPSLKPEKKVAEAEKKVEEAKK------KAKDQKEEDRRnyptnt 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1253 --TLEDQANEYRTKLEEAQRSLndfTTQQAKlQTENGELARQ----LEEKEALISQLTRGKLSYTQQTEDLKRQLEEEGK 1326
Cdd:NF033838 336 ykTLELEIAESDVKVKEAELEL---VKEEAK-EPRNEEKIKQakakVESKKAEATRLEKIKTDRKKAEEEAKRKAAEEDK 411
|
410
....*....|..
gi 431907173 1327 AKNALAHALQSA 1338
Cdd:NF033838 412 VKEKPAEQPQPA 423
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1683-1867 |
3.30e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.24 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1683 ELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKK---AITDAA 1759
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKlntAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1760 MMAEELKKE--------------QDTSAHLERMKKNMEQtIKDLQHRLDEAE--QIALKGGKKQLQKLEARVRELENELE 1823
Cdd:PHA02562 269 SKIEQFQKVikmyekggvcptctQQISEGPDRITKIKDK-LKELQHSLEKLDtaIDELEEIMDEFNEQSKKLLELKNKIS 347
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 431907173 1824 AEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKL 1867
Cdd:PHA02562 348 TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1050-1204 |
3.32e-05 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 49.37 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1050 LERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKkefdISQQNSKIEDEQALALQLQKKLKENQARIeeleeeleaERT 1129
Cdd:COG1193 502 IERARELLGEESIDVEKLIEELERERRELEEEREE----AERLREELEKLREELEEKLEELEEEKEEI---------LEK 568
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1130 ARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAE 1204
Cdd:COG1193 569 AREEAEEILREARKEAEELIRELREA-----------QAEEEELKEARKKLEELKQELEEKLEKPKKKAKPAKPP 632
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1545-1858 |
3.38e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 49.26 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1545 ASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHL--RVVDSLQTSLDAETRSRNEALRVKkkmeGDLNEME 1622
Cdd:pfam05667 206 PSLLERNAAELAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLlkRIAEQLRSAALAGTEATSGASRSA----QDLAELL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1623 IQLSQANRTASEAQKHLKIAqaHLKDTQLQMDDAVRANDDLKENIAIVERRNNLlQAELEELRAVVEQTERSRKLAEQEL 1702
Cdd:pfam05667 282 SSFSGSSTTDTGLTKGSRFT--HTEKLQFTNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLESSIQELEKEI 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1703 ietservqllhsqntslinqkKKMESDLTQLQSEVEEavQECRNAEEKAKKAItdAAMMAEELKkeqDTSAHLERMKKNM 1782
Cdd:pfam05667 359 ---------------------KKLESSIKQVEEELEE--LKEQNEELEKQYKV--KKKTLDLLP---DAEENIAKLQALV 410
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1783 EQTIKDLQH--RLDEAEQIALkggkkqLQKLEaRVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLL 1858
Cdd:pfam05667 411 DASAQRLVElaGQWEKHRVPL------IEEYR-ALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLV 481
|
|
| SH3_ASPP1 |
cd11954 |
Src Homology 3 domain of Apoptosis Stimulating of p53 protein 1; ASPP1, like ASPP2, activates ... |
1929-1985 |
3.46e-05 |
|
Src Homology 3 domain of Apoptosis Stimulating of p53 protein 1; ASPP1, like ASPP2, activates the apoptotic function of the p53 family of tumor suppressors (p53, p63, and p73). In addition, it functions in the cytoplasm to regulate the nuclear localization of the transcriptional cofactors YAP and TAZ by inihibiting their phosphorylation; YAP and TAZ are important regulators of cell expansion, differentiation, migration, and invasion. ASPP1 is downregulated in breast tumors expressing wild-type p53. It contains a proline-rich region, four ankyrin (ANK) repeats, and an SH3 domain at its C-terminal half. The SH3 domain and the ANK repeats of ASPP1 contribute to the p53 binding site; they bind to the DNA binding domain of p53. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212887 [Multi-domain] Cd Length: 57 Bit Score: 43.47 E-value: 3.46e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1929 LARALYDNTAESPQELSFRRGDVLRVLQREGAGGLDgWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd11954 2 MVYALWDYEAQNADELSFQEGDAITILRRKDDSETE-WWWARLNDKEGYVPKNLLGL 57
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1128-1921 |
3.56e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 49.44 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1128 RTARAKVEKLRSDLSRELEEISERLEEAggATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAA-----ALRKKHADSV 1202
Cdd:NF041483 308 RTAKEEIARLVGEATKEAEALKAEAEQA--LADARAEAEKLVAEAAEKARTVAAEDTAAQLAKAArtaeeVLTKASEDAK 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1203 AELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKakanlekvsrtleDQANEYRTK---LEEAQRSLNDFTTQQ 1279
Cdd:NF041483 386 ATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAK-------------DDTKEYRAKtveLQEEARRLRGEAEQL 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1280 AKLQTENGELARQLEEKEALisqltrgklsytQQTEDLKRQLEEE-GKAKNALAHALQSARHDCDLLR-EQYEEETEAKA 1357
Cdd:NF041483 453 RAEAVAEGERIRGEARREAV------------QQIEEAARTAEELlTKAKADADELRSTATAESERVRtEAIERATTLRR 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1358 ELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAA 1437
Cdd:NF041483 521 QAEETLERTRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALADARA 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1438 LDKKQR-----NFDKILAEWKQKyeeSQSELESSQKEARSLSTE---------------LFKLKNAYEESLEHLETFKRE 1497
Cdd:NF041483 601 EAERIRreaaeETERLRTEAAER---IRTLQAQAEQEAERLRTEaaadasaaraegenvAVRLRSEAAAEAERLKSEAQE 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1498 NKN-LQEEISDLTEQLGEGGK---NVHELEKVRKQLEAEKL----------ELQSALEEAEASLEHEEGKILRAQLEFNQ 1563
Cdd:NF041483 678 SADrVRAEAAAAAERVGTEAAealAAAQEEAARRRREAEETlgsaraeadqERERAREQSEELLASARKRVEEAQAEAQR 757
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1564 IKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAET------------RSRNEALRVKKKMEGD-LNEMEIQLSQANR 1630
Cdd:NF041483 758 LVEEADRRATELVSAAEQTAQQVRDSVAGLQEQAEEEIaglrsaaehaaeRTRTEAQEEADRVRSDaYAERERASEDANR 837
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1631 TASEAQKHLKIAQAHLKDTqlqMDDAVRANDDLKENIAIVERRnnlLQAELEELRAVVEQ-TERSRKLAEQEL----IET 1705
Cdd:NF041483 838 LRREAQEETEAAKALAERT---VSEAIAEAERLRSDASEYAQR---VRTEASDTLASAEQdAARTRADAREDAnrirSDA 911
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1706 SERVQLLHSQNTSLINQ-KKKMESDLTQLQSEVEEAVQECR-NAEEKAKKAITDAAMMAEELKKEQ-----DTSAHLERM 1778
Cdd:NF041483 912 AAQADRLIGEATSEAERlTAEARAEAERLRDEARAEAERVRaDAAAQAEQLIAEATGEAERLRAEAaetvgSAQQHAERI 991
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1779 KKNMEQTIKDLQhrlDEAEQIalkggkkqlqKLEARV---RELENELEAEQKRNAESVKgmrKSERRIKELTYQTEEdkk 1855
Cdd:NF041483 992 RTEAERVKAEAA---AEAERL----------RTEAREeadRTLDEARKDANKRRSEAAE---QADTLITEAAAEADQ--- 1052
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1856 nllrlqdLVDKLQlkvKAYKRQAEEAEEQANTNLSKFRKvqheldEAEERADIAESQVNKLRAKSR 1921
Cdd:NF041483 1053 -------LTAKAQ---EEALRTTTEAEAQADTMVGAARK------EAERIVAEATVEGNSLVEKAR 1102
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1567-1910 |
3.77e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1567 EIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRTASEAQKHLKIAQAHL 1646
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1647 KDTQLQMDDAVRANDDLKENIAIVERRNNLLQAELEELRAvveqterSRKLAEQELIETSERVQLLHSQNTSLINQKKKM 1726
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK-------ERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1727 ESDLTQLQSEVEEAVQECRNAEEKAKKAItdaammAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKK 1806
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAEAEQA------LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1807 QLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQAN 1886
Cdd:COG4372 230 KLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
330 340
....*....|....*....|....
gi 431907173 1887 TNLSKFRKVQHELDEAEERADIAE 1910
Cdd:COG4372 310 IGALEDALLAALLELAKKLELALA 333
|
|
| SH3_srGAP4 |
cd11956 |
Src homology 3 domain of Slit-Robo GTPase Activating Protein 4; srGAP4, also called ARHGAP4, ... |
1930-1979 |
3.91e-05 |
|
Src homology 3 domain of Slit-Robo GTPase Activating Protein 4; srGAP4, also called ARHGAP4, is highly expressed in hematopoietic cells and may play a role in lymphocyte differentiation. It is able to stimulate the GTPase activity of Rac1, Cdc42, and RhoA. In the nervous system, srGAP4 has been detected in differentiating neurites and may be involved in axon and dendritic growth. srGAPs are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. srGAPs contain an N-terminal F-BAR domain, a Rho GAP domain, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212889 [Multi-domain] Cd Length: 55 Bit Score: 43.29 E-value: 3.91e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGAggldGWCLCSLHGQQGIVP 1979
Cdd:cd11956 4 AVACFDYTGRTAQELSFKRGDVLLLHSKASS----DWWRGEHNGMRGLIP 49
|
|
| PHA03321 |
PHA03321 |
tegument protein VP11/12; Provisional |
1989-2215 |
4.13e-05 |
|
tegument protein VP11/12; Provisional
Pssm-ID: 223041 [Multi-domain] Cd Length: 694 Bit Score: 49.19 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1989 GPTPK--PSLSQVPPAEPGSPyPAPEHSNEdqevyvvPPPARPCLTSESPAGPCLPspdpiyKVPRGSGTQPATPGDALE 2066
Cdd:PHA03321 413 VPSEHyeASLRLLSSRQPPGA-PAPRRDND-------PPPPPRARPGSTPACARRA------RAQRARDAGPEYVDPLGA 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2067 VYDVPPAALRVSASGPYDTPASFSHLLARVAPQPPGEDEAPYDVPLAPKPPSELEPD------LEWEGGREPGPPLYAAP 2140
Cdd:PHA03321 479 LRRLPAGAAPPPEPAAAPSPATYYTRMGGGPPRLPPRNRATETLRPDWGPPAAAPPEqmedpyLEPDDDRFDRRDGAAAA 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2141 SNLKRASALLNLYEAPEELLADGEEGGSDE----GIYDVPLLGPE----------TPPSP-----EPL-----GALASND 2196
Cdd:PHA03321 559 ATSHPREAPAPDDDPIYEGVSDSEEPVYEEiptpRVYQNPLPRPMegageppdldAPTSPwveeeNPIygwgdSPLFSPP 638
|
250 260
....*....|....*....|....*
gi 431907173 2197 PDTLA----LLLARSPP--PSHRPR 2215
Cdd:PHA03321 639 PAARFpppdPALSPEPPalPAHRPR 663
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1238-1580 |
4.41e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1238 EQIIKAKANLEKVS---RTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLTRGKLSYTQQT 1314
Cdd:COG4372 31 EQLRKALFELDKLQeelEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1315 EDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKLQ 1394
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1395 DAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKyeesqsELESSQKEARSLS 1474
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL------LEEVILKEIEELE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1475 TELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKI 1554
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQ 344
|
330 340
....*....|....*....|....*.
gi 431907173 1555 LRAQLEFNQIKAEIERKLAEKDEEME 1580
Cdd:COG4372 345 LLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1492-1847 |
4.56e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.74 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1492 ETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEA-------EKLELQSALEEAEASLEHEEGKI-------LRA 1557
Cdd:pfam07888 69 EQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAsseelseEKDALLAQRAAHEARIRELEEDIktltqrvLER 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1558 QLEFNQIKAEIERKLAEKDEEMEQAKrnhlrvvdSLQTSLDAetrSRNEALRVKKKMEGDLNEMEIQLSQANRTASE-AQ 1636
Cdd:pfam07888 149 ETELERMKERAKKAGAQRKEEEAERK--------QLQAKLQQ---TEEELRSLSKEFQELRNSLAQRDTQVLQLQDTiTT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1637 KHLKIAQAHLKDTQL-QMDDAVRAnddLKENIAIVERRNNLLQAELEEL------------RAVVEQTERSRKLAEQELI 1703
Cdd:pfam07888 218 LTQKLTTAHRKEAENeALLEELRS---LQERLNASERKVEGLGEELSSMaaqrdrtqaelhQARLQAAQLTLQLADASLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1704 ETSERVQLlhSQNTSLINQKKKMESDLTQLQSE----VEEAVQECRNAEEKAKKaitdaammaeELKKEQDTSahlermk 1779
Cdd:pfam07888 295 LREGRARW--AQERETLQQSAEADKDRIEKLSAelqrLEERLQEERMEREKLEV----------ELGREKDCN------- 355
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1780 knmeqtikdlqhrldeaeQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELT 1847
Cdd:pfam07888 356 ------------------RVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVA 405
|
|
| SH3_SKAP2 |
cd12045 |
Src Homology 3 domain of Src Kinase-Associated Phosphoprotein 2; SKAP2, also called ... |
1931-1979 |
4.73e-05 |
|
Src Homology 3 domain of Src Kinase-Associated Phosphoprotein 2; SKAP2, also called SKAP55-Related (SKAP55R) or SKAP55 homolog (SKAP-HOM or SKAP55-HOM), is an immune cell-specific adaptor protein that plays an important role in adhesion and migration of B-cells and macrophages. Binding partners include ADAP (adhesion and degranulation-promoting adaptor protein), YopH, SHPS1, and HPK1. SKAP2 has also been identified as a substrate for lymphoid-specific tyrosine phosphatase (Lyp), which has been implicated in a wide variety of autoimmune diseases. It contains a pleckstrin homology (PH) domain, a C-terminal SH3 domain, and several tyrosine phosphorylation sites. Like SKAP1, SKAP2 is expected to bind primarily to a proline-rich region of ADAP through its SH3 domain; its degradation may be regulated by ADAP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212978 Cd Length: 53 Bit Score: 42.97 E-value: 4.73e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREgaGGLDGWCLCSLHGQQGIVP 1979
Cdd:cd12045 3 QGLWDCTGDQPDELSFKRGDTIYILSKE--YNRFGWWVGEMKGTIGLVP 49
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
845-1295 |
4.95e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 49.06 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 845 AETEKEMANMKEEFGRLKETLEKsearrkeLEEKMVSLLQEKNDLQLqvqaEQDNLNDAeercdqlikNKIQLEAK---V 921
Cdd:PTZ00440 1112 VNADKEKNKQTEHYNKKKKSLEK-------IYKQMEKTLKELENMNL----EDITLNEV---------NEIEIEYErilI 1171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 922 KEMNERLEDEeemnaeltAKKRKLEDEcsELKRDIDDLELTLAKVEKEK--HATENKVKNLTEEMAGLDEIIAKLTKEKK 999
Cdd:PTZ00440 1172 DHIVEQINNE--------AKKSKTIME--EIESYKKDIDQVKKNMSKERndHLTTFEYNAYYDKATASYENIEELTTEAK 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1000 ALQEA--HQQALDDLQAEEDKVNTLTKskvKLEQQVDDLEGSLEQEKKVRMDLERAK-------------------RKLE 1058
Cdd:PTZ00440 1242 GLKGEanRSTNVDELKEIKLQVFSYLQ---QVIKENNKMENALHEIKNMYEFLISIDsekilkeilnstkkaeefsNDAK 1318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1059 GDLKLTQESIMDLENDKLQLEEklKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTaRAKVEKLR 1138
Cdd:PTZ00440 1319 KELEKTDNLIKQVEAKIEQAKE--HKNKIYGSLEDKQIDDEIKKIEQIKEEISNKRKEINKYLSNIKSNKE-KCDLHVRN 1395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1139 SDLSRELEEISERLEEAGGATSVQIEMNKKREAeFQKMRRDLEEATlqheATAAALRKKHaDSVAELGEQIDNLQRVKQK 1218
Cdd:PTZ00440 1396 ASRGKDKIDFLNKHEAIEPSNSKEVNIIKITDN-INKCKQYSNEAM----ETENKADENN-DSIIKYEKEITNILNNSSI 1469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1219 LEKEKsEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYR--TKLEEAQRSLNDFTTQQAK--LQTENGELARQLE 1294
Cdd:PTZ00440 1470 LGKKT-KLEKKKKEATNIMDDINGEHSIIKTKLTKSSEKLNQLNeqPNIKREGDVLNNDKSTIAYetIQYNLGRVKHNLL 1548
|
.
gi 431907173 1295 E 1295
Cdd:PTZ00440 1549 N 1549
|
|
| SH3_PACSIN1-2 |
cd11998 |
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1) ... |
1931-1984 |
5.03e-05 |
|
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1) and PACSIN 2; PACSIN 1 or Syndapin I (Synaptic dynamin-associated protein I) is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. PACSIN 2 or Syndapin II is expressed ubiquitously and is involved in the regulation of tubulin polymerization. It associates with Golgi membranes and forms a complex with dynamin II which is crucial in promoting vesicle formation from the trans-Golgi network. PACSINs act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212931 [Multi-domain] Cd Length: 56 Bit Score: 43.01 E-value: 5.03e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGAgglDGWCLCSL-HGQQGIVPANRVK 1984
Cdd:cd11998 4 RALYDYDGQEQDELSFKAGDELTKLEDEDE---QGWCKGRLdSGQVGLYPANYVE 55
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1972-2138 |
5.48e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 49.01 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1972 HGQQGIVPANRVKLLPAGPTPKPSLSQVPPAEPGSPYPAPEHSNEDQEVYVVPPPARPCLTSESPAGpcLPSPDPIYKVP 2051
Cdd:PHA03307 259 RPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESS--SSSTSSSSESS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2052 RGSGTQP-------ATPGDALEVYDVPP--AALRVSASGPYDTPASFSHLLARVAPQPPGED---EAPYDVPLAPKPPSE 2119
Cdd:PHA03307 337 RGAAVSPgpspsrsPSPSRPPPPADPSSprKRPRPSRAPSSPAASAGRPTRRRARAAVAGRArrrDATGRFPAGRPRPSP 416
|
170
....*....|....*....
gi 431907173 2120 LEPDLEWEGGREPGPPLYA 2138
Cdd:PHA03307 417 LDAGAASGAFYARYPLLTP 435
|
|
| SH3_Sho1p |
cd11855 |
Src homology 3 domain of High osmolarity signaling protein Sho1p; Sho1p (or Sho1), also called ... |
1930-1985 |
5.61e-05 |
|
Src homology 3 domain of High osmolarity signaling protein Sho1p; Sho1p (or Sho1), also called SSU81 (Suppressor of SUA8-1 mutation), is a yeast membrane protein that regulates adaptation to high salt conditions by activating the HOG (high-osmolarity glycerol) pathway. High salt concentrations lead to the localization to the membrane of the MAPKK Pbs2, which is then activated by the MAPKK Ste11 and in turn, activates the MAPK Hog1. Pbs2 is localized to the membrane though the interaction of its PxxP motif with the SH3 domain of Sho1p. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212789 [Multi-domain] Cd Length: 55 Bit Score: 42.79 E-value: 5.61e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1930 ARALYDNTA--ESPQELSFRRGDVLRVLQREGagglDGWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd11855 2 ARALYPYDAspDDPNELSFEKGEILEVSDTSG----KWWQARKSNGETGICPSNYLQL 55
|
|
| SH3_PIX |
cd11877 |
Src Homology 3 domain of Pak Interactive eXchange factors; PIX proteins are Rho guanine ... |
1929-1985 |
5.74e-05 |
|
Src Homology 3 domain of Pak Interactive eXchange factors; PIX proteins are Rho guanine nucleotide exchange factors (GEFs), which activate small GTPases by exchanging bound GDP for free GTP. They act as GEFs for both Cdc42 and Rac 1, and have been implicated in cell motility, adhesion, neurite outgrowth, and cell polarity. Vertebrates contain two proteins from the PIX subfamily, alpha-PIX and beta-PIX. Alpha-PIX, also called ARHGEF6, is localized in dendritic spines where it regulates spine morphogenesis. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. Beta-PIX play roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion. PIX proteins contain an N-terminal SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains, and a C-terminal leucine-zipper domain for dimerization. The SH3 domain of PIX binds to an atypical PxxxPR motif in p21-activated kinases (PAKs) with high affinity. The binding of PAKs to PIX facilitate the localization of PAKs to focal complexes and also localizes PAKs to PIX targets Cdc43 and Rac, leading to the activation of PAKs. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212810 [Multi-domain] Cd Length: 53 Bit Score: 42.69 E-value: 5.74e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1929 LARALYDNTAESPQELSFRRGDVLRVLQR-EGaggldGWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd11877 1 LVRAKFNFEGTNEDELSFDKGDIITVTQVvEG-----GWWEGTLNGKTGWFPSNYVKE 53
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
857-1323 |
5.92e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.58 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 857 EFGRLKETLEKSEARRKELEEKMVSLLQEkndLQLQVQ-------------------AEQDNLNDAEERCDQLIKNKIQL 917
Cdd:pfam05557 150 EAEQLRQNLEKQQSSLAEAEQRIKELEFE---IQSQEQdseivknskselaripeleKELERLREHNKHLNENIENKLLL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 918 EAKVKEMNERLEDEEEMNAELTA---KKRKLEDECSELKRDIDDLELTLAKVEkekhATENKVKNLTEEMAGLDEIIAKL 994
Cdd:pfam05557 227 KEEVEDLKRKLEREEKYREEAATlelEKEKLEQELQSWVKLAQDTGLNLRSPE----DLSRRIEQLQQREIVLKEENSSL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 995 TKEKKALQEAHQQalddlqaeedkvntltkskvkLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKL-TQEsiMDLen 1073
Cdd:pfam05557 303 TSSARQLEKARRE---------------------LEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLlTKE--RDG-- 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1074 dklqLEEKLKKKEFDISQQNSkiedeqalALQLQKKLKEnqarieeleeeleaertarakVEKLRSDLSRELEEISERLE 1153
Cdd:pfam05557 358 ----YRAILESYDKELTMSNY--------SPQLLERIEE---------------------AEDMTQKMQAHNEEMEAQLS 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1154 EAGGATSVQIEMNKKREAEFQKMRRDleeatlqheaTAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELddv 1233
Cdd:pfam05557 405 VAEEELGGYKQQAQTLERELQALRQQ----------ESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMEL--- 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1234 tsnMEQIIKAKANLEKvSRTLEDQANeyrTKLEEAQRSLNdfttQQAKLQTENGELARQLEEKEALISQLTRGKLSYT-- 1311
Cdd:pfam05557 472 ---ERRCLQGDYDPKK-TKVLHLSMN---PAAEAYQQRKN----QLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTStm 540
|
490
....*....|....
gi 431907173 1312 --QQTEDLKRQLEE 1323
Cdd:pfam05557 541 nfKEVLDLRKELES 554
|
|
| SH3_Src_like |
cd11845 |
Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members ... |
1931-1981 |
6.06e-05 |
|
Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, Yes, and Brk. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). However, Brk lacks the N-terminal myristoylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells, and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, Lyn, and Brk show a limited expression pattern. This subfamily also includes Drosophila Src42A, Src oncogene at 42A (also known as Dsrc41) which accumulates at sites of cell-cell or cell-matrix adhesion, and participates in Drosphila development and wound healing. It has been shown to promote tube elongation in the tracheal system, is essential for proper cell-cell matching during dorsal closure, and regulates cell-cell contacts in developing Drosophila eyes. The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212779 [Multi-domain] Cd Length: 52 Bit Score: 42.57 E-value: 6.06e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGAgglDGWCLCSLH-GQQGIVPAN 1981
Cdd:cd11845 3 VALYDYEARTDDDLSFKKGDRLQILDDSDG---DWWLARHLStGKEGYIPSN 51
|
|
| SH3_Intersectin_5 |
cd11840 |
Fifth Src homology 3 domain (or SH3E) of Intersectin; Intersectins (ITSNs) are adaptor ... |
1931-1985 |
6.07e-05 |
|
Fifth Src homology 3 domain (or SH3E) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The fifth SH3 domain (or SH3E) of ITSN1 has been shown to bind many protein partners including SGIP1, Sos1, dynamin1/2, CIN85, c-Cbl, SHIP2, N-WASP, and synaptojanin-1, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212774 [Multi-domain] Cd Length: 53 Bit Score: 42.79 E-value: 6.07e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGAggldGWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd11840 3 IALFPYTAQNEDELSFQKGDIINVLSKDDP----DWWRGELNGQTGLFPSNYVEP 53
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1189-1409 |
6.22e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1189 ATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELD----DVTSNMEQIIKAKANLEKVSRTLEDQANEYRTK 1264
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNelqaELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1265 LEEAQRSLNDFTTQQAKLQTEN-GELARQLEekeaLISQLTRGKLSYTQQTEDLKRQLEEegkAKNALAHALQSarhdcd 1343
Cdd:COG3883 92 ARALYRSGGSVSYLDVLLGSESfSDFLDRLS----ALSKIADADADLLEELKADKAELEA---KKAELEAKLAE------ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1344 lLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKLQDAEEAVEAVNAKCSS 1409
Cdd:COG3883 159 -LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
913-1182 |
6.22e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.58 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 913 NKIQLEAKVKEM-NERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDeiI 991
Cdd:pfam17380 285 SERQQQEKFEKMeQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRE--L 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 992 AKLTKEKKALQEAHQQALDDLQAEEDKVN--------TLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAK----RKLEG 1059
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELERLQMERQQKNervrqeleAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARqrevRRLEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1060 DLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQAlalqlQKKLKENQARiEELEEELEAERTARAKVEKLRS 1139
Cdd:pfam17380 443 ERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKR-----DRKRAEEQRR-KILEKELEERKQAMIEEERKRK 516
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 431907173 1140 DLSRELEEIS------ERLEEAGGATSVQIEMNKKREAEfQKMRRDLEE 1182
Cdd:pfam17380 517 LLEKEMEERQkaiyeeERRREAEEERRKQQEMEERRRIQ-EQMRKATEE 564
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1760-1919 |
6.23e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1760 MMAEELKK-----EQDTS-AHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELENELEAEQKRNAESV 1833
Cdd:COG1579 1 AMPEDLRAlldlqELDSElDRLEHRLKELPAELAELEDELAALEA-RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1834 K--GMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAES 1911
Cdd:COG1579 80 EqlGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
....*...
gi 431907173 1912 QVNKLRAK 1919
Cdd:COG1579 160 ELEAEREE 167
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
976-1223 |
6.47e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 976 KVKNLTEEMAGLD----EIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEgslEQEKKVRMDLE 1051
Cdd:PHA02562 175 KIRELNQQIQTLDmkidHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELT---DELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1052 rakrKLEGDL-KLTQESI-MDLENDKLQLEEKLKKK-------EFDISQQNSKIEDEQALALQLQKKLKENQARIEELEE 1122
Cdd:PHA02562 252 ----DPSAALnKLNTAAAkIKSKIEQFQKVIKMYEKggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1123 ELEAERTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnKKREAEFQKmrrdleeatlqheatAAALRKKHADSV 1202
Cdd:PHA02562 328 IMDEFNEQSKKLLELKNKISTNKQSLITLVDKA-----------KKVKAAIEE---------------LQAEFVDNAEEL 381
|
250 260
....*....|....*....|.
gi 431907173 1203 AELGEQIDNLQRVKQKLEKEK 1223
Cdd:PHA02562 382 AKLQDELDKIVKTKSELVKEK 402
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
991-1172 |
6.59e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 991 IAKLTKEKKaLQEAHQQALDDLQAEEDKVNTLTKSKVkleqqvddlegsLEQEKKVrmdlERAKRKLEGDLKLTQESIMD 1070
Cdd:PRK12704 24 VRKKIAEAK-IKEAEEEAKRILEEAKKEAEAIKKEAL------------LEAKEEI----HKLRNEFEKELRERRNELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1071 LENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEEleaertARAKVEKLrSDLSRE------ 1144
Cdd:PRK12704 87 LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE------QLQELERI-SGLTAEeakeil 159
|
170 180
....*....|....*....|....*...
gi 431907173 1145 LEEISERLEEAGGATSVQIEMNKKREAE 1172
Cdd:PRK12704 160 LEKVEEEARHEAAVLIKEIEEEAKEEAD 187
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
1973-2229 |
7.56e-05 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 48.14 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1973 GQQGIVPANRVKLLPAGPTPKPSLSQVPPAEPGSPYPAPEHSNEDQEVYVVPPPArPCLTSESPAGPCLPSPDPIYKVPR 2052
Cdd:COG5180 205 EVKDEAQEEPPDLTGGADHPRPEAASSPKVDPPSTSEARSRPATVDAQPEMRPPA-DAKERRRAAIGDTPAAEPPGLPVL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2053 GSGTQPATPGDALEVY---DVPPAALRVSASGPYDTPASfshLLARVAPQPPGEDEAPYDVPL----APKPPSELEPdle 2125
Cdd:COG5180 284 EAGSEPQSDAPEAETArpiDVKGVASAPPATRPVRPPGG---ARDPGTPRPGQPTERPAGVPEaasdAGQPPSAYPP--- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2126 weggREPGPPLYAAPSNLKRASallnlyeapeELLADGEEGGSDEGIYDVPLLGPETPPSPEPLGALASNDPD-----TL 2200
Cdd:COG5180 358 ----AEEAVPGKPLEQGAPRPG----------SSGGDGAPFQPPNGAPQPGLGRRGAPGPPMGAGDLVQAALDgggreTA 423
|
250 260
....*....|....*....|....*....
gi 431907173 2201 ALLLARSPPPSHRPRLPSAESLSRRPLPA 2229
Cdd:COG5180 424 SLGGAAGGAGQGPKADFVPGDAESVSGPA 452
|
|
| SH3_Intersectin1_5 |
cd11995 |
Fifth Src homology 3 domain (or SH3E) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor ... |
1932-1985 |
8.10e-05 |
|
Fifth Src homology 3 domain (or SH3E) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN1 localizes in membranous organelles, CCPs, the Golgi complex, and may be involved in the cell membrane trafficking system. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The fifth SH3 domain (or SH3E) of ITSN1 has been shown to bind many protein partners including SGIP1, Sos1, dynamin1/2, CIN85, c-Cbl, SHIP2, N-WASP, and synaptojanin-1, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212928 [Multi-domain] Cd Length: 54 Bit Score: 42.25 E-value: 8.10e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQREGAggldGWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd11995 5 GMYDYTAQNDDELAFSKGQIINVLNKEDP----DWWKGELNGQVGLFPSNYVKL 54
|
|
| SH3_ASPP2 |
cd11953 |
Src Homology 3 (SH3) domain of Apoptosis Stimulating of p53 protein 2; ASPP2 is the full ... |
1932-1985 |
8.35e-05 |
|
Src Homology 3 (SH3) domain of Apoptosis Stimulating of p53 protein 2; ASPP2 is the full length form of the previously-identified tumor supressor, p53-binding protein 2 (p53BP2). ASPP2 activates the apoptotic function of the p53 family of tumor suppressors (p53, p63, and p73). It plays a central role in regulating apoptosis and cell growth; ASPP2-deficient mice show postnatal death. Downregulated expression of ASPP2 is frequently found in breast tumors, lung cancer, and diffuse large B-cell lymphoma where it is correlated with a poor clinical outcome. ASPP2 contains a proline-rich region, four ankyrin (ANK) repeats, and an SH3 domain at its C-terminal half. The SH3 domain and the ANK repeats of ASPP2 contribute to the p53 binding site; they bind to the DNA binding domain of p53. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212886 [Multi-domain] Cd Length: 57 Bit Score: 42.25 E-value: 8.35e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQREGAGGLDgWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd11953 5 ALWDYEGESDDELSFKEGDCMTILRREDEDETE-WWWARLNDKEGYVPRNLLGL 57
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
867-1015 |
8.38e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 867 KSEARRKELEEKMVSLLQEKNdlqlqvqaeqdnlNDAEErcdqlIKNKIQLEAKVKEMNERLEDEEE---MNAELTAKKR 943
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAK-------------KEAEA-----IKKEALLEAKEEIHKLRNEFEKElreRRNELQKLEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 944 KLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAK----------LTKEkkalqEAHQQALDDLQ 1013
Cdd:PRK12704 90 RLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEqlqelerisgLTAE-----EAKEILLEKVE 164
|
..
gi 431907173 1014 AE 1015
Cdd:PRK12704 165 EE 166
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1072-1323 |
9.63e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 47.71 E-value: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1072 ENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIeeleeeleaeRTARAKVEKLRSDLSRELEEISER 1151
Cdd:pfam05667 211 RNAAELAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQL----------RSAALAGTEATSGASRSAQDLAEL 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1152 LEEAGGATSVQIEMNK------KREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEkse 1225
Cdd:pfam05667 281 LSSFSGSSTTDTGLTKgsrfthTEKLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKE--- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1226 fkleLDDVTSNMEQIikaKANLEKVSRTLEDQANEYRTK------LEEAQRSLndfttqqAKLQTENG-------ELARQ 1292
Cdd:pfam05667 358 ----IKKLESSIKQV---EEELEELKEQNEELEKQYKVKkktldlLPDAEENI-------AKLQALVDasaqrlvELAGQ 423
|
250 260 270
....*....|....*....|....*....|..
gi 431907173 1293 LEEK-EALISQLTRGKLSYTQQTEDLKRQLEE 1323
Cdd:pfam05667 424 WEKHrVPLIEEYRALKEAKSNKEDESQRKLEE 455
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1392-1585 |
1.01e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1392 KLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKyeesqselessqkeAR 1471
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR--------------IK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1472 SLSTELFKLKNAYE-ESLEH-LETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEASLEh 1549
Cdd:COG1579 77 KYEEQLGNVRNNKEyEALQKeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE- 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 431907173 1550 EEGKILRAQLEfnQIKAEIERKLAEKDEEMEQAKRN 1585
Cdd:COG1579 156 AELEELEAERE--ELAAKIPPELLALYERIRKRKNG 189
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
1377-1794 |
1.03e-04 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 47.84 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1377 YETDAI---QRTEELEEAKLQ-DAEEAVEAVNAKCSSL-EKTKHRLQNEIEDLMVDVER-----SNAAAAALDKKQRNFD 1446
Cdd:pfam18971 381 YKEDQLtgsQRALSQEEIRNKvDFMEFLAQNNTKLDNLsEKEKEKFQNEIEDFQKDSKAyldalGNDRIAFVSKKDTKHS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1447 KILAEWK--------QKYEESQSELESSQKEArSLSTEL------------FKLKNAYEE---------SLEHLE----- 1492
Cdd:pfam18971 461 ALITEFNngdlsytlKDYGKKADKALDREKNV-TLQGSLkhdgvmfvdysnFKYTNASKNpnkgvgatnGVSHLEagfnk 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1493 ---------------TFKRenKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEASLEHEegkilra 1557
Cdd:pfam18971 540 vavfnlpdlnnlaitSFVR--RNLENKLTAKGLSLQEANKLIKDFLSSNKELAGKALNFNKAVAEAKSTGNYD------- 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1558 qlefnqikaeiERKLAEKDEEMEQAKRNHLRvvDSLQTSLDAETRSRNealRVKKKMEGDLNEMEIqLSQANRTASEAQK 1637
Cdd:pfam18971 611 -----------EVKKAQKDLEKSLRKREHLE--KEVEKKLESKSGNKN---KMEAKAQANSQKDEI-FALINKEANRDAR 673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1638 HLKIAQaHLKDTQLQMDDAV-RANDDLKENIAIVERRNNLLQAELEElravVEQTERSRKLAEQELIETSERVQLLHSQN 1716
Cdd:pfam18971 674 AIAYTQ-NLKGIKRELSDKLeKISKDLKDFSKSFDEFKNGKNKDFSK----AEETLKALKGSVKDLGINPEWISKVENLN 748
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1717 TSL---INQKKKMESDLTQLQSEVEEAV------QECRNAEEKAKKAITDAAMMAEELKKEQdTSAHLERMKKnmEQTIK 1787
Cdd:pfam18971 749 AALnefKNGKNKDFSKVTQAKSDLENSVkdviinQKVTDKVDNLNQAVSVAKAMGDFSRVEQ-VLADLKNFSK--EQLAQ 825
|
....*..
gi 431907173 1788 DLQHRLD 1794
Cdd:pfam18971 826 QAQKNED 832
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
847-1117 |
1.06e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 47.44 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 847 TEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDN--LNDAEERCDQLIKNKIQLEAKVKEm 924
Cdd:pfam09731 159 VKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPplLDAAPETPPKLPEHLDNVEEKVEK- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 925 NERLEDEEEMNAELTAKKRklEDECSELKRDIDDLELTLAKVEKEKHATENKVknLTEEMAGLDEIIAKLTKEKKALQEA 1004
Cdd:pfam09731 238 AQSLAKLVDQYKELVASER--IVFQQELVSIFPDIIPVLKEDNLLSNDDLNSL--IAHAHREIDQLSKKLAELKKREEKH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1005 HQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESImdleNDKLQLEEKLKK 1084
Cdd:pfam09731 314 IERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAH----EEHLKDVLVEQE 389
|
250 260 270
....*....|....*....|....*....|....*.
gi 431907173 1085 KEFDISQQ---NSKIEDEQALalqLQKKLKENQARI 1117
Cdd:pfam09731 390 IELQREFLqdiKEKVEEERAG---RLLKLNELLANL 422
|
|
| SH3_Sorbs2_1 |
cd11920 |
First Src Homology 3 domain of Sorbin and SH3 domain containing 2 (Sorbs2), also called ... |
1930-1986 |
1.08e-04 |
|
First Src Homology 3 domain of Sorbin and SH3 domain containing 2 (Sorbs2), also called Arg-binding protein 2 (ArgBP2); Sorbs2 or ArgBP2 is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It regulates actin-dependent processes including cell adhesion, morphology, and migration. It is expressed in many tissues and is abundant in the heart. Like vinexin, it is found in focal adhesion where it interacts with vinculin and afadin. It also localizes in epithelial cell stress fibers and in cardiac muscle cell Z-discs. Sorbs2 has been implicated to play roles in the signaling of c-Arg, Akt, and Pyk2. Other interaction partners of Sorbs2 include c-Abl, flotillin, spectrin, dynamin 1/2, synaptojanin, PTP-PEST, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212853 [Multi-domain] Cd Length: 55 Bit Score: 41.92 E-value: 1.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQRegaggLD-GWCLCSLHGQQGIVPANRVKLL 1986
Cdd:cd11920 3 ARAVYDFKAQTSKELSFKKGDTVYILRK-----IDqNWYEGEHHGRVGIFPISYVEKL 55
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1781-1928 |
1.10e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1781 NMEQTIK---DLQHRLDEAEQIA--LKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKK 1855
Cdd:COG1579 1 AMPEDLRallDLQELDSELDRLEhrLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1856 NLLRLQDL--VDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKAQ 1928
Cdd:COG1579 81 QLGNVRNNkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
979-1251 |
1.11e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 979 NLTEEMAGLDEIIAKLTKE----KKALQEAhQQALDDLQAEEDKVNTLTKSKVkLEQQVDDLEGSLEQEKKVRMDLERAK 1054
Cdd:COG3206 165 NLELRREEARKALEFLEEQlpelRKELEEA-EAALEEFRQKNGLVDLSEEAKL-LLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1055 RKLEGDLKLTQESIMDLENDklQLEEKLKKKEFDISQQnskiedeqaLAlQLQKKLKENQARIeeleeeleaeRTARAKV 1134
Cdd:COG3206 243 AALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAE---------LA-ELSARYTPNHPDV----------IALRAQI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1135 EKLRSDLSRELEEISERLEeaggatsVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRkkhadsvaELGEQIDNLQR 1214
Cdd:COG3206 301 AALRAQLQQEAQRILASLE-------AELEALQAREASLQAQLAQLEARLAELPELEAELR--------RLEREVEVARE 365
|
250 260 270
....*....|....*....|....*....|....*..
gi 431907173 1215 VKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVS 1251
Cdd:COG3206 366 LYESLLQRLEEARLAEALTVGNVRVIDPAVVPLKPVS 402
|
|
| SH3_MLK |
cd11876 |
Src Homology 3 domain of Mixed Lineage Kinases; MLKs are Serine/Threonine Kinases (STKs), ... |
1932-1983 |
1.17e-04 |
|
Src Homology 3 domain of Mixed Lineage Kinases; MLKs are Serine/Threonine Kinases (STKs), catalyzing the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212809 [Multi-domain] Cd Length: 58 Bit Score: 42.11 E-value: 1.17e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQRE-GAGGLDGWCLCSLHGQQGIVPANRV 1983
Cdd:cd11876 4 ALFDYDARGEDELTLRRGQPVEVLSKDaAVSGDEGWWTGKIGDKVGIFPSNYV 56
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1730-1939 |
1.19e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 46.18 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1730 LTQLQSEVEEAVQECRNAEEK---AKKAITDAAMMAEELKKE-QDTSAHLERMKKNMEQTikdlQHRLDEAEQIA----- 1800
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKleeAEKRAEKAEAEVAALNRRiQLLEEELERTEERLAEA----LEKLEEAEKAAdeser 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1801 -LKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTE--EDKKNLL--RLQDLVDKLQL---KVK 1872
Cdd:pfam00261 79 gRKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLEraEERAELAesKIVELEEELKVvgnNLK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1873 AYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKAQLARALYDNTAE 1939
Cdd:pfam00261 159 SLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISE 225
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1567-1882 |
1.21e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.17 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1567 EIERKLAEKDEEMEQAKRNHLRVVDSLQTsldAETRSRNEALRVKKKMEGDLNEMEIQLSQANRTASEAQKHLKIAQahl 1646
Cdd:pfam02029 10 ERRRRAREERRRQKEEEEPSGQVTESVEP---NEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEAL--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1647 kDTQLQMDDAvraNDDLKENIAIVERRNnllqaELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKM 1726
Cdd:pfam02029 84 -ERQKEFDPT---IADEKESVAERKENN-----EEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1727 ESDLTQLQSEVEEAVQECRNAEEKAK--KAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQH------------R 1792
Cdd:pfam02029 155 EGEEEEDKSEEAEEVPTENFAKEEVKdeKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVttkrrqgglsqsQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1793 LDEAEQIALKGGKKQLQKLEARVRELENElEAEQKRNA--------ESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLV 1864
Cdd:pfam02029 235 EREEEAEVFLEAEQKLEELRRRRQEKESE-EFEKLRQKqqeaelelEELKKKREERRKLLEEEEQRRKQEEAERKLREEE 313
|
330
....*....|....*...
gi 431907173 1865 DKLQLKVKAYKRQAEEAE 1882
Cdd:pfam02029 314 EKRRMKEEIERRRAEAAE 331
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
962-1172 |
1.30e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 962 TLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLE 1041
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1042 ------QEKKVRMD--------------LERA---KRKLEGDLKLTQEsimdLENDKLQLEEKLKKKEFDISQQNSKIED 1098
Cdd:COG3883 90 eraralYRSGGSVSyldvllgsesfsdfLDRLsalSKIADADADLLEE----LKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1099 EQALALQLQKKLKENQARIeelEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAE 1172
Cdd:COG3883 166 LEAAKAELEAQQAEQEALL---AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| SH3_MYO15 |
cd11884 |
Src Homology 3 domain of Myosin XV; This subfamily is composed of proteins with similarity to ... |
1930-1983 |
1.32e-04 |
|
Src Homology 3 domain of Myosin XV; This subfamily is composed of proteins with similarity to Myosin XVa. Myosin XVa is an unconventional myosin that is critical for the normal growth of mechanosensory stereocilia of inner ear hair cells. Mutations in the myosin XVa gene are associated with nonsyndromic hearing loss. Myosin XVa contains a unique N-terminal extension followed by a motor domain, light chain-binding IQ motifs, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain, and a PDZ domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.
Pssm-ID: 212817 [Multi-domain] Cd Length: 56 Bit Score: 41.54 E-value: 1.32e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGAggLD-GWCLCSLHGQQGIVPANRV 1983
Cdd:cd11884 2 VVAVRAYITRDQTLLSFHKGDVIKLLPKEGP--LDpGWLFGTLDGRSGAFPKEYV 54
|
|
| SH3_CIN85_3 |
cd12057 |
Third Src Homology 3 domain (SH3C) of Cbl-interacting protein of 85 kDa; CIN85, also called ... |
1931-1986 |
1.38e-04 |
|
Third Src Homology 3 domain (SH3C) of Cbl-interacting protein of 85 kDa; CIN85, also called SH3 domain-containing kinase-binding protein 1 (SH3KBP1) or CD2-binding protein 3 (CD2BP3) or Ruk, is an adaptor protein that is involved in the downregulation of receptor tyrosine kinases by facilitating endocytosis through interaction with endophilin-associated ubiquitin ligase Cbl proteins. It is also important in many other cellular processes including vesicle-mediated transport, cytoskeletal remodelling, apoptosis, cell adhesion and migration, and viral infection, among others. CIN85 exists as multiple variants from alternative splicing; the main variant contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the third SH3 domain (SH3C) of CIN85. SH3C has been shown to bind ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212990 [Multi-domain] Cd Length: 56 Bit Score: 41.81 E-value: 1.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGAGGldGWCLCSLHGQQGIVPANRVKLL 1986
Cdd:cd12057 3 KVLFPYEAQNEDELTIKEGDIVTLISKDCIDA--GWWEGELNGRRGVFPDNFVKLL 56
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
909-1114 |
1.49e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 46.55 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 909 QLIKNKIQLeakVKEMnerledeeemnAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKhatenkvKNLTEEMAGLD 988
Cdd:smart00787 113 LLMDKQFQL---VKTF-----------ARLEAKKMWYEWRMKLLEGLKEGLDENLEGLKEDY-------KLLMKELELLN 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 989 EIIAKLTKEKKALQEAHQQalddlqaeedkvntltkskvkLEQQVDDLEgSLEQEkkvrmDLERAKRKLegdlKLTQESI 1068
Cdd:smart00787 172 SIKPKLRDRKDALEEELRQ---------------------LKQLEDELE-DCDPT-----ELDRAKEKL----KKLLQEI 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 431907173 1069 MDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQ 1114
Cdd:smart00787 221 MIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCR 266
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1496-1794 |
1.50e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 46.45 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1496 RENKNLQEEISDLTEQLGEGGKNVHELekvrkqLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEK 1575
Cdd:pfam00038 25 QQNKLLETKISELRQKKGAEPSRLYSL------YEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1576 dEEMEQAKRNHLRVVDSL---QTSLDAETRSRNEALR-VKKKMEGDLNEMEIQLSQANRTAS-EAQKHLKIAQAhLKDTQ 1650
Cdd:pfam00038 99 -TSAENDLVGLRKDLDEAtlaRVDLEAKIESLKEELAfLKKNHEEEVRELQAQVSDTQVNVEmDAARKLDLTSA-LAEIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1651 LQMDDAVRAN-DDLKENiaiverrnnlLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESD 1729
Cdd:pfam00038 177 AQYEEIAAKNrEEAEEW----------YQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQ 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 431907173 1730 LtqlqSEVEEavqecrnaeekakkaitdaaMMAEELKKEQDTSAHLER----MKKNMEQTIKDLQHRLD 1794
Cdd:pfam00038 247 L----AETEE--------------------RYELQLADYQELISELEAelqeTRQEMARQLREYQELLN 291
|
|
| SH3_GRB2_N |
cd11946 |
N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical ... |
1930-1985 |
1.55e-04 |
|
N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. It is ubiquitously expressed in all tissues throughout development and is important in cell cycle progression, motility, morphogenesis, and angiogenesis. In lymphocytes, GRB2 is associated with antigen receptor signaling components. GRB2 contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. Its N-terminal SH3 domain binds to Sos and Sos-derived proline-rich peptides. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212879 [Multi-domain] Cd Length: 56 Bit Score: 41.55 E-value: 1.55e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGAgglDGWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd11946 3 AIAKYDFKATADDELSFKRGDILKVLNEECD---QNWYKAELNGKDGFIPKNYIEM 55
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1170-1372 |
1.56e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1170 EAEFQKMRRDLEEATLQHEATAAALRKKHADsVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTsnmEQIIKAKANLEK 1249
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAE-LEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1250 VSRTL--EDQANEYRTKLEEAQrSLNDFTTQQAKLQTENGELARQLEEKEALISQLTRGKLSYTQQTEDLKRQLEEEGKA 1327
Cdd:COG3883 91 RARALyrSGGSVSYLDVLLGSE-SFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 431907173 1328 KNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQ 1372
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1179-1535 |
1.61e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1179 DLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQA 1258
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1259 NEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLTRGKLSYTQQTEDLKRQLEEEGKAKNALAHALqsa 1338
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL--- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1339 rhdcdllreQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEA----KLQDAEEAVEAVNAKCSSLEKTK 1414
Cdd:COG4372 174 ---------QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAeellEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1415 HRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETF 1494
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 431907173 1495 KRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLE 1535
Cdd:COG4372 325 AKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
845-1000 |
1.63e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 845 AETEKEMANMKEEfgRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEErcdQLIKNKIQLEAKVKEM 924
Cdd:PRK12704 45 EEAKKEAEAIKKE--ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE---LLEKREEELEKKEKEL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 925 NERLEDEEEMNAELTAKKRKLEDE---CSELKRDiDDLELTLAKVEKE-KHATENKVKNLTEEmagldeiiAKLTKEKKA 1000
Cdd:PRK12704 120 EQKQQELEKKEEELEELIEEQLQElerISGLTAE-EAKEILLEKVEEEaRHEAAVLIKEIEEE--------AKEEADKKA 190
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1366-1582 |
1.73e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1366 ANSEVAQWRTKYETDAIQRTEELEEAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNaaaAALDKKQRNF 1445
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1446 DKIL-AEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEK 1524
Cdd:COG3883 89 GERArALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1525 VRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQA 1582
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
881-1043 |
1.73e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 45.13 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 881 SLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNERLEDE-EEMNAELTAKKRKLED---------ECS 950
Cdd:cd00176 37 ALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRwEELRELAEERRQRLEEaldlqqffrDAD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 951 ELKRDIDDLELTLAKVEKEKHATE-----NKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQalDDLQAEEDKVNTLTKS 1025
Cdd:cd00176 117 DLEQWLEEKEAALASEDLGKDLESveellKKHKELEEELEAHEPRLKSLNELAEELLEEGHP--DADEEIEEKLEELNER 194
|
170
....*....|....*...
gi 431907173 1026 KVKLEQQVDDLEGSLEQE 1043
Cdd:cd00176 195 WEELLELAEERQKKLEEA 212
|
|
| SH3_ARHGEF9_like |
cd11828 |
Src homology 3 domain of ARHGEF9-like Rho guanine nucleotide exchange factors; Members of this ... |
1929-1985 |
1.93e-04 |
|
Src homology 3 domain of ARHGEF9-like Rho guanine nucleotide exchange factors; Members of this family contain a SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains. They include the Rho guanine nucleotide exchange factors ARHGEF9, ASEF (also called ARHGEF4), ASEF2, and similar proteins. GEFs activate small GTPases by exchanging bound GDP for free GTP. ARHGEF9 specifically activates Cdc42, while both ASEF and ASEF2 can activate Rac1 and Cdc42. ARHGEF9 is highly expressed in the brain and it interacts with gephyrin, a postsynaptic protein associated with GABA and glycine receptors. ASEF plays a role in angiogenesis and cell migration. ASEF2 is important in cell migration and adhesion dynamics. ASEF exists in an autoinhibited form and is activated upon binding of the tumor suppressor APC (adenomatous polyposis coli), leading to the activation of Rac1 or Cdc42. In its autoinhibited form, the SH3 domain of ASEF forms an extensive interface with the DH and PH domains, blocking the Rac binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212762 [Multi-domain] Cd Length: 53 Bit Score: 41.21 E-value: 1.93e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1929 LARALYDNTAESPQELSFRRGDVLRVLQREGAggldGWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd11828 1 LAEALWDHVTMDPEELGFKAGDVIEVLDMSDK----DWWWGSIRDEEGWFPASFVRL 53
|
|
| SH3_Noxa1_C |
cd12047 |
C-terminal Src Homology 3 domain of NADPH oxidase activator 1; Noxa1 is a homolog of p67phox ... |
1931-1979 |
1.94e-04 |
|
C-terminal Src Homology 3 domain of NADPH oxidase activator 1; Noxa1 is a homolog of p67phox and is a cytosolic subunit of the nonphagocytic NADPH oxidase complex Nox1, which catalyzes the transfer of electrons from NADPH to molecular oxygen to form superoxide. Noxa1 is co-expressed with Nox1 in colon, stomach, uterus, prostate, and vascular smooth muscle cells, consistent with its regulatory role. It does not interact with p40phox, unlike p67phox, making Nox1 activity independent of p40phox, unlike Nox2. Noxa1 contains TPR, PB1, and C-terminal SH3 domains, but lacks the central SH3 domain that is present in p67phox. The TPR domain binds activated GTP-bound Rac. The C-terminal SH3 domain binds the polyproline motif found at the C-terminus of Noxo1, a homolog of p47phox. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212980 Cd Length: 53 Bit Score: 41.34 E-value: 1.94e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGAGGLDGWClcslHGQQGIVP 1979
Cdd:cd12047 3 VAQHDYSAQGPEDLEFSQGDTIDILSEVNQEWLEGHC----DGRIGIFP 47
|
|
| SH3_GRAP_N |
cd11948 |
N-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor ... |
1930-1985 |
2.04e-04 |
|
N-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor protein that is highly expressed in lymphoid tissues. It acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. It has been identified as a regulator of TGFbeta signaling in diabetic kidney tubules and may have a role in the pathogenesis of the disease. GRAP contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The N-terminal SH3 domain of the related protein GRB2 binds to Sos and Sos-derived proline-rich peptides. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212881 [Multi-domain] Cd Length: 54 Bit Score: 41.34 E-value: 2.04e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGAgglDGWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd11948 2 AVALYSFQATESDELPFQKGDILKILNMEDD---QNWYKAELQGREGYIPKNYIKV 54
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1591-1759 |
2.15e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1591 DSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMDdAVRANDDLKEniaiv 1670
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG-NVRNNKEYEA----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1671 errnnlLQAELEELravveqtERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEK 1750
Cdd:COG1579 94 ------LQKEIESL-------KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
....*....
gi 431907173 1751 AKKAITDAA 1759
Cdd:COG1579 161 LEAEREELA 169
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
837-1085 |
2.25e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 45.96 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 837 KIKPLLKSAETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAeERCDQLIKNKIQ 916
Cdd:pfam15905 68 NLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLEL-TRVNELLKAKFS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 917 LEAKVKEMN----ERLEDEEEMNA---ELTAKKRKLEDECSELKRD-------IDDLELTLAKVEKEKHATENKVKNLTE 982
Cdd:pfam15905 147 EDGTQKKMSslsmELMKLRNKLEAkmkEVMAKQEGMEGKLQVTQKNlehskgkVAQLEEKLVSTEKEKIEEKSETEKLLE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 983 EMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLK 1062
Cdd:pfam15905 227 YITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLN 306
|
250 260
....*....|....*....|...
gi 431907173 1063 LTQESIMDLENDKLQLEEKLKKK 1085
Cdd:pfam15905 307 AELEELKEKLTLEEQEHQKLQQK 329
|
|
| SH3_Myosin-I_fungi |
cd11858 |
Src homology 3 domain of Type I fungal Myosins; Type I myosins (myosin-I) are actin-dependent ... |
1930-1985 |
2.54e-04 |
|
Src homology 3 domain of Type I fungal Myosins; Type I myosins (myosin-I) are actin-dependent motors in endocytic actin structures and actin patches. They play roles in membrane traffic in endocytic and secretory pathways, cell motility, and mechanosensing. Saccharomyces cerevisiae has two myosins-I, Myo3 and Myo5, which are involved in endocytosis and the polarization of the actin cytoskeleton. Myosin-I contains an N-terminal actin-activated ATPase, a phospholipid-binding TH1 (tail homology 1) domain, and a C-terminal extension which includes an F-actin-binding TH2 domain, an SH3 domain, and an acidic peptide that participates in activating the Arp2/3complex. The SH3 domain of myosin-I is required for myosin-I-induced actin polymerization. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212792 [Multi-domain] Cd Length: 55 Bit Score: 40.83 E-value: 2.54e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSLHGQ--QGIVPANRVKL 1985
Cdd:cd11858 2 YKALYDFAGSVANELSLKKDDIVYIVQKED----NGWWLAKKLDEskEGWVPAAYLEE 55
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1737-1953 |
2.61e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.39 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1737 VEEAVQECRNAEEkakkaitdaammAEELKKEQDTSAHLERMKKNMEQTIKDLQhrldeaeqialkggkKQLQKLEARVR 1816
Cdd:COG2433 378 IEEALEELIEKEL------------PEEEPEAEREKEHEERELTEEEEEIRRLE---------------EQVERLEAEVE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1817 ELENELEAEQKRNAES---VKGMRKSERR-------IKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRqAEEAEEQAN 1886
Cdd:COG2433 431 ELEAELEEKDERIERLereLSEARSEERReirkdreISRLDREIERLERELEEERERIEELKRKLERLKE-LWKLEHSGE 509
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1887 T----NLSKFRKvqHELDEAEERADIAESQVNKLRAKSrdiGAKAQLARALYDNTAE---SPQELSFRRGDVLR 1953
Cdd:COG2433 510 LvpvkVVEKFTK--EAIRRLEEEYGLKEGDVVYLRDAS---GAGRSTAELLAEAGPRaviVPGELSEAADEVLF 578
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1390-1584 |
2.64e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1390 EAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMvdvERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKE 1469
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELN---EEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1470 ARSL------STELFKLKNA--YEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALE 1541
Cdd:COG3883 92 ARALyrsggsVSYLDVLLGSesFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 431907173 1542 EAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKR 1584
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1601-1855 |
2.66e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 45.57 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1601 TRSRNEALRVKKKMEGDLNEM------EIQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKENIAIVERRN 1674
Cdd:pfam15905 52 TARKVKSLELKKKSQKNLKESkdqkelEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1675 NLLQAELEELRAVVEQTERSRKLA--EQELIETSERvqlLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAK 1752
Cdd:pfam15905 132 LELTRVNELLKAKFSEDGTQKKMSslSMELMKLRNK---LEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1753 -----------------KAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAlkggKKQLQKLEARV 1815
Cdd:pfam15905 209 stekekieeksetekllEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQEL----SKQIKDLNEKC 284
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 431907173 1816 RELENELEAEQKRNAESVKGMRKSERRIKE-LTYQTEEDKK 1855
Cdd:pfam15905 285 KLLESEKEELLREYEEKEQTLNAELEELKEkLTLEEQEHQK 325
|
|
| SH3_Lasp1_C |
cd11934 |
C-terminal Src Homology 3 domain of LIM and SH3 domain protein 1; Lasp1 is a cytoplasmic ... |
1931-1984 |
2.67e-04 |
|
C-terminal Src Homology 3 domain of LIM and SH3 domain protein 1; Lasp1 is a cytoplasmic protein that binds focal adhesion proteins and is involved in cell signaling, migration, and proliferation. It is overexpressed in several cancer cells including breast, ovarian, bladder, and liver. In cancer cells, it can be found in the nucleus; its degree of nuclear localization correlates with tumor size and poor prognosis. Lasp1 is a 36kD protein containing an N-terminal LIM domain, two nebulin repeats, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212867 [Multi-domain] Cd Length: 59 Bit Score: 41.14 E-value: 2.67e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSLH--GQQGIVPANRVK 1984
Cdd:cd11934 6 RAVYDYNAADEDEVSFQDGDTIVNVQQID----DGWMYGTVErtGDTGMLPANYVE 57
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1489-1931 |
2.80e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 46.36 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1489 EHLETFKRENKNLQ---EEISDLTEQLGeggknvHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILR-AQLEFNQI 1564
Cdd:NF041483 15 DHLSRFEAEMDRLKterEKAVQHAEDLG------YQVEVLRAKLHEARRSLASRPAYDGADIGYQAEQLLRnAQIQADQL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1565 KAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEAL-----RVKKKMEGDLNEmEIQLSQANRTASEAQkhl 1639
Cdd:NF041483 89 RADAERELRDARAQTQRILQEHAEHQARLQAELHTEAVQRRQQLdqelaERRQTVESHVNE-NVAWAEQLRARTESQ--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1640 kiAQAHLKDTQLQMDDAVRANDDLKENIAIVERRNnlLQAELEELRAVVEQT-ERSRKLAEQELIETSERVQ-------L 1711
Cdd:NF041483 165 --ARRLLDESRAEAEQALAAARAEAERLAEEARQR--LGSEAESARAEAEAIlRRARKDAERLLNAASTQAQeatdhaeQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1712 LHSQNTSLINQKKKMESDLT----QLQSEVEEAVQECRNAEEKAKKAITDAA---MMAEELKKEQDTSAHLERMKKNMEQ 1784
Cdd:NF041483 241 LRSSTAAESDQARRQAAELSraaeQRMQEAEEALREARAEAEKVVAEAKEAAakqLASAESANEQRTRTAKEEIARLVGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1785 TIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELENELEAEqkrnaESVKGMRKSERRIKELTYQTEEDKKNllrlqdlv 1864
Cdd:NF041483 321 ATKEAEALKAEAEQ-ALADARAEAEKLVAEAAEKARTVAAE-----DTAAQLAKAARTAEEVLTKASEDAKA-------- 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1865 dklqlKVKAYKRQAEEAEEQANTNLSKFRKVQHelDEAEERADIAESQVNKLRAKSRDIGAKAQLAR 1931
Cdd:NF041483 387 -----TTRAAAEEAERIRREAEAEADRLRGEAA--DQAEQLKGAAKDDTKEYRAKTVELQEEARRLR 446
|
|
| SH3_RIM-BP_2 |
cd12012 |
Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ... |
1932-1984 |
2.86e-04 |
|
Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212945 Cd Length: 62 Bit Score: 41.12 E-value: 2.86e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 431907173 1932 ALYDNTAE--SP------QELSFRRGDVLRVLqreGAGGLDGWCLCSLHGQQGIVPANRVK 1984
Cdd:cd12012 4 ALFDYDPLtmSPnpdaaeEELPFKEGQLIKVY---GDKDADGFYLGEINGRRGLVPCNMVS 61
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1134-1398 |
2.89e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.27 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1134 VEKLRSDLSRELEEISERLEEAggatsvQIEMNKKREAEFQKMRRDLEEATLQHEAT---AAALRKKHADSVAELGEQID 1210
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQE------RLRQEKEEKAREVERRRKLEEAEKARQAEmdrQAAIYAEQERMAMERERELE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1211 NLQRVKQKLEKEK---SEFKLELDDVTSNMEQIIKAKANLEKVSRTLEdQANEYRTKLEEAQRSLNDFTTQQAKLQTENg 1287
Cdd:pfam17380 352 RIRQEERKRELERirqEEIAMEISRMRELERLQMERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQIRAEQ- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1288 ELARQL------EEKEALISQLTRGKLSYTQQTEDLkRQLEEEGKAKNALAHALQSARHDCD-----LLREQYEEETEAK 1356
Cdd:pfam17380 430 EEARQRevrrleEERAREMERVRLEEQERQQQVERL-RQQEEERKRKKLELEKEKRDRKRAEeqrrkILEKELEERKQAM 508
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 431907173 1357 AELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKLQDAEE 1398
Cdd:pfam17380 509 IEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEE 550
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1521-1740 |
2.97e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 44.98 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1521 ELEKvRKQLEAEKLELQSALEEAEASLEHEEgkilraqlEFNQIKAEIERKLAEKDEEMEQAKRNhlrvVDSLQTSLDAE 1600
Cdd:pfam12795 4 ELEK-AKLDEAAKKKLLQDLQQALSLLDKID--------ASKQRAAAYQKALDDAPAELRELRQE----LAALQAKAEAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1601 TRSRNEALRVK------KKMEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDA-VRANDDLKENIAIVERR 1673
Cdd:pfam12795 71 PKEILASLSLEeleqrlLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIrNRLNGPAPPGEPLSEAQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1674 NNLLQAELEELRAVVEQTERS-------RKLAEQELIETSERVQLLHSQNT---SLINQKKKMESDLTQLQSEVEEA 1740
Cdd:pfam12795 151 RWALQAELAALKAQIDMLEQEllsnnnrQDLLKARRDLLTLRIQRLEQQLQalqELLNEKRLQEAEQAVAQTEQLAE 227
|
|
| SH3_RUSC1 |
cd11958 |
Src homology 3 domain of RUN and SH3 domain-containing protein 1; RUSC1, also called NESCA ... |
1931-1979 |
3.08e-04 |
|
Src homology 3 domain of RUN and SH3 domain-containing protein 1; RUSC1, also called NESCA (New molecule containing SH3 at the carboxy-terminus), is highly expressed in the brain and is translocated to the nuclear membrane from the cytoplasm upon stimulation with neurotrophin. It plays a role in facilitating neurotrophin-dependent neurite outgrowth. It also interacts with NEMO (or IKKgamma) and may function in NEMO-mediated activation of NF-kB. RUSC proteins are adaptor proteins consisting of RUN, leucine zipper, and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212891 [Multi-domain] Cd Length: 51 Bit Score: 40.59 E-value: 3.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 431907173 1931 RALYDNTAeSPQELSFRRGDVLRVLqregaGGLD-GWCLCSLHGQQGIVP 1979
Cdd:cd11958 3 RALCDHAG-SESQLSFRKGEELQVL-----GTVDeDWIRCRRGDREGLVP 46
|
|
| SH3_Nebulette_C |
cd11935 |
C-terminal Src Homology 3 domain of Nebulette and LIM-nebulette (or Lasp2); Nebulette is a ... |
1931-1986 |
3.15e-04 |
|
C-terminal Src Homology 3 domain of Nebulette and LIM-nebulette (or Lasp2); Nebulette is a cardiac-specific protein that localizes to the Z-disc. It interacts with tropomyosin and is important in stabilizing actin thin filaments in cardiac muscles. Polymorphisms in the nebulette gene are associated with dilated cardiomyopathy, with some mutations resulting in severe heart failure. Nebulette is a 107kD protein that contains an N-terminal acidic region, multiple nebulin repeats, and a C-terminal SH3 domain. LIM-nebulette, also called Lasp2 (LIM and SH3 domain protein 2), is an alternatively spliced variant of nebulette. Although it shares a gene with nebulette, Lasp2 is not transcribed from a muscle-specific promoter, giving rise to its multiple tissue expression pattern with highest amounts in the brain. It can crosslink actin filaments and it affects cell spreading. Lasp2 is a 34kD protein containing an N-terminal LIM domain, three nebulin repeats, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212868 [Multi-domain] Cd Length: 58 Bit Score: 40.76 E-value: 3.15e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSLH--GQQGIVPANRVKLL 1986
Cdd:cd11935 4 RAMYDYSAQDEDEVSFRDGDYIVNVQPID----EGWMYGTVQrtGRTGMLPANYIEFV 57
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
841-1080 |
3.27e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.32 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 841 LLKSAETEKEMANMKEEFGRLKETLEKSEARRKELEekmvsllQEKNDLqlqvqaeQDNLNDAEERCDQLIKNKIQLEAK 920
Cdd:pfam01576 825 LAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQ-------QERDEL-------ADEIASGASGKSALQDEKRRLEAR 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 921 VKEMNERLEdEEEMNAELTAKK-RKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLteemagldeiiakltkeKK 999
Cdd:pfam01576 891 IAQLEEELE-EEQSNTELLNDRlRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKEL-----------------KA 952
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1000 ALQEAHQQAlddlqaeedkvntltKSKVK-----LEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKltqESIMDLEND 1074
Cdd:pfam01576 953 KLQEMEGTV---------------KSKFKssiaaLEAKIAQLEEQLEQESRERQAANKLVRRTEKKLK---EVLLQVEDE 1014
|
....*.
gi 431907173 1075 KLQLEE 1080
Cdd:pfam01576 1015 RRHADQ 1020
|
|
| ycf1 |
CHL00204 |
Ycf1; Provisional |
830-999 |
3.39e-04 |
|
Ycf1; Provisional
Pssm-ID: 214395 [Multi-domain] Cd Length: 1832 Bit Score: 46.25 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 830 PW--MKLYFKIKPLLKSAETEKE------MANMKEE--FGRLKETLEKSEARRKELEEKMVSLlQEKNDLQLQVQAEQDN 899
Cdd:CHL00204 867 PWhrSKLRSSHKDRMKKKKKKKNdfcfltVWGMETElpFGSPRKRPSFFEPIFKELKKKIRKF-KKKYFLVLKILKERTK 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 900 --LNDAEERCDQLIKNKIQLEAKVKEMNERledeeemNAELTAKKRKLeDECSELKRDIDDL-------ELTLAKVEKE- 969
Cdd:CHL00204 946 lfLKVSKETKKWIIKSFLFLKRIIKELSKR-------NPILLFGLREI-YELNETKKEKDSIisnqmihESSVQIRSMEw 1017
|
170 180 190
....*....|....*....|....*....|..
gi 431907173 970 --KHATENKVKNLTEEMAGLDEIIAKLTKEKK 999
Cdd:CHL00204 1018 tnSSLTEKKIKDLTDRTKTIRNQIEKITKEKK 1049
|
|
| SH3_VAV_2 |
cd11830 |
C-terminal (or second) Src homology 3 domain of VAV proteins; VAV proteins function both as ... |
1930-1984 |
3.48e-04 |
|
C-terminal (or second) Src homology 3 domain of VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and scaffold proteins and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The SH3 domain of VAV is involved in the localization of proteins to specific sites within the cell, by interacting with proline-rich sequences within target proteins. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212764 [Multi-domain] Cd Length: 54 Bit Score: 40.69 E-value: 3.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGAgglDGWCLCSLHGQQGIVPANRVK 1984
Cdd:cd11830 2 AKARYDFCARDMRELSLKEGDVVKIYNKKGQ---QGWWRGEINGRIGWFPSTYVE 53
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
837-1093 |
3.48e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 837 KIKPLLKSAETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQ 916
Cdd:PRK02224 497 RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 917 LEAKVKEMNERLEDEEEMnAELTAKKRKLEDECSELKRDIDDleltLAKVEKEKHATenkvknLTEEMAGLDEIIAKLTK 996
Cdd:PRK02224 577 LNSKLAELKERIESLERI-RTLLAAIADAEDEIERLREKREA----LAELNDERRER------LAEKRERKRELEAEFDE 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 997 EK-KALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQekkvrmdLERAKRKLEgDLKLTQESIMDLENDK 1075
Cdd:PRK02224 646 ARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE-------LEELRERRE-ALENRVEALEALYDEA 717
|
250
....*....|....*...
gi 431907173 1076 LQLEEKLKKKEFDISQQN 1093
Cdd:PRK02224 718 EELESMYGDLRAELRQRN 735
|
|
| SH3_Nephrocystin |
cd11770 |
Src Homology 3 domain of Nephrocystin (or Nephrocystin-1); Nephrocystin contains an SH3 domain ... |
1931-1985 |
3.56e-04 |
|
Src Homology 3 domain of Nephrocystin (or Nephrocystin-1); Nephrocystin contains an SH3 domain involved in signaling pathways that regulate cell adhesion and cytoskeletal organization. It is a protein that in humans is associated with juvenile nephronophthisis, an inherited kidney disease characterized by renal fibrosis that lead to chronic renal failure in children. It is localized in cell-cell junctions in renal duct cells, and is known to interact with Ack1, an activated Cdc42-associated kinase. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212704 [Multi-domain] Cd Length: 54 Bit Score: 40.37 E-value: 3.56e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREgaggLDGWCLC-SLHGQQGIVPANRVKL 1985
Cdd:cd11770 3 EALSDFQAEQEGDLSFKKGEVLRIISKR----ADGWWLAeNSKGNRGLVPKTYLKV 54
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
884-1349 |
3.66e-04 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 45.62 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 884 QEKNDLQLQV-QAEQDNLNDAEERCDQLIKnkiQLEAKVKEM----NERLEDEEEmnaELTAKKRKLEDECSELKRDIDD 958
Cdd:pfam03148 2 RANNQELYREaEAQRNDAERLRQESRRLRN---ETDAKTKWDqydsNRRLGERIQ---DITFWKSELEKELEELDEEIEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 959 LELTLAKVEKEKHATENKVkNLTEEMAGL-----------DEIIAKLTKEKKALQEAHQQalddlqaeedkvntltkskv 1027
Cdd:pfam03148 76 LLEEKRRLEKALEALEEPL-HIAQECLTLrekrqgidlvhDEVEKELLKEVELIEGIQEL-------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1028 kLEQQVDDLEgslEQEKkvrmDLERAKRKLEGDLKLTQESimdLENDKLQLEekLKKKEFDISQQNS--KIEDEQALALQ 1105
Cdd:pfam03148 135 -LQRTLEQAW---EQLR----LLRAARHKLEKDLSDKKEA---LEIDEKCLS--LNNTSPNISYKPGptRIPPNSSTPEE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1106 LQKKLKENQARIEEleeeleaertARAKVEKLRSDLSRELEeiserleeaggatsvqiemnkkreaefqKMRRDLEEatl 1185
Cdd:pfam03148 202 WEKFTQDNIERAEK----------ERAASAQLRELIDSILE----------------------------QTANDLRA--- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1186 QHEATAAALRKKhadsvaelgeqIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLE---KVSRT-LEDQAneY 1261
Cdd:pfam03148 241 QADAVNFALRKR-----------IEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEaplKLAQTrLENRT--Y 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1262 RTKLE----EAQRSLNDfttqqaklqtengELARQLEEKEALISQLTRGKLSYtQQTEDLKRQLEEEGKAKNalaHALQS 1337
Cdd:pfam03148 308 RPNVElcrdEAQYGLVD-------------EVKELEETIEALKQKLAEAEASL-QALERTRLRLEEDIAVKA---NSLFI 370
|
490
....*....|..
gi 431907173 1338 ARHDCDLLREQY 1349
Cdd:pfam03148 371 DREKCMGLRKRL 382
|
|
| SH3_PACSIN3 |
cd11997 |
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 3 (PACSIN3); ... |
1931-1984 |
3.72e-04 |
|
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 3 (PACSIN3); PACSIN 3 or Syndapin III (Synaptic dynamin-associated protein III) is expressed ubiquitously and regulates glucose uptake in adipocytes through its role in GLUT1 trafficking. It also modulates the subcellular localization and stimulus-specific function of the cation channel TRPV4. PACSINs act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212930 [Multi-domain] Cd Length: 56 Bit Score: 40.33 E-value: 3.72e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGAgglDGWCLCSL-HGQQGIVPANRVK 1984
Cdd:cd11997 5 RALYDYTGQEADELSFKAGEELLKIGEEDE---QGWCKGRLlSGRIGLYPANYVE 56
|
|
| SH3_DNMBP_N3 |
cd11796 |
Third N-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba; DNMBP or ... |
1930-1983 |
3.75e-04 |
|
Third N-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba; DNMBP or Tuba is a cdc42-specific guanine nucleotide exchange factor (GEF) that contains four N-terminal SH3 domains, a central RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. It provides a functional link between dynamin and key regulatory proteins of the actin cytoskeleton. It plays an important role in regulating cell junction configuration. The four N-terminal SH3 domains of DNMBP binds the GTPase dynamin, which plays an important role in the fission of endocytic vesicles. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212730 Cd Length: 51 Bit Score: 40.42 E-value: 3.75e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSLHGQQGIVPANRV 1983
Cdd:cd11796 2 ARVLQDLSAQLDEELDLREGDVVTITGILD----KGWFRGELNGRRGIFPEGFV 51
|
|
| SH3_D21-like |
cd12142 |
Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins; ... |
1931-1983 |
3.81e-04 |
|
Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins; N-terminal SH3 domain of the uncharacterized protein SH3 domain-containing protein 21, and similar uncharacterized domains, it belongs to the CD2AP-like_3 subfamily of proteins. The CD2AP-like_3 subfamily is composed of the third SH3 domain (SH3C) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3C of both proteins have been shown to bind to ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 213018 [Multi-domain] Cd Length: 55 Bit Score: 40.53 E-value: 3.81e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREgaGGLDGWCLCSLHGQQGIVPANRV 1983
Cdd:cd12142 3 RVLFDYNPVAPDELALKKGDVIEVISKE--TEDEGWWEGELNGRRGFFPDNFV 53
|
|
| SH3_Abl |
cd11850 |
Src homology 3 domain of the Protein Tyrosine Kinase, Abelson kinase; Abl (or c-Abl) is a ... |
1932-1981 |
3.90e-04 |
|
Src homology 3 domain of the Protein Tyrosine Kinase, Abelson kinase; Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212784 Cd Length: 56 Bit Score: 40.47 E-value: 3.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQREGAGgldGWC--LCSLHGQQGIVPAN 1981
Cdd:cd11850 4 ALYDFVASGENQLSIKKGEQLRVLGYNKNG---EWCeaESKSTGGQGWVPSN 52
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1767-1928 |
4.00e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.89 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1767 KEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGK------KQLQKLEARVRELENELEAEQKRNAESVKGMRKSE 1840
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRqldresDRNQELQKRIRLLEKREAEAEEALREQAELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1841 RRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKS 1920
Cdd:pfam05557 83 KYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQ 162
|
....*...
gi 431907173 1921 RDIGAKAQ 1928
Cdd:pfam05557 163 SSLAEAEQ 170
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1234-1454 |
4.09e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 45.05 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1234 TSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQ----QAKLQTENGELARQLEEKEALISQltrgkls 1309
Cdd:cd22656 106 ATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQtekdQTALETLEKALKDLLTDEGGAIAR------- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1310 ytQQTEDLKRQLEeegKAKNALAHALQSARHDcdlLREQYEEETEAKAELQRVLSKANSEVAQwrtkyeTDAIqrteele 1389
Cdd:cd22656 179 --KEIKDLQKELE---KLNEEYAAKLKAKIDE---LKALIADDEAKLAAALRLIADLTAADTD------LDNL------- 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1390 eakLQDAEEAVEAVNAkcssLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQ 1454
Cdd:cd22656 238 ---LALIGPAIPALEK----LQGAWQAIATDLDSLKDLLEDDISKIPAAILAKLELEKAIEKWNE 295
|
|
| SH3_Sla1p_2 |
cd11774 |
Second Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates ... |
1930-1983 |
4.13e-04 |
|
Second Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates endocytosis by playing a role as an adaptor protein in coupling components of the actin cytoskeleton to the endocytic machinery. It interacts with Abp1p, Las17p and Pan1p, which are activator proteins of actin-related protein 2/3 (Arp2/3). Sla1p contains multiple domains including three SH3 domains, a SAM (sterile alpha motif) domain, and a Sla1 homology domain 1 (SHD1), which binds to the NPFXD motif that is found in many integral membrane proteins such as the Golgi-localized Arf-binding protein Lsb5p and the P4-ATPases, Drs2p and Dnf1p. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212708 [Multi-domain] Cd Length: 52 Bit Score: 40.14 E-value: 4.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLqregaGGLDG-WCLCSLHGQQ-GIVPANRV 1983
Cdd:cd11774 2 AKALYDYDKQTEEELSFNEGDTLDVY-----DDSDSdWILVGFNGTQfGFVPANYI 52
|
|
| SH3_HS1 |
cd12073 |
Src homology 3 domain of Hematopoietic lineage cell-specific protein 1; HS1, also called HCLS1 ... |
1930-1986 |
4.37e-04 |
|
Src homology 3 domain of Hematopoietic lineage cell-specific protein 1; HS1, also called HCLS1 (hematopoietic cell-specific Lyn substrate 1), is a cortactin homolog expressed specifically in hematopoietic cells. It is an actin regulatory protein that binds the Arp2/3 complex and stabilizes branched actin filaments. It is required for cell spreading and signaling in lymphocytes. It regulates cytoskeletal remodeling that controls lymphocyte trafficking, and it also affects tissue invasion and infiltration of leukemic B cells. Like cortactin, HS1 contains an N-terminal acidic domain, several copies of a repeat domain found in cortactin and HS1, a proline-rich region, and a C-terminal SH3 domain. The N-terminal region binds the Arp2/3 complex and F-actin, while the C-terminal region acts as an adaptor or scaffold that can connect varied proteins that bind the SH3 domain within the actin network. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 213006 [Multi-domain] Cd Length: 55 Bit Score: 40.20 E-value: 4.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGAGGLDGWClcslHGQQGIVPANRVKLL 1986
Cdd:cd12073 3 AVALYDYQGEGDDEISFDPQETITDIEMVDEGWWKGTC----HGHRGLFPANYVELL 55
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
832-991 |
4.42e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 45.01 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 832 MKLYFKIKPLL--KSAETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQ 909
Cdd:smart00787 139 MKLLEGLKEGLdeNLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQ 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 910 LIKNKIQleaKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKR-----------DIDDLELTLAKVEKEKHATENKVK 978
Cdd:smart00787 219 EIMIKVK---KLEELEEELQELESKIEDLTNKKSELNTEIAEAEKkleqcrgftfkEIEKLKEQLKLLQSLTGWKITKLS 295
|
170
....*....|...
gi 431907173 979 NLTEEMAGLDEII 991
Cdd:smart00787 296 GNTLSMTYDREIN 308
|
|
| SH3_Intersectin_1 |
cd11836 |
First Src homology 3 domain (or SH3A) of Intersectin; Intersectins (ITSNs) are adaptor ... |
1931-1983 |
4.44e-04 |
|
First Src homology 3 domain (or SH3A) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The first SH3 domain (or SH3A) of ITSN1 has been shown to bind many proteins including Sos1, dynamin1/2, CIN85, c-Cbl, PI3K-C2, SHIP2, N-WASP, and CdGAP, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212770 [Multi-domain] Cd Length: 55 Bit Score: 40.03 E-value: 4.44e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGAGglDGWCLCSLHGQQGIVPANRV 1983
Cdd:cd11836 3 RALYAFEARNPDEISFQPGDIIQVDESQVAE--PGWLAGELKGKTGWFPANYV 53
|
|
| PRK15374 |
PRK15374 |
type III secretion system needle tip complex protein SipB; |
1145-1363 |
4.47e-04 |
|
type III secretion system needle tip complex protein SipB;
Pssm-ID: 185272 [Multi-domain] Cd Length: 593 Bit Score: 45.72 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1145 LEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALrkKHADSVAE-LGEQIDNLQRVKQKLEKEK 1223
Cdd:PRK15374 101 LSQLESRLAVWQAMIESQKEMGIQVSKEFQTALGEAQEATDLYEASIKKT--DTAKSVYDaAEKKLTQAQNKLQSLDPAD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1224 SEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFttqQAKLQTENGELARQLEEKEalISQL 1303
Cdd:PRK15374 179 PGYAQAEAAVEQAGKEATEAKEALDKATDATVKAGTDAKAKAEKADNILTKF---QGTANAASQNQVSQGEQDN--LSNV 253
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 431907173 1304 TRGKLSYTQQTEDLKRQLEEEGKAKNALAHALQSARH-DCDLLREQYEEETEAKAELQRVL 1363
Cdd:PRK15374 254 ARLTMLMAMFIEIVGKNTEESLQNDLALFNALQEGRQaEMEKKSAEFQEETRKAEETNRIM 314
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
861-997 |
4.62e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.62 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 861 LKETLEKSEARRKELEEKmvsllqeknDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTA 940
Cdd:COG2433 378 IEEALEELIEKELPEEEP---------EAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 941 KKRKL----------EDECSELKRDIDDLELTLAKVEKEKHATENKVKNLtEEMAGLDE--------IIAKLTKE 997
Cdd:COG2433 449 ELSEArseerreirkDREISRLDREIERLERELEEERERIEELKRKLERL-KELWKLEHsgelvpvkVVEKFTKE 522
|
|
| SH3_Abp1_eu |
cd11960 |
Src homology 3 domain of eumetazoan Actin-binding protein 1; Abp1, also called drebrin-like ... |
1930-1985 |
4.73e-04 |
|
Src homology 3 domain of eumetazoan Actin-binding protein 1; Abp1, also called drebrin-like protein, is an adaptor protein that functions in receptor-mediated endocytosis and vesicle trafficking. It contains an N-terminal actin-binding module, the actin-depolymerizing factor (ADF) homology domain, a helical domain, and a C-terminal SH3 domain. Mammalian Abp1, unlike yeast Abp1, does not contain an acidic domain that interacts with the Arp2/3 complex. It regulates actin dynamics indirectly by interacting with dynamin and WASP family proteins. Abp1 deficiency causes abnormal organ structure and function of the spleen, heart, and lung of mice. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212893 [Multi-domain] Cd Length: 54 Bit Score: 40.08 E-value: 4.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGAGgldGWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd11960 2 ARALYDYQAADDTEISFDPGDIITDIEQIDEG---WWRGTGPDGTYGLFPANYVEL 54
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
866-1024 |
4.83e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 44.67 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 866 EKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDqliKNKIQLEAKVKEMNERLEDEEEMN-----AELTA 940
Cdd:cd22656 110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTE---KDQTALETLEKALKDLLTDEGGAIarkeiKDLQK 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 941 KKRKLEDEC-SELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQ--EAHQQAL-DDLQAEE 1016
Cdd:cd22656 187 ELEKLNEEYaAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEklQGAWQAIaTDLDSLK 266
|
....*...
gi 431907173 1017 DKVNTLTK 1024
Cdd:cd22656 267 DLLEDDIS 274
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1653-1919 |
4.99e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 45.70 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1653 MDDAVRANDDLKENIAIVERRNNLLQAELE----------ELRAVVEQTERSRK---LAEQELIetSERVQLLHSQ---- 1715
Cdd:PLN03188 928 MDGVLSKEDFLEEELASLMHEHKLLKEKYEnhpevlrtkiELKRVQDELEHYRNfydMGEREVL--LEEIQDLRSQlqyy 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1716 -NTSLINQKKK---------MESDLTQLQSEVEEAVQECrnAEEKAKK-------AITDAAMMAEELKKEQDTSAHLERM 1778
Cdd:PLN03188 1006 iDSSLPSARKRnsllkltysCEPSQAPPLNTIPESTDES--PEKKLEQerlrwteAESKWISLAEELRTELDASRALAEK 1083
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1779 KKNMEQTIKDLQHRLDEAEQIALKGGKKQLQK----------LEARVRELENELEAEQKrnAESVKGMRKSERRI----- 1843
Cdd:PLN03188 1084 QKHELDTEKRCAEELKEAMQMAMEGHARMLEQyadleekhiqLLARHRRIQEGIDDVKK--AAARAGVRGAESKFinala 1161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1844 KELTYQTEEDKKNLLRLQDLVDKLQLKVkaykRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAE-------SQVNKL 1916
Cdd:PLN03188 1162 AEISALKVEREKERRYLRDENKSLQAQL----RDTAEAVQAAGELLVRLKEAEEALTVAQKRAMDAEqeaaeayKQIDKL 1237
|
...
gi 431907173 1917 RAK 1919
Cdd:PLN03188 1238 KRK 1240
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1129-1295 |
5.13e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1129 TARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGE- 1207
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAAL-----------EARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1208 -----------QIDNLQRVKQKLEKEKSEFklelddvtsnMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFT 1276
Cdd:COG1579 86 rnnkeyealqkEIESLKRRISDLEDEILEL----------MERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
170
....*....|....*....
gi 431907173 1277 TQQAKLQTENGELARQLEE 1295
Cdd:COG1579 156 AELEELEAEREELAAKIPP 174
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1019-1285 |
5.35e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1019 VNTLTKSKVK--LEQQVDDLEGSL----EQEKKVRMDLERAKRKLEgDLKlTQESIMDLENDKLQLEEKLKkkefdisqq 1092
Cdd:COG3206 154 ANALAEAYLEqnLELRREEARKALefleEQLPELRKELEEAEAALE-EFR-QKNGLVDLSEEAKLLLQQLS--------- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1093 nskiedeqalalQLQKKLKENQARIeeleeeleaeRTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnkkreaE 1172
Cdd:COG3206 223 ------------ELESQLAEARAEL----------AEAEARLAALRAQLGSGPDALPELLQSP----------------V 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1173 FQKMRRDLEEATLQHEATAAALRKKHADsVAELGEQIDNL-QRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVS 1251
Cdd:COG3206 265 IQQLRAQLAELEAELAELSARYTPNHPD-VIALRAQIAALrAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARL 343
|
250 260 270
....*....|....*....|....*....|....*..
gi 431907173 1252 RTLEDQANEYRT---KLEEAQRSLNDFTTQQAKLQTE 1285
Cdd:COG3206 344 AELPELEAELRRlerEVEVARELYESLLQRLEEARLA 380
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1677-1922 |
5.43e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.66 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1677 LQAELEELRAVVEQTERSRKLAEQELIetseRVQLLHSQntsLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAIT 1756
Cdd:PLN02939 168 LQGKINILEMRLSETDARIKLAAQEKI----HVEILEEQ---LEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1757 DAAMMAEELKKEQDTS---AHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESV 1833
Cdd:PLN02939 241 DIQFLKAELIEVAETEervFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1834 ---KGMRKSERRIKELTYQTEEDKKNLLRLQdLVDKLQLKVKAYKRQAEEAEEQANTnlskfrKVQHELDEAEERADIAE 1910
Cdd:PLN02939 321 lvlDQNQDLRDKVDKLEASLKEANVSKFSSY-KVELLQQKLKLLEERLQASDHEIHS------YIQLYQESIKEFQDTLS 393
|
250
....*....|..
gi 431907173 1911 SQVNKLRAKSRD 1922
Cdd:PLN02939 394 KLKEESKKRSLE 405
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
846-1086 |
5.65e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 846 ETEKEMANMKEE---FGRLKETLEKSEARRKELE-EKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQ-LEAK 920
Cdd:PRK01156 487 EIEIEVKDIDEKivdLKKRKEYLESEEINKSINEyNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEdLDSK 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 921 VKEMNERLEDEEEMNAElTAKKRKledecSELKRDIDDLELTLAKVEKE----KHATENKVKNLTEEMAGLDEIIaKLTK 996
Cdd:PRK01156 567 RTSWLNALAVISLIDIE-TNRSRS-----NEIKKQLNDLESRLQEIEIGfpddKSYIDKSIREIENEANNLNNKY-NEIQ 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 997 EKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKL 1076
Cdd:PRK01156 640 ENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRIN 719
|
250
....*....|
gi 431907173 1077 QLEEKLKKKE 1086
Cdd:PRK01156 720 DINETLESMK 729
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1035-1249 |
5.88e-04 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 45.21 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1035 DLEGSLE--QEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQN------SK--------IED 1098
Cdd:pfam15066 299 DTEQSFEslQPLEEDMALNEVLQKLKHTNRKQQMQIQDLQCSNLYLEKKVKELQMKITKQQvfvdiiNKlkenveelIED 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1099 EQALALQ----------LQKKLKENQARIEELEEELEaerTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNK- 1167
Cdd:pfam15066 379 KYNVILEkndinktlqnLQEILANTQKHLQESRKEKE---TLQLELKKIKVNYVHLQERYITEMQQKNKSVSQCLEMDKt 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1168 --KREAE---FQKMRRDLEEATlqheATAAALRKKHADSvaeLGEQIDNLQRVKQKLEKEksefklelddvtsNMEQIIK 1242
Cdd:pfam15066 456 lsKKEEEverLQQLKGELEKAT----TSALDLLKREKET---REQEFLSLQEEFQKHEKE-------------NLEERQK 515
|
....*..
gi 431907173 1243 AKANLEK 1249
Cdd:pfam15066 516 LKSRLEK 522
|
|
| SH3_GRAP_C |
cd11951 |
C-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor ... |
1930-1983 |
5.98e-04 |
|
C-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor protein that is highly expressed in lymphoid tissues. It acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. It has been identified as a regulator of TGFbeta signaling in diabetic kidney tubules and may have a role in the pathogenesis of the disease. GRAP contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domains (SH3c) of the related proteins, GRB2 and GRAP2, have been shown to bind to classical PxxP motif ligands, as well as to non-classical motifs. GRB2 SH3c binds Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, while the SH3c of GRAP2 binds to the phosphatase-like protein HD-PTP via a RxxxxK motif. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212884 Cd Length: 53 Bit Score: 39.78 E-value: 5.98e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGAggldGWCLCSLHGQQGIVPANRV 1983
Cdd:cd11951 2 VQAQYDFSAEDPSQLSFRRGDIIEVLDCPDP----NWWRGRISGRVGFFPRNYV 51
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1485-1862 |
6.32e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.33 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1485 EESLEHLE---TFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEkleLQSA---LEEAEASLEHEEgKILRAQ 1558
Cdd:COG3096 278 NERRELSEralELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQD---YQAAsdhLNLVQTALRQQE-KIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1559 LEFnqikAEIERKLAEKDEEMEQAKRNHLRV----------VDSL-------QTSLDA-ETRS--RNEALRVKKKMEGDL 1618
Cdd:COG3096 354 EDL----EELTERLEEQEEVVEEAAEQLAEAearleaaeeeVDSLksqladyQQALDVqQTRAiqYQQAVQALEKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1619 NEMEIQLSQANRTASEAQKHLKIAQAHLKD--TQLQMDDAVRANDD----LKENIA-IVER------------------- 1672
Cdd:COG3096 430 GLPDLTPENAEDYLAAFRAKEQQATEEVLEleQKLSVADAARRQFEkayeLVCKIAgEVERsqawqtarellrryrsqqa 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1673 ---RNNLLQAELEELRAVVEQTERSRKLAEQ------ELIETSERVQLLHSQNTSLInqkkkmeSDLTQLQSEVEEAVQE 1743
Cdd:COG3096 510 laqRLQQLRAQLAELEQRLRQQQNAERLLEEfcqrigQQLDAAEELEELLAELEAQL-------EELEEQAAEAVEQRSE 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1744 CRNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQhrldeaeqialkggkkqlQKLEARVRELENELE 1823
Cdd:COG3096 583 LRQQLEQLRARIKELAARAPAWLAAQDA---LERLREQSGEALADSQ------------------EVTAAMQQLLERERE 641
|
410 420 430
....*....|....*....|....*....|....*....
gi 431907173 1824 AEQKRNaESVKGMRKSERRIKELTYQTEEDKKNLLRLQD 1862
Cdd:COG3096 642 ATVERD-ELAARKQALESQIERLSQPGGAEDPRLLALAE 679
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
861-1036 |
6.42e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 45.31 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 861 LKETLEKSEARRKELEEKMVSLLQEkndLQLQVQAEQDNLN------DAEERCDQLIKNKIQLEAK-VKEMNERLEDEEE 933
Cdd:PLN03188 1045 PEKKLEQERLRWTEAESKWISLAEE---LRTELDASRALAEkqkhelDTEKRCAEELKEAMQMAMEgHARMLEQYADLEE 1121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 934 MNAELTAKKRKLEDECSELK-------------RDIDDL--ELTLAKVEKEKHAT----ENK-----VKNLTEEMAGLDE 989
Cdd:PLN03188 1122 KHIQLLARHRRIQEGIDDVKkaaaragvrgaesKFINALaaEISALKVEREKERRylrdENKslqaqLRDTAEAVQAAGE 1201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 431907173 990 IIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDL 1036
Cdd:PLN03188 1202 LLVRLKEAEEALTVAQKRAMDAEQEAAEAYKQIDKLKRKHENEISTL 1248
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1194-1678 |
6.48e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1194 LRKKHADSVAELGEQIDNLQ--RVKQKLEKEKS------------EFKLELDDVTSNmeqiikAKANLEKVSRTLEDQAN 1259
Cdd:PRK04778 23 LRKRNYKRIDELEERKQELEnlPVNDELEKVKKlnltgqseekfeEWRQKWDEIVTN------SLPDIEEQLFEAEELND 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1260 EYR-----TKLEEAQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLtrgKLSYtqqtEDLKRQLEEE----GKAKNA 1330
Cdd:PRK04778 97 KFRfrkakHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQL---KDLY----RELRKSLLANrfsfGPALDE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1331 LAHALQSARHDcdllREQYEEETEA--KAELQRVLSKANSEVAQWRTKYE----------TDAIQRTEELEEA--KLQDA 1396
Cdd:PRK04778 170 LEKQLENLEEE----FSQFVELTESgdYVEAREILDQLEEELAALEQIMEeipellkelqTELPDQLQELKAGyrELVEE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1397 EEAVEAVNakcssLEKTKHRLQNEIEDLMVDVERSN--AAAAALDKKQRNFDKILAEWKQKYeesqselessqkEARSls 1474
Cdd:PRK04778 246 GYHLDHLD-----IEKEIQDLKEQIDENLALLEELDldEAEEKNEEIQERIDQLYDILEREV------------KARK-- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1475 tELFKLKNAYEESLEHLetfKRENKNLQEEISDLTE--QLGEG-GKNVHELEKVRKQLEAEKLELQSALEEAEASLehee 1551
Cdd:PRK04778 307 -YVEKNSDTLPDFLEHA---KEQNKELKEEIDRVKQsyTLNESeLESVRQLEKQLESLEKQYDEITERIAEQEIAY---- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1552 gkilraqlefnqikAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEG--------------- 1616
Cdd:PRK04778 379 --------------SELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEikryleksnlpglpe 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1617 ----DLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKENIAIVERrnnLLQ 1678
Cdd:PRK04778 445 dyleMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVENATLTEQ---LIQ 507
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1485-1624 |
6.71e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1485 EESLEHLETFKRENKNLQEEISDLTEQlgeggknVHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQi 1564
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEE-------IRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR- 459
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1565 KAEIERKLAEKDEEmeqakrnhlrvVDSLQTSLDaETRSRNEALRVKKKMEGDLNEMEIQ 1624
Cdd:COG2433 460 EIRKDREISRLDRE-----------IERLERELE-EERERIEELKRKLERLKELWKLEHS 507
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1143-1442 |
6.82e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.94 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1143 RELEEISERLEEAggatsvqiemnKKR-EAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELgeqidnLQRVKQKLEK 1221
Cdd:PRK05035 439 RAIEQEKKKAEEA-----------KARfEARQARLEREKAAREARHKKAAEARAAKDKDAVAAA------LARVKAKKAA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1222 EKSEFKLELDDVTSNMEQIIKAKAnlekvsrtledqaneyrTKLEEAQRslndfttqQAKLQTENGELARqleeKEALIS 1301
Cdd:PRK05035 502 ATQPIVIKAGARPDNSAVIAAREA-----------------RKAQARAR--------QAEKQAAAAADPK----KAAVAA 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1302 QLTRGKLSYTQQTEDLKRQLEEEGKAKNALAHALqsARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDA 1381
Cdd:PRK05035 553 AIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAI--ARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAE 630
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 431907173 1382 IQRTEELEEAKlQDAEEAVEAVNAKCSSleKTKHRLQNEIEDLMVDVERSNAAAAALDKKQ 1442
Cdd:PRK05035 631 QQANAEPEEPV-DPRKAAVAAAIARAKA--RKAAQQQANAEPEEAEDPKKAAVAAAIARAK 688
|
|
| SH3_Intersectin2_5 |
cd11996 |
Fifth Src homology 3 domain (or SH3E) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor ... |
1932-1985 |
6.86e-04 |
|
Fifth Src homology 3 domain (or SH3E) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The fifth SH3 domain (or SH3E) of ITSN2 is expected to bind protein partners, similar to ITSN1 which has been shown to bind many protein partners including SGIP1, Sos1, dynamin1/2, CIN85, c-Cbl, SHIP2, N-WASP, and synaptojanin-1, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212929 [Multi-domain] Cd Length: 54 Bit Score: 39.58 E-value: 6.86e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQREGAggldGWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd11996 5 AMYDYTANNEDELSFSKGQLINVLNKDDP----DWWQGEINGVTGLFPSNYVKM 54
|
|
| SH3_SH3RF2_1 |
cd11929 |
First Src Homology 3 domain of SH3 domain containing ring finger 2; SH3RF2 is also called ... |
1930-1985 |
6.92e-04 |
|
First Src Homology 3 domain of SH3 domain containing ring finger 2; SH3RF2 is also called POSHER (POSH-eliminating RING protein) or HEPP1 (heart protein phosphatase 1-binding protein). It acts as an anti-apoptotic regulator of the JNK pathway by binding to and promoting the degradation of SH3RF1 (or POSH), a scaffold protein that is required for pro-apoptotic JNK activation. It may also play a role in cardiac functions together with protein phosphatase 1. SH3RF2 contains an N-terminal RING finger domain and three SH3 domains. This model represents the first SH3 domain, located at the N-terminal half, of SH3RF2. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212862 Cd Length: 54 Bit Score: 39.54 E-value: 6.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLrVLQREgaggLD-GWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd11929 3 AKALCNYRGHNPGDLKFNKGDVI-LLRRQ----LDeNWYLGEINGVSGIFPASSVEV 54
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1327-1455 |
7.34e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1327 AKNALAHALQSARHDCDLLREqyEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELE--EAKLQDAEEAVEavn 1404
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQklEKRLLQKEENLD--- 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 431907173 1405 AKCSSLEKTKHRLQNEIEDLmvdversNAAAAALDKKQRNFDKILAEWKQK 1455
Cdd:PRK12704 100 RKLELLEKREEELEKKEKEL-------EQKQQELEKKEEELEELIEEQLQE 143
|
|
| SH3_Alpha_Spectrin |
cd11808 |
Src homology 3 domain of Alpha Spectrin; Spectrin is a major structural component of the red ... |
1932-1984 |
7.61e-04 |
|
Src homology 3 domain of Alpha Spectrin; Spectrin is a major structural component of the red blood cell membrane skeleton and is important in erythropoiesis and membrane biogenesis. It is a flexible, rope-like molecule composed of two subunits, alpha and beta, which consist of many spectrin-type repeats. Alpha and beta spectrin associate to form heterodimers and tetramers; spectrin tetramer formation is critical for red cell shape and deformability. Defects in alpha spectrin have been associated with inherited hemolytic anemias including hereditary spherocytosis (HSp), hereditary elliptocytosis (HE), and hereditary pyropoikilocytosis (HPP). Alpha spectrin contains a middle SH3 domain and a C-terminal EF-hand binding motif in addition to multiple spectrin repeats. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212742 [Multi-domain] Cd Length: 53 Bit Score: 39.39 E-value: 7.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQregAGGLDGWCLcSLHGQQGIVPANRVK 1984
Cdd:cd11808 4 ALYDYQEKSPREVSMKKGDILTLLN---SSNKDWWKV-EVNDRQGFVPAAYVK 52
|
|
| SH3_Pex13p_fungal |
cd11771 |
Src Homology 3 domain of fungal peroxisomal membrane protein Pex13p; Pex13p, located in the ... |
1930-1983 |
7.78e-04 |
|
Src Homology 3 domain of fungal peroxisomal membrane protein Pex13p; Pex13p, located in the peroxisomal membrane, contains two transmembrane regions and a C-terminal SH3 domain. It binds to the peroxisomal targeting type I (PTS1) receptor Pex5p and the docking factor Pex14p through its SH3 domain. It is essential for both PTS1 and PTS2 protein import pathways into the peroxisomal matrix. Pex13p binds Pex14p, which contains a PxxP motif, in a classical fashion to the proline-rich ligand binding site of its SH3 domain. It binds the WxxxF/Y motif of Pex5p in a novel site that does not compete with Pex14p binding. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212705 [Multi-domain] Cd Length: 60 Bit Score: 39.57 E-value: 7.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1930 ARALYDNTAESPQ-ELSFRRGDVLRVLQREGAGGLD-GWCLCSLH-GQQGIVPANRV 1983
Cdd:cd11771 2 CRALYDFTPENPEmELSLKKGDIVAVLSKTDPLGRDsEWWKGRTRdGRIGWFPSNYV 58
|
|
| SH3_Srms |
cd11846 |
Src homology 3 domain of Srms Protein Tyrosine Kinase; Src-related kinase lacking C-terminal ... |
1932-1983 |
7.87e-04 |
|
Src homology 3 domain of Srms Protein Tyrosine Kinase; Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristoylation sites (Srms) is a cytoplasmic (or non-receptor) PTK with limited homology to Src kinases. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). However, Srms lacks the N-terminal myristoylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212780 Cd Length: 55 Bit Score: 39.37 E-value: 7.87e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQREGaggldGWCLC-SLHGQ--QGIVPANRV 1983
Cdd:cd11846 4 ALYDFTARSTHELSVEQGDKLCVIEEEG-----DYIFArKLTGNpeSGLVPASYV 53
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
843-1025 |
7.92e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.97 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 843 KSAETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLLQEKNDLQlqvqaeqdnlndaeercdqliknkiQLEAKVK 922
Cdd:pfam13851 41 KEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLK-------------------------NLKARLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 923 EMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLA-KVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKAL 1001
Cdd:pfam13851 96 VLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQqKTGLKNLLLEKKLQALGETLEKKEAQLNEVLAAANLD 175
|
170 180
....*....|....*....|....
gi 431907173 1002 QEAHQQALDDLQAEEDKVNTLTKS 1025
Cdd:pfam13851 176 PDALQAVTEKLEDVLESKNQLIKD 199
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
854-1403 |
8.07e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.46 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 854 MKEEFGRLK------ETLEKSEARRKELEEkmvSLLQEKNDLQLQV-QAEQDN----LNDAEERCDQLIKNKIQLEAKVK 922
Cdd:pfam06160 27 VQEELSKVKklnltgETQEKFEEWRKKWDD---IVTKSLPDIEELLfEAEELNdkyrFKKAKKALDEIEELLDDIEEDIK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 923 EMNERLEDEEEMNAELTAKKRKLEDECSELKRDI----DDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKltkek 998
Cdd:pfam06160 104 QILEELDELLESEEKNREEVEELKDKYRELRKTLlanrFSYGPAIDELEKQLAEIEEEFSQFEELTESGDYLEAR----- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 999 KALQEAHQQaLDDLQAEEDKVNTL-TKSKVKLEQQVDDLEGSLEQekkvrmdLERAKRKLEgDLKLTQEsIMDLENDKLQ 1077
Cdd:pfam06160 179 EVLEKLEEE-TDALEELMEDIPPLyEELKTELPDQLEELKEGYRE-------MEEEGYALE-HLNVDKE-IQQLEEQLEE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1078 LEEKLKKKEFD-ISQQNSKIEDeqalalqlqkklkenqaRIEELEEELEAERTARAKVEKlrsdlsrELEEISERLEEAg 1156
Cdd:pfam06160 249 NLALLENLELDeAEEALEEIEE-----------------RIDQLYDLLEKEVDAKKYVEK-------NLPEIEDYLEHA- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1157 gatsvqiemnkkrEAEFQKMRRDLEEA----TLQHEATAaalrkkhadSVAELGEQIDNL----QRVKQKLEKEKSEFKL 1228
Cdd:pfam06160 304 -------------EEQNKELKEELERVqqsyTLNENELE---------RVRGLEKQLEELekryDEIVERLEEKEVAYSE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1229 ELDDVTSNMEQIIKAKANLEKVSrtleDQANEYRTKLEEAQRSLndfttqqAKLQTENGELARQLEEK------EALISQ 1302
Cdd:pfam06160 362 LQEELEEILEQLEEIEEEQEEFK----ESLQSLRKDELEAREKL-------DEFKLELREIKRLVEKSnlpglpESYLDY 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1303 LTRGklsyTQQTEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANsevaQWRTKYET--D 1380
Cdd:pfam06160 431 FFDV----SDEIEDLADELNEVPLNMDEVNRLLDEAQDDVDTLYEKTEELIDNATLAEQLIQYAN----RYRSSNPEvaE 502
|
570 580
....*....|....*....|....*....
gi 431907173 1381 AIQRTEEL------EEAkLQDAEEAVEAV 1403
Cdd:pfam06160 503 ALTEAELLfrnydyEKA-LEIAATALEKV 530
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1071-1394 |
8.24e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 44.90 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1071 LENDKLQLEEKLKKKEFDISQQ---NSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRsdlsRELEE 1147
Cdd:pfam15964 149 LENEKLQQELKSQTQEETLREQtllDSSGNMQNSWCTPEDSRVHQTSKRPASHNLAERLKSATTGEDEKWR----LELEK 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1148 ISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAA--------LRKKHADSVAELGEQIDNLQ-RVKQK 1218
Cdd:pfam15964 225 LKLLYEAKTEVLESQVKSLRKDLAESQKTCEDLKERLKHKESLVAAstssrvggLCLKCAQHEAVLAQTHTNVHmQTIER 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1219 LEKEKSEFKLELDDVTSNMEQIIKAKAN-LEKVSRTLE--DQANEYRTK-LEEAQRSLNDFTTQQAKLQTE-NGELARQL 1293
Cdd:pfam15964 305 LTKERDDLMSALVSVRSSLAEAQQRESSaYEQVKQAVQmtEEANFEKTKaLIQCEQLKSELERQKERLEKElASQQEKRA 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1294 EEKEALISQLTRGK-------LSYTQQTEDLKRQLEEEGKAKNALAHALQSARHDcdlLREQYEEETEAKAELQRVLSKA 1366
Cdd:pfam15964 385 QEKEALRKEMKKEReelgatmLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQ---LASQEMDVTKVCGEMRYQLNQT 461
|
330 340 350
....*....|....*....|....*....|....*
gi 431907173 1367 N-------SEVAQWRTKYETDAIQRTEELEEAKLQ 1394
Cdd:pfam15964 462 KmkkdeaeKEHREYRTKTGRQLEIKDQEIEKLGLE 496
|
|
| SH3_Intersectin_3 |
cd11838 |
Third Src homology 3 domain (or SH3C) of Intersectin; Intersectins (ITSNs) are adaptor ... |
1932-1985 |
8.60e-04 |
|
Third Src homology 3 domain (or SH3C) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The third SH3 domain (or SH3C) of ITSN1 has been shown to bind many proteins including dynamin1/2, CIN85, c-Cbl, SHIP2, Reps1, synaptojanin-1, and WNK, among others. The SH3C of ITSN2 has been shown to bind the K15 protein of Kaposi's sarcoma-associated herpesvirus. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212772 [Multi-domain] Cd Length: 52 Bit Score: 39.32 E-value: 8.60e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQREGAggldgWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd11838 4 ALYPYESNEPGDLTFNAGDVILVTKKDGE-----WWTGTIGDRTGIFPSNYVRP 52
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1037-1348 |
8.64e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1037 EGSLEQEKKVRMDLER-AKRKL-EGDLKLTQEsimDLENDKLQLEeklkkkefDISQQNSKIEDEQALALQLQKKLKENQ 1114
Cdd:PRK11281 32 NGDLPTEADVQAQLDAlNKQKLlEAEDKLVQQ---DLEQTLALLD--------KIDRQKEETEQLKQQLAQAPAKLRQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1115 ARIEELEEELEAERTARAKVEKLRsDLSRELEEISERLEEA----GGATS-----------VQIEM--NKKReaeFQKMR 1177
Cdd:PRK11281 101 AELEALKDDNDEETRETLSTLSLR-QLESRLAQTLDQLQNAqndlAEYNSqlvslqtqperAQAALyaNSQR---LQQIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1178 RDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTsnmEQIikakANLEKVSRTLEDQ 1257
Cdd:PRK11281 177 NLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLT---ARI----QRLEHQLQLLQEA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1258 ANEYRtkLEEAQRSLNDFTTQQAKLQ-TENGELARQLEEKealiSQLTRGKLSYTQQTEDLKRQleeEGKAKNALAHALQ 1336
Cdd:PRK11281 250 INSKR--LTLSEKTVQEAQSQDEAARiQANPLVAQELEIN----LQLSQRLLKATEKLNTLTQQ---NLRVKNWLDRLTQ 320
|
330
....*....|..
gi 431907173 1337 SARHdcdlLREQ 1348
Cdd:PRK11281 321 SERN----IKEQ 328
|
|
| SH3_DLG5 |
cd11860 |
Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein ... |
1931-1954 |
8.97e-04 |
|
Src homology 3 domain of Disks Large homolog 5; DLG5 is a multifunctional scaffold protein that is located at sites of cell-cell contact and is involved in the maintenance of cell shape and polarity. Mutations in the DLG5 gene are associated with Crohn's disease (CD) and inflammatory bowel disease (IBD). DLG5 is a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG5 contains 4 PDZ domains as well as an N-terminal domain of unknown function. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212794 Cd Length: 63 Bit Score: 39.63 E-value: 8.97e-04
10 20
....*....|....*....|....
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRV 1954
Cdd:cd11860 3 RALFDRSAENEDELSFKKDDILYV 26
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1473-1814 |
8.97e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 44.51 E-value: 8.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1473 LSTELFKLKNAYEESLE-HLETFKRENKNLQEEISDLTEQLGEG----GKNVHELEKVRKQLEAEKLELQSALEEAEASL 1547
Cdd:pfam15964 361 LKSELERQKERLEKELAsQQEKRAQEKEALRKEMKKEREELGATmlalSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQL 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1548 EHEEgkilraqLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRsRNEALRVkkkmegDLNEMEIQLSQ 1627
Cdd:pfam15964 441 ASQE-------MDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQ-EIEKLGL------ELSESKQRLEQ 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1628 ANRTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKENIAiverrNNLLQAELEELRAVVEQTERSRKLAEQELIETSE 1707
Cdd:pfam15964 507 AQQDAARAREECLKLTELLGESEHQLHLTRLEKESIQQSFS-----NEAKAQALQAQQREQELTQKMQQMEAQHDKTVNE 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1708 RVQLLHSQNTSLINQK-------KKMESDLTQLQSEVEEAVQECRNAEEKAKKaitdaamMAEELKKEQDTSAHLERMKK 1780
Cdd:pfam15964 582 QYSLLTSQNTFIAKLKeecctlaKKLEEITQKSRSEVEQLSQEKEYLQDRLEK-------LQKRNEELEEQCVQHGRMHE 654
|
330 340 350
....*....|....*....|....*....|....
gi 431907173 1781 NMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEAR 1814
Cdd:pfam15964 655 RMKQRLRQLDKHCQATAQQLVQLLSKQNQLFKER 688
|
|
| SH3_Intersectin2_2 |
cd11990 |
Second Src homology 3 domain (or SH3B) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor ... |
1929-1985 |
9.08e-04 |
|
Second Src homology 3 domain (or SH3B) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The second SH3 domain (or SH3B) of ITSN2 is expected to bind protein partners, similar to ITSN1 which has been shown to bind WNK and CdGAP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212923 [Multi-domain] Cd Length: 52 Bit Score: 39.25 E-value: 9.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1929 LARALYDNTAESPQELSFRRGDVLRVLQREgagglDGWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd11990 1 KAQALCSWTAKKDNHLNFSKNDIITVLEQQ-----ENWWFGEVHGGRGWFPKSYVKL 52
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1558-1832 |
9.10e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.66 E-value: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1558 QLEFNQIKAEIERklAEKDEEMEQAKrnhlrVVDSLQTSLDAETRSRNEALRVKK---------KMEGDLNEMEIQLSQA 1628
Cdd:PRK10929 22 APDEKQITQELEQ--AKAAKTPAQAE-----IVEALQSALNWLEERKGSLERAKQyqqvidnfpKLSAELRQQLNNERDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1629 NRTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKENIAIVERRNNLLQaeleelravvEQTERSRKLAEQElietsER 1708
Cdd:PRK10929 95 PRSVPPNMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQ----------QQTEARRQLNEIE-----RR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1709 VQLLHSQNTSLinqkkkMESDLTQLQseveeavqecrnAEEKAKKAITDaammaeELKkeqdtsahLERMKKNMEQTIKD 1788
Cdd:PRK10929 160 LQTLGTPNTPL------AQAQLTALQ------------AESAALKALVD------ELE--------LAQLSANNRQELAR 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 431907173 1789 LQHRLdeaeqialkgGKKQLQKLEARVRELENELEAEQKRNAES 1832
Cdd:PRK10929 208 LRSEL----------AKKRSQQLDAYLQALRNQLNSQRQREAER 241
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
848-1038 |
9.54e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.83 E-value: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 848 EKEMANMKEEFGR--LKETLEKSEARR---KELEEKMVSLLQEKNDLQLQVQAEQDNLNdaEERCDQLIK------NKIQ 916
Cdd:pfam12128 695 DKKHQAWLEEQKEqkREARTEKQAYWQvveGALDAQLALLKAAIAARRSGAKAELKALE--TWYKRDLASlgvdpdVIAK 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 917 LEAKVKEMNERLEDEEEMNAE------------------LTAKKRKLEDECSELK----RDIDDLELTLAKVEKEKHATE 974
Cdd:pfam12128 773 LKREIRTLERKIERIAVRRQEvlryfdwyqetwlqrrprLATQLSNIERAISELQqqlaRLIADTKLRRAKLEMERKASE 852
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 975 NKVKNLTEEMAGLDEIIAKLT--KEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEG 1038
Cdd:pfam12128 853 KQQVRLSENLRGLRCEMSKLAtlKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKN 918
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1698-1894 |
9.59e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1698 AEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAvqecRNAEEKAKKAITDaammaeelkkeqdtsahLER 1777
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAAL----EARLEAAKTELED-----------------LEK 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1778 MKKNMEQTIKDLQHRLDEAEQiALKGGK--KQLQklearvrELENELEAEQKRNAEsvkgmrkSERRIKELTYQTEEDKK 1855
Cdd:COG1579 60 EIKRLELEIEEVEARIKKYEE-QLGNVRnnKEYE-------ALQKEIESLKRRISD-------LEDEILELMERIEELEE 124
|
170 180 190
....*....|....*....|....*....|....*....
gi 431907173 1856 NLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRK 1894
Cdd:COG1579 125 ELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| SH3_RIM-BP |
cd11851 |
Src homology 3 domains of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding ... |
1929-1984 |
9.89e-04 |
|
Src homology 3 domains of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212785 Cd Length: 62 Bit Score: 39.61 E-value: 9.89e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1929 LARALYD-NTAE-SP-----QELSFRRGDVLRVLqreGAGGLDGWCLCSLHG-QQGIVPANRVK 1984
Cdd:cd11851 1 LMVALYDyNPETmSPnddpeEELSFHAGDVVRVY---GPMDEDGFYYGELEGgRKGLVPSNFVQ 61
|
|
| SH3_STAM |
cd11820 |
Src homology 3 domain of Signal Transducing Adaptor Molecules; STAMs were discovered as ... |
1931-1984 |
1.01e-03 |
|
Src homology 3 domain of Signal Transducing Adaptor Molecules; STAMs were discovered as proteins that are highly phosphorylated following cytokine and growth factor stimulation. They function in cytokine signaling and surface receptor degradation, as well as regulate Golgi morphology. They associate with many proteins including Jak2 and Jak3 tyrosine kinases, Hrs, AMSH, and UBPY. STAM adaptor proteins contain VHS (Vps27, Hrs, STAM homology), ubiquitin interacting (UIM), and SH3 domains. There are two vertebrate STAMs, STAM1 and STAM2, which may be functionally redundant; vertebrate STAMs contain ITAM motifs. They are part of the endosomal sorting complex required for transport (ESCRT-0). STAM2 deficiency in mice did not cause any obvious abnormality, while STAM1 deficiency resulted in growth retardation. Loss of both STAM1 and STAM2 in mice proved lethal, indicating that STAMs are important for embryonic development. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212754 [Multi-domain] Cd Length: 54 Bit Score: 39.37 E-value: 1.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGAggldGWCLCSLHGQQGIVPANRVK 1984
Cdd:cd11820 4 RALYDFEAAEDNELTFKAGEIITVLDDSDP----NWWKGSNHRGEGLFPANFVT 53
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
950-1282 |
1.02e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 950 SELKRDIDDLELTLAKVEKEKHATENKVKNLTEEmagLDEIIAKLTKEKKALQEAHQQalddLQAEEDKVNTLTKSKVKL 1029
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREE---LEQLEEELEQARSELEQLEEE----LEELNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1030 EQQV-------DDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQAL 1102
Cdd:COG4372 100 QEELeslqeeaEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1103 ALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEE 1182
Cdd:COG4372 180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1183 ATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYR 1262
Cdd:COG4372 260 IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339
|
330 340
....*....|....*....|
gi 431907173 1263 TKLEEAQRSLNDFTTQQAKL 1282
Cdd:COG4372 340 ADLLQLLLVGLLDNDVLELL 359
|
|
| SH3_Blk |
cd12009 |
Src homology 3 domain of Blk Protein Tyrosine Kinase; Blk is a member of the Src subfamily of ... |
1932-1983 |
1.03e-03 |
|
Src homology 3 domain of Blk Protein Tyrosine Kinase; Blk is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. It is expressed specifically in B-cells and is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212942 [Multi-domain] Cd Length: 54 Bit Score: 39.03 E-value: 1.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSL-HGQQGIVPANRV 1983
Cdd:cd12009 4 AQYDFVPSNERDLQLKKGEKLQVLKSDG----EWWLAKSLtTGKEGYIPSNYV 52
|
|
| SH3_GRAF2 |
cd12065 |
Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase 2; GRAF2, also ... |
1930-1985 |
1.04e-03 |
|
Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase 2; GRAF2, also called Rho GTPase activating protein 10 (ARHGAP10) or PS-GAP, is a GAP with activity towards Cdc42 and RhoA. It regulates caspase-activated p21-activated protein kinase-2 (PAK-2p34). GRAF2 interacts with PAK-2p34, leading to its stabilization and decrease of cell death. It is highly expressed in skeletal muscle, and is involved in alpha-catenin recruitment at cell-cell junctions. GRAF2 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. The SH3 domain of GRAF binds PKNbeta, a target of the small GTPase Rho. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.
Pssm-ID: 212998 [Multi-domain] Cd Length: 54 Bit Score: 39.20 E-value: 1.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQ--REgagglDGWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd12065 2 AKAVYPCEAEHSSELSFEVGAIFEDVTlsRE-----PGWLEGTLNGKRGLIPENYVEI 54
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1618-1939 |
1.06e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1618 LNEMeIQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDAVRAnddlkeniaiVERRNNL------LQAELEELRAVVEQT 1691
Cdd:pfam17380 271 LNQL-LHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKARE----------VERRRKLeeaekaRQAEMDRQAAIYAEQ 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1692 ERSRKLAEQEL--IETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAitdaaMMAEElkkeq 1769
Cdd:pfam17380 340 ERMAMERERELerIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKV-----KILEE----- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1770 dtsahlERMKKNMEQTIKDLQHRLDEAEqialkGGKKQLQKLEA-RVRELENELEAEQKRNaESVKGMRKSERRIKELTY 1848
Cdd:pfam17380 410 ------ERQRKIQQQKVEMEQIRAEQEE-----ARQREVRRLEEeRAREMERVRLEEQERQ-QQVERLRQQEEERKRKKL 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1849 QTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQvnklRAKSRDIGAKAQ 1928
Cdd:pfam17380 478 ELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEE----RRKQQEMEERRR 553
|
330
....*....|.
gi 431907173 1929 LARALYDNTAE 1939
Cdd:pfam17380 554 IQEQMRKATEE 564
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1745-1910 |
1.09e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1745 RNAEEKAKKAITDAAMMAEELKKEqdtsahLERMKKNMEQTIKDLQHRLdeaeqialkggkkqLQKLEARVRELENELEA 1824
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKE------AEAIKKEALLEAKEEIHKL--------------RNEFEKELRERRNELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1825 EQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQAnTNLSKFRKVQHELDEAEE 1904
Cdd:PRK12704 87 LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI-SGLTAEEAKEILLEKVEE 165
|
....*...
gi 431907173 1905 --RADIAE 1910
Cdd:PRK12704 166 eaRHEAAV 173
|
|
| SH3_SNX18 |
cd11897 |
Src Homology 3 domain of Sorting nexin 18; SNX18 is localized to peripheral endosomal ... |
1930-1985 |
1.13e-03 |
|
Src Homology 3 domain of Sorting nexin 18; SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1. It binds FIP5 and is required for apical lumen formation. It may also play a role in axonal elongation. SNXs are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNX18 also contains BAR and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212830 [Multi-domain] Cd Length: 55 Bit Score: 39.20 E-value: 1.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREgagGLDGWCL-CSLHGQQGIVPANRVKL 1985
Cdd:cd11897 2 ARALYDFRSENPGEISLREHEVLSLCSEQ---DIEGWLEgVNSRGDRGLFPASYVEV 55
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1654-1935 |
1.14e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1654 DDAVRANDDLKENIAIVERRN-----NLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLinqkkkmeS 1728
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKDlherlNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL--------E 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1729 DLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQD---TSAHLERMK-KNMEQTIKDLQHRLDEAEQialkgg 1804
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDdllAEAGLDDADaEAVEARREELEDRDEELRD------ 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1805 kkqlQKLEARVRELENELEAEqkRNAESVKgmrKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQ 1884
Cdd:PRK02224 329 ----RLEECRVAAQAHNEEAE--SLREDAD---DLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 431907173 1885 ANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKAQLARALYD 1935
Cdd:PRK02224 400 FGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLE 450
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1001-1638 |
1.18e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.41 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1001 LQEAHQQALDD-LQAEEDKVNTLTKSKVKLEQQVDDL--EGSLEQEKKVRMDLERAkrklegdlklTQESIMDLENDKLQ 1077
Cdd:PRK10246 213 LTPEQVQSLTAsLQVLTDEEKQLLTAQQQQQQSLNWLtrLDELQQEASRRQQALQQ----------ALAAEEKAQPQLAA 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1078 LEekLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTA----RAKVEKLRSDLSRELEEiSERL- 1152
Cdd:PRK10246 283 LS--LAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHaakqSAELQAQQQSLNTWLAE-HDRFr 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1153 ---EEAGGATSVQIEMNKKReAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLE 1229
Cdd:PRK10246 360 qwnNELAGWRAQFSQQTSDR-EQLRQWQQQLTHAEQKLNALPAITLTLTADEVAAALAQHAEQRPLRQRLVALHGQIVPQ 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1230 LDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQR---------SLNDFTTQQAKLQ----------TENGELA 1290
Cdd:PRK10246 439 QKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADvkticeqeaRIKDLEAQRAQLQagqpcplcgsTSHPAVE 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1291 rQLEEKEALISQLTRGKLsytqqtEDLKRQLEEEGKAknalahalqsARHDCDLLREQYEEETEakaELQRVLSKANSEV 1370
Cdd:PRK10246 519 -AYQALEPGVNQSRLDAL------EKEVKKLGEEGAA----------LRGQLDALTKQLQRDES---EAQSLRQEEQALT 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1371 AQWRTKYETDAIQRTEELEEAKLQDAEEAVEavnaKCSSLEKTKHRLQNEIedlmvdversnaaaAALDKKQRNFDKILA 1450
Cdd:PRK10246 579 QQWQAVCASLNITLQPQDDIQPWLDAQEEHE----RQLRLLSQRHELQGQI--------------AAHNQQIIQYQQQIE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1451 EWKQKYEESQSELESSQKEARSLSTELfklkNAYEESLEHLETFKRENKNLQEEISDLT---EQLGEGGKNVHELEKVR- 1526
Cdd:PRK10246 641 QRQQQLLTALAGYALTLPQEDEEASWL----ATRQQEAQSWQQRQNELTALQNRIQQLTpllETLPQSDDLPHSEETVAl 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1527 ---KQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFnqikaeiERKLAEKDEEMEQAkrnhlrvvdSLQTSLDAETRS 1603
Cdd:PRK10246 717 dnwRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQF-------DTALQASVFDDQQA---------FLAALLDEETLT 780
|
650 660 670
....*....|....*....|....*....|....*
gi 431907173 1604 RNEALrvKKKMEGDLNEMEIQLSQANRTASEAQKH 1638
Cdd:PRK10246 781 QLEQL--KQNLENQRQQAQTLVTQTAQALAQHQQH 813
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
955-1085 |
1.23e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.30 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 955 DIDDLELTLAKVEKEKHATENkvknltEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVD 1034
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKK------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1035 DLEGSLEQEKKVRMDLERAKRKLEGDL------------------KLTQEsimdlENDKL-QLEEKLKKK 1085
Cdd:COG0542 486 KIPELEKELAELEEELAELAPLLREEVteediaevvsrwtgipvgKLLEG-----EREKLlNLEEELHER 550
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
897-1296 |
1.24e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 897 QDNLNDAEERCDQLiknkiqlEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEkhaTENK 976
Cdd:PRK04778 104 KHEINEIESLLDLI-------EEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDE---LEKQ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 977 VKNLTEEMAGLDEIIAK--LTKEKKALQEAHQQaLDDLQAEEDKVNTL-TKSKVKLEQQVDDLEGSLEQekkvrmdLERA 1053
Cdd:PRK04778 174 LENLEEEFSQFVELTESgdYVEAREILDQLEEE-LAALEQIMEEIPELlKELQTELPDQLQELKAGYRE-------LVEE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1054 KRKLEgDLKLTQEsIMDLENDKLQLEEKLKKKEFD-ISQQNSKIEDE-QALALQLQKKLKenqarieeleeeleaertAR 1131
Cdd:PRK04778 246 GYHLD-HLDIEKE-IQDLKEQIDENLALLEELDLDeAEEKNEEIQERiDQLYDILEREVK------------------AR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1132 AKVEKlrsdlsrELEEISERLEEAggatsvqIEMNKKREAEFQKMRrdlEEATLQHEAtaaalrkkhADSVAELGEQIDN 1211
Cdd:PRK04778 306 KYVEK-------NSDTLPDFLEHA-------KEQNKELKEEIDRVK---QSYTLNESE---------LESVRQLEKQLES 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1212 LQRV----KQKLEKEK---SEFKLELDDVTSNMEQI-------IKAKANLEKVSRTLEDQANEYRTKLEEAQRSL----- 1272
Cdd:PRK04778 360 LEKQydeiTERIAEQEiaySELQEELEEILKQLEEIekeqeklSEMLQGLRKDELEAREKLERYRNKLHEIKRYLeksnl 439
|
410 420
....*....|....*....|....*...
gi 431907173 1273 ----NDFTTQQAKLQTENGELARQLEEK 1296
Cdd:PRK04778 440 pglpEDYLEMFFEVSDEIEALAEELEEK 467
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1692-1912 |
1.27e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.17 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1692 ERSRKLAEQELIETSERVQllhSQNTSLINQKKKMEsdltqlQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDT 1771
Cdd:pfam15709 314 ERSEEDPSKALLEKREQEK---ASRDRLRAERAEMR------RLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQR 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1772 SAHLERMKKnmeQTIKDLQHRLDEAEqialKGGKKQLQKLEARVRELENE-----LEAEQKRNAESVKGMRKSERRIKEL 1846
Cdd:pfam15709 385 RFEEIRLRK---QRLEEERQRQEEEE----RKQRLQLQAAQERARQQQEEfrrklQELQRKKQQEEAERAEAEKQRQKEL 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1847 TYQTEEDKKnllRLQDLVDKLQLKvkaYKRQAEEAEEQAntnlskfrkvqheLDEAEERADIAESQ 1912
Cdd:pfam15709 458 EMQLAEEQK---RLMEMAEEERLE---YQRQKQEAEEKA-------------RLEAEERRQKEEEA 504
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1987-2262 |
1.35e-03 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 44.37 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1987 PAGPTPKPSL-SQVPPAE--------------PGSPYPAPEHSNEDQevyvVPPPARPCLTSESPAGPCLPSPDPIYKVP 2051
Cdd:pfam03154 262 SPQPLPQPSLhGQMPPMPhslqtgpshmqhpvPPQPFPLTPQSSQSQ----VPPGPSPAAPGQSQQRIHTPPSQSQLQSQ 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2052 RGSGTQPATPGDALEVYDVPPAALRVSasgPYDTPASFSHLLARVAPQPpgeDEAPYDVPLAPK-----------PPSEL 2120
Cdd:pfam03154 338 QPPREQPLPPAPLSMPHIKPPPTTPIP---QLPNPQSHKHPPHLSGPSP---FQMNSNLPPPPAlkplsslsthhPPSAH 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2121 EPDLEWEGGREPGPPLYAAPSNLKRAsallnlyeapEELLADGEEGGSDEGIYDVPllgPETPPSPEPLgaLASNDPDTL 2200
Cdd:pfam03154 412 PPPLQLMPQSQQLPPPPAQPPVLTQS----------QSLPPPAASHPPTSGLHQVP---SQSPFPQHPF--VPGGPPPIT 476
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 2201 AlllARSPPPSHRPRLP------SAESLSRRPLPALPVPEAPSPSPVPSPAPgrkgSIQDRPLPPPPP 2262
Cdd:pfam03154 477 P---PSGPPTSTSSAMPgiqppsSASVSSSGPVPAAVSCPLPPVQIKEEALD----EAEEPESPPPPP 537
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1745-1932 |
1.40e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.64 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1745 RNAEEKAKKaitDAAMMAEELKKEQDtsAHLERMKKNMEQTIKDLQHRlDEAEQIALKGGKKQLQKLEARVRELEN---E 1821
Cdd:PRK09510 75 KRAEEQRKK---KEQQQAEELQQKQA--AEQERLKQLEKERLAAQEQK-KQAEEAAKQAALKQKQAEEAAAKAAAAakaK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1822 LEAEQKRNAESVKgmrkserrikeltyQTEEDKKNLlrlqdlvDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHElDE 1901
Cdd:PRK09510 149 AEAEAKRAAAAAK--------------KAAAEAKKK-------AEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAE-AE 206
|
170 180 190
....*....|....*....|....*....|.
gi 431907173 1902 AEERADIAESQVNKLRAKSRDIGAKAQLARA 1932
Cdd:PRK09510 207 AKKKAAAEAKKKAAAEAKAAAAKAAAEAKAA 237
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
1987-2128 |
1.41e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 43.93 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1987 PAGPTPKPSLSQVPPAEPGSPYPAPEHSNEDQEVYVVPPPArPCLTSESPAGPCLPSPDPIYKVPRGSGTQPATPGdale 2066
Cdd:PRK14951 367 AAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAP-AAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAA---- 441
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 431907173 2067 vydvpPAALRVSASGPYDTPASFSHLLARVAPQPPGEDEAPYDVPLAPKPPSELEPDLE-WEG 2128
Cdd:PRK14951 442 -----PAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEEGDvWHA 499
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
1974-2228 |
1.57e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 44.07 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1974 QQGIVPANRVKLLPAGPTPKPSLSQVPPAEPGSPyPAPEHSNEDQEVYVVPPPARPC-LTSESPAGPCLPSPDPiykVPR 2052
Cdd:PRK07003 376 VAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAA-LAPKAAAAAAATRAEAPPAAPApPATADRGDDAADGDAP---VPA 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2053 GSGTQPATPGDALEVYDVPPAALRVSASGPYDTP-------ASFSHLLARVAPQPPGEDEAPYDVPL--APKPPSELEPD 2123
Cdd:PRK07003 452 KANARASADSRCDERDAQPPADSGSASAPASDAPpdaafepAPRAAAPSAATPAAVPDARAPAAASRedAPAAAAPPAPE 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2124 LeweggREPGPPLYAAPSNLKRASALLNLyeapeeLLADGEEGGSDEGIYDVPLLGPETPPSPEPLGA---LASNDPDTL 2200
Cdd:PRK07003 532 A-----RPPTPAAAAPAARAGGAAAALDV------LRNAGMRVSSDRGARAAAAAKPAAAPAAAPKPAaprVAVQVPTPR 600
|
250 260
....*....|....*....|....*...
gi 431907173 2201 ALLLARSPPPSHRPRLPSAESlSRRPLP 2228
Cdd:PRK07003 601 ARAATGDAPPNGAARAEQAAE-SRGAPP 627
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1429-1856 |
1.60e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 43.90 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1429 ERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFK--LKNAYEESLEHLETFKRENKNLQEEIS 1506
Cdd:pfam13166 89 EESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDECWKkiKRKKNSALSEALNGFKYEANFKSRLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1507 DLteqlgeggknvhelekVRKQLEAEKLELQSALEEAEASLEhEEGKILRAQLEFNQIkaeiERKLAEKDEEMEQAKRNH 1586
Cdd:pfam13166 169 EI----------------EKDNFNAGVLLSDEDRKAALATVF-SDNKPEIAPLTFNVI----DFDALEKAEILIQKVIGK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1587 LRVVDSLQTSLDAE------------------------TRSRNEALrvkkkmEGDLNEmEIQLSQAN--RTASEAQKHLK 1640
Cdd:pfam13166 228 SSAIEELIKNPDLAdwveqglelhkahldtcpfcgqplPAERKAAL------EAHFDD-EFTEFQNRlqKLIEKVESAIS 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1641 IAQAHLKDtqlqMDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQterSRKlaeqeliETSERVQLlhsqnTSLI 1720
Cdd:pfam13166 301 SLLAQLPA----VSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALEA---KRK-------DPFKSIEL-----DSVD 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1721 NQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITD-AAMMAEELKKEQDTsahLERMKKNMEQTIKDLQHRLDEAEqi 1799
Cdd:pfam13166 362 AKIESINDLVASINELIAKHNEITDNFEEEKNKAKKKlRLHLVEEFKSEIDE---YKDKYAGLEKAINSLEKEIKNLE-- 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1800 alkggkKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYqtEEDKKN 1856
Cdd:pfam13166 437 ------AEIKKLREEIKELEAQLRDHKPGADEINKLLKAFGFGELELSF--NEEGKG 485
|
|
| CBD_MYO6-like |
cd21759 |
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ... |
804-928 |
1.60e-03 |
|
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).
Pssm-ID: 409646 [Multi-domain] Cd Length: 149 Bit Score: 41.34 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 804 KKMVERRDALLVIQWNIRAFMGVKnwpwmKLYFKIKPLLKSAETEKEMANMKEEFGRLKETLEKSEARRKELEEKMVSLL 883
Cdd:cd21759 39 NKILYRREALIKIQKTVRGYLARK-----KHRPRIKGLRKIRALEKQLKEMEEIASQLKKDKDKWTKQVKELKKEIDALI 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 431907173 884 QE-KNDlqlqvqaEQDNLNDAEERCDQLIKNkiqLEAKVKEMNERL 928
Cdd:cd21759 114 KKiKTN-------DMITRKEIDKLYNALVKK---VDKQLAELQKKL 149
|
|
| SH3_Intersectin_4 |
cd11839 |
Fourth Src homology 3 domain (or SH3D) of Intersectin; Intersectins (ITSNs) are adaptor ... |
1929-1985 |
1.62e-03 |
|
Fourth Src homology 3 domain (or SH3D) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The fourth SH3 domain (or SH3D) of ITSN1 has been shown to bind SHIP2, Numb, CdGAP, and N-WASP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212773 [Multi-domain] Cd Length: 58 Bit Score: 38.86 E-value: 1.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 431907173 1929 LARALYDNTAESPQELSFRRGDVLRVLQREGAggldGWCLCSLHG-----QQGIVPANRVKL 1985
Cdd:cd11839 1 IAQVIAPFTATAENQLSLAVGQLVLVRKKSPS----GWWEGELQArgkkrQIGWFPANYVKL 58
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1583-1934 |
1.64e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1583 KRNHLRVVDSLQTSLDAETRSRNEAlrvkkkmEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQlqmdDAVRANDD 1662
Cdd:COG3096 280 RRELSERALELRRELFGARRQLAEE-------QYRLVEMARELEELSARESDLEQDYQAASDHLNLVQ----TALRQQEK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1663 lkeniaiVERRnnllQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQkkkmesdLTQLQSEVEE--- 1739
Cdd:COG3096 349 -------IERY----QEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQ-------LADYQQALDVqqt 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1740 ---AVQECRNAEEKAKKAITDAAMMAEELKKEQdtsAHLERMKKNMEQTIKDLQHRLDEAEQialkgGKKQLQKLEARVR 1816
Cdd:COG3096 411 raiQYQQAVQALEKARALCGLPDLTPENAEDYL---AAFRAKEQQATEEVLELEQKLSVADA-----ARRQFEKAYELVC 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1817 ELENELEAEQkrnAESVKgmRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAyKRQAEEAEEQANTNLSKFRKVQ 1896
Cdd:COG3096 483 KIAGEVERSQ---AWQTA--RELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNA-ERLLEEFCQRIGQQLDAAEELE 556
|
330 340 350
....*....|....*....|....*....|....*...
gi 431907173 1897 HELDEAEERADIAESQVNKLRAKSRDIGAKAQLARALY 1934
Cdd:COG3096 557 ELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARI 594
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
915-1222 |
1.65e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 43.69 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 915 IQLEAKVKEMNERLEDEEEMNAELTakKRKLEDECSELKRDIDdLELTLAKvekEKHATENKVKNLTEEMA--------- 985
Cdd:PLN03229 432 RELEGEVEKLKEQILKAKESSSKPS--ELALNEMIEKLKKEID-LEYTEAV---IAMGLQERLENLREEFSkansqdqlm 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 986 --GLDEIIAKLTKE-KKALQEAhqQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVR--MDLERAKRKLEGD 1060
Cdd:PLN03229 506 hpVLMEKIEKLKDEfNKRLSRA--PNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKevMDRPEIKEKMEAL 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1061 LKLTQESIMDLENDklqLEEKLKKKefdISQQNSKIEDEQA-----LALQLQKKLKENQARIEELEEELEaertaRAKVE 1135
Cdd:PLN03229 584 KAEVASSGASSGDE---LDDDLKEK---VEKMKKEIELELAgvlksMGLEVIGVTKKNKDTAEQTPPPNL-----QEKIE 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1136 KLRSDLSRELEEISE-----------RLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATlqheaTAAALRKKHADSVAE 1204
Cdd:PLN03229 653 SLNEEINKKIERVIRssdlkskiellKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEAL-----NSSELKEKFEELEAE 727
|
330
....*....|....*...
gi 431907173 1205 LGEQIDNLQRVKQKLEKE 1222
Cdd:PLN03229 728 LAAARETAAESNGSLKND 745
|
|
| SH3_Vinexin_1 |
cd11921 |
First Src Homology 3 domain of Vinexin, also called Sorbin and SH3 domain containing 3 (Sorbs3) ... |
1930-1986 |
1.69e-03 |
|
First Src Homology 3 domain of Vinexin, also called Sorbin and SH3 domain containing 3 (Sorbs3); Vinexin is also called Sorbs3, SH3P3, and SH3-containing adapter molecule 1 (SCAM-1). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. Vinexin was first identified as a vinculin binding protein; it is co-localized with vinculin at cell-ECM and cell-cell adhesion sites. There are several splice variants of vinexin: alpha, which contains the SoHo and three SH3 domains and displays tissue-specific expression; and beta, which contains only the three SH3 domains and is widely expressed. Vinexin alpha stimulates the accumulation of F-actin at focal contact sites. Vinexin also promotes keratinocyte migration and wound healing. The SH3 domains of vinexin have been reported to bind a number of ligands including vinculin, WAVE2, DLG5, Abl, and Cbl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212854 Cd Length: 55 Bit Score: 38.75 E-value: 1.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGAGGLDGwclcSLHGQQGIVPANRVKLL 1986
Cdd:cd11921 3 ARLKFDFQAQSPKELTLQKGDIVYIHKEVDKNWLEG----EHHGRVGIFPANYVEVL 55
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1013-1297 |
1.71e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1013 QAEEDKVNTLTKSKvKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEE---------KLK 1083
Cdd:pfam17380 303 QEKEEKAREVERRR-KLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEiameisrmrELE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1084 KKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARA-----KVEKLRSDLSRELEEIseRLEEAggA 1158
Cdd:pfam17380 382 RLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEearqrEVRRLEEERAREMERV--RLEEQ--E 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1159 TSVQIEMNKKREAEFQKMRRDLEEATlQHEATAAALRKKHADSvaelgeqidNLQRVKQKLEKEKSEFKLelddVTSNME 1238
Cdd:pfam17380 458 RQQQVERLRQQEEERKRKKLELEKEK-RDRKRAEEQRRKILEK---------ELEERKQAMIEEERKRKL----LEKEME 523
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1239 QIIKAKANLEKVSRTLED----QANEYRTKLEEAQRSLNDFTTQQAKLQTENgELARQLEEKE 1297
Cdd:pfam17380 524 ERQKAIYEEERRREAEEErrkqQEMEERRRIQEQMRKATEERSRLEAMERER-EMMRQIVESE 585
|
|
| SH3_Cortactin_like |
cd11819 |
Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, ... |
1930-1985 |
1.75e-03 |
|
Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, Abp1 (actin-binding protein 1), hematopoietic lineage cell-specific protein 1 (HS1), and similar proteins. These proteins are involved in regulating actin dynamics through direct or indirect interaction with the Arp2/3 complex, which is required to initiate actin polymerization. They all contain at least one C-terminal SH3 domain. Cortactin and HS1 bind Arp2/3 and actin through an N-terminal region that contains an acidic domain and several copies of a repeat domain found in cortactin and HS1. Abp1 binds actin via an N-terminal actin-depolymerizing factor (ADF) homology domain. Yeast Abp1 binds Arp2/3 directly through two acidic domains. Mammalian Abp1 does not directly interact with Arp2/3; instead, it regulates actin dynamics indirectly by interacting with dynamin and WASP family proteins. The C-terminal region of these proteins acts as an adaptor or scaffold that can connect membrane trafficking and signaling proteins that bind the SH3 domain within the actin network. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212753 [Multi-domain] Cd Length: 54 Bit Score: 38.45 E-value: 1.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCL--CSlHGQQGIVPANRVKL 1985
Cdd:cd11819 2 AKALYDYQAAEDNEISFVEGDIITQIEQID----EGWWLgvNA-KGQKGLFPANYVEL 54
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
877-1042 |
1.77e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.13 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 877 EKMVSLLQEKNDLQLQVQAEQdNLNDAEERCDQLIKNKIQLEAKVKEMNERLedeeemnaeltakkRKLEDECSELKRDI 956
Cdd:cd22656 94 AEILELIDDLADATDDEELEE-AKKTIKALLDDLLKEAKKYQDKAAKVVDKL--------------TDFENQTEKDQTAL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 957 DDLELTL-AKVEKEKHATENK-VKNLTEEMAGL-DEIIAKLtkeKKALQEAHQQaLDDLQAEEDKVNTLTKSKVKLEQQV 1033
Cdd:cd22656 159 ETLEKALkDLLTDEGGAIARKeIKDLQKELEKLnEEYAAKL---KAKIDELKAL-IADDEAKLAAALRLIADLTAADTDL 234
|
....*....
gi 431907173 1034 DDLEGSLEQ 1042
Cdd:cd22656 235 DNLLALIGP 243
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1439-1694 |
1.78e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.48 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1439 DKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTEL--FKLKNAYEESLEHLETFKRENK-NLQEEISDLTEQLGEG 1515
Cdd:pfam05667 243 RKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLssFSGSSTTDTGLTKGSRFTHTEKlQFTNEAPAATSSPPTK 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1516 GKNvheLEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKdEEMEQAKRNHLRVVDSLQt 1595
Cdd:pfam05667 323 VET---EEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQN-EELEKQYKVKKKTLDLLP- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1596 slDAETRSRNEALRVKKKMEgDLNEMEIQLSQANRTASEAQKHLKIAQA-HLKDTQLQMDDAVRANDDLKENIAIVERRN 1674
Cdd:pfam05667 398 --DAEENIAKLQALVDASAQ-RLVELAGQWEKHRVPLIEEYRALKEAKSnKEDESQRKLEEIKELREKIKEVAEEAKQKE 474
|
250 260
....*....|....*....|
gi 431907173 1675 NLLQAELEELRAVVEQTERS 1694
Cdd:pfam05667 475 ELYKQLVAEYERLPKDVSRS 494
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
884-1060 |
1.80e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 43.32 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 884 QEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNA---ELTAKKRKLEDECSELKRDIDDLE 960
Cdd:PRK00106 42 QEAVNLRGKAERDAEHIKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKSerqELKQIESRLTERATSLDRKDENLS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 961 LTLAKVEKEKHATENKVKNLTEEmaglDEIIAKLTKEKkalqEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSL 1040
Cdd:PRK00106 122 SKEKTLESKEQSLTDKSKHIDER----EEQVEKLEEQK----KAELERVAALSQAEAREIILAETENKLTHEIATRIREA 193
|
170 180
....*....|....*....|....*.
gi 431907173 1041 EQEKKVRMD------LERAKRKLEGD 1060
Cdd:PRK00106 194 EREVKDRSDkmakdlLAQAMQRLAGE 219
|
|
| SH3_Sdc25 |
cd11883 |
Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is ... |
1931-1965 |
1.88e-03 |
|
Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is composed of the Saccharomyces cerevisiae guanine nucleotide exchange factors (GEFs) Sdc25 and Cdc25, and similar proteins. These GEFs regulate Ras by stimulating the GDP/GTP exchange on Ras. Cdc25 is involved in the Ras/PKA pathway that plays an important role in the regulation of metabolism, stress responses, and proliferation, depending on available nutrients and conditions. Proteins in this subfamily contain an N-terminal SH3 domain as well as REM (Ras exchanger motif) and RasGEF domains at the C-terminus. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.
Pssm-ID: 212816 Cd Length: 55 Bit Score: 38.42 E-value: 1.88e-03
10 20 30
....*....|....*....|....*....|....*
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGAGGLDG 1965
Cdd:cd11883 3 VALYDFTPKSKNQLSFKAGDIIYVLNKDPSGWWDG 37
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1049-1263 |
1.90e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 42.74 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1049 DLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQAlalQLQKKLKENQARIeeleeeleaer 1128
Cdd:cd22656 111 ELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEK---ALKDLLTDEGGAI----------- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1129 tARAKVEKLRSDLSRELEEISERLEEAggatsvqIEMNKKREAEfqkmrrdlEEATLQHEATAAALRKKHADSVAELGEQ 1208
Cdd:cd22656 177 -ARKEIKDLQKELEKLNEEYAAKLKAK-------IDELKALIAD--------DEAKLAAALRLIADLTAADTDLDNLLAL 240
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1209 IDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIK-------AKANLEKVSR---TLEDQANEYRT 1263
Cdd:cd22656 241 IGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISkipaailAKLELEKAIEkwnELAEKADKFRQ 305
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1698-1885 |
1.92e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1698 AEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDT-SAHLE 1776
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1777 RMKKNMEQT-----------IKDLQHRLD------EAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAEsvkgmrkS 1839
Cdd:COG3883 94 ALYRSGGSVsyldvllgsesFSDFLDRLSalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAE-------L 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 431907173 1840 ERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQA 1885
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1602-1939 |
1.98e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.59 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1602 RSRNEALRVKKKMEGDLNEMEIQLSQANRTASEAQKhlkiaqahLKDTQLQMDDAVRANDDLKENIAIVERRNnllQAEL 1681
Cdd:pfam07111 49 RGRSLELEGSQALSQQAELISRQLQELRRLEEEVRL--------LRETSLQQKMRLEAQAMELDALAVAEKAG---QAEA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1682 EELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEsdLTQLQSEVEEAVQECRNAEEKAKKAITDAAMM 1761
Cdd:pfam07111 118 EGLRAALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLTQAHEEA--LSSLTSKAEGLEKSLNSLETKRAGEAKQLAEA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1762 AEElkkeqdtsahLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENE-----LEAEQKRNAESVKGM 1836
Cdd:pfam07111 196 QKE----------AELLRKQLSKTQEELEAQVTLVESLRKYVGEQVPPEVHSQTWELERQelldtMQHLQEDRADLQATV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1837 RKSERRIKELTY----QTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLsKFRKVQHELDEAEERADIAESQ 1912
Cdd:pfam07111 266 ELLQVRVQSLTHmlalQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMVQL-KAQDLEHRDSVKQLRGQVAELQ 344
|
330 340
....*....|....*....|....*..
gi 431907173 1913 vNKLRAKSRDigaKAQLARALYDNTAE 1939
Cdd:pfam07111 345 -EQVTSQSQE---QAILQRALQDKAAE 367
|
|
| CENP-Q |
pfam13094 |
CENP-Q, a CENPA-CAD centromere complex subunit; CENP-Q is one of the components that assembles ... |
1007-1111 |
2.05e-03 |
|
CENP-Q, a CENPA-CAD centromere complex subunit; CENP-Q is one of the components that assembles onto the CENPA-nucleosome distal (CAD) centromere. The centromere, which is the basic element of chromosome inheritance, is epigenetically determined in mammals. CENP-A, the centromere-specific histone H3 variant, assembles an array of nucleosomes and it is this that seems to be the prime candidate for specifying centromere identity. CENPA nucleosomes directly recruit a proximal CENPA-nucleosome-associated complex (NAC) comprised of CENP-M, CENP-N and CENP-T, CENP-U(50), CENP-C and CENP-H. Assembly of the CENPA NAC at centromeres is dependent on CENP-M, CENP-N and CENP-T. Additionally, there are seven other subunits which make up the CENPA-nucleosome distal (CAD) centromere, CENP-K, CENP-L, CENP-O, CENP-P, CENP-Q, CENP-R and CENP-S, also assembling on the CENP-A NAC. Fta7 is the equivalent component of the fission yeast Sim4 complex.
Pssm-ID: 432970 [Multi-domain] Cd Length: 159 Bit Score: 41.12 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1007 QALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLE--------RAKRKLEGDLKLTQESiMDLENDKLQL 1078
Cdd:pfam13094 23 KLLDRNKALEAQLSAELHSLELLEEEIEKEEALLESDEEYLEELEknakaearERKEKLKKEHPLLQED-DSGVLSLPEL 101
|
90 100 110
....*....|....*....|....*....|....
gi 431907173 1079 EEKLKKKEFDISQQNSKIEDE-QALALQLQKKLK 1111
Cdd:pfam13094 102 SSDLGLGDTDFSLFDPTLDEElLPLLEQLQKHLE 135
|
|
| SH3_Nck_3 |
cd11767 |
Third Src Homology 3 domain of Nck adaptor proteins; This group contains the third SH3 domain ... |
1930-1985 |
2.06e-03 |
|
Third Src Homology 3 domain of Nck adaptor proteins; This group contains the third SH3 domain of Nck, the first SH3 domain of Caenorhabditis elegans Ced-2 (Cell death abnormality protein 2), and similar domains. Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4), which show partly overlapping functions but also bind distinct targets. Their SH3 domains are involved in recruiting downstream effector molecules, such as the N-WASP/Arp2/3 complex, which when activated induces actin polymerization that results in the production of pedestals, or protrusions of the plasma membrane. The third SH3 domain of Nck appears to prefer ligands with a PxAPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. Ced-2 is a cell corpse engulfment protein that interacts with Ced-5 in a pathway that regulates the activation of Ced-10, a Rac small GTPase.
Pssm-ID: 212701 [Multi-domain] Cd Length: 56 Bit Score: 38.45 E-value: 2.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGAGglDGWCLC-SLHGQQGIVPANRVKL 1985
Cdd:cd11767 2 VVALYPFTGENDEELSFEKGERLEIIEKPEDD--PDWWKArNALGTTGLVPRNYVEV 56
|
|
| SH3_FCHSD2_2 |
cd11894 |
Second Src Homology 3 domain of FCH and double SH3 domains protein 2; FCHSD2 has a domain ... |
1931-1980 |
2.15e-03 |
|
Second Src Homology 3 domain of FCH and double SH3 domains protein 2; FCHSD2 has a domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. It has only been characterized in silico and its function is unknown. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212827 Cd Length: 56 Bit Score: 38.38 E-value: 2.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGAGGlDGWCLCSLHGQQGIVPA 1980
Cdd:cd11894 3 KALYDYEGQTDDELSFPEGAIIRILNKENQDD-DGFWEGEFNGRIGVFPS 51
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1726-1945 |
2.22e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1726 MESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAhLERMKKNMEQTIKDLQHRLDEAEQialkggk 1805
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD-LSEEAKLLLQQLSELESQLAEARA------- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1806 kQLQKLEARVRELENELEAEQKRNAESVkgmrkSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQA 1885
Cdd:COG3206 234 -ELAEAEARLAALRAQLGSGPDALPELL-----QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 431907173 1886 NTNLSK-FRKVQHELDEAEERADIAESQVNKLRAKSRDIGAK----------AQLARALYDNTAESPQELS 1945
Cdd:COG3206 308 QQEAQRiLASLEAELEALQAREASLQAQLAQLEARLAELPELeaelrrlereVEVARELYESLLQRLEEAR 378
|
|
| SH3_SH3RF2_3 |
cd11784 |
Third Src Homology 3 domain of SH3 domain containing ring finger 2; SH3RF2 is also called ... |
1932-1983 |
2.26e-03 |
|
Third Src Homology 3 domain of SH3 domain containing ring finger 2; SH3RF2 is also called POSHER (POSH-eliminating RING protein) or HEPP1 (heart protein phosphatase 1-binding protein). It acts as an anti-apoptotic regulator of the JNK pathway by binding to and promoting the degradation of SH3RF1 (or POSH), a scaffold protein that is required for pro-apoptotic JNK activation. It may also play a role in cardiac functions together with protein phosphatase 1. SH3RF2 contains an N-terminal RING finger domain and three SH3 domains. This model represents the third SH3 domain, located in the middle, of SH3RF2. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212718 Cd Length: 55 Bit Score: 38.22 E-value: 2.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQREGAGGLDGWCLcsLHGQQGIVPANRV 1983
Cdd:cd11784 4 ALHSYSAHRPEELELQKGEGVRVLGKFQEGWLRGLSL--VTGRVGIFPSNYV 53
|
|
| SH3_Bzz1_2 |
cd11778 |
Second Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP ... |
1932-1981 |
2.27e-03 |
|
Second Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP/Las17-interacting protein involved in endocytosis and trafficking to the vacuole. It physically interacts with type I myosins and functions in the early steps of endocytosis. Together with other proteins, it induces membrane scission in yeast. Bzz1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. This model represents the second C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212712 [Multi-domain] Cd Length: 51 Bit Score: 38.25 E-value: 2.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQREGAgglDGWCLCSLHGQQGIVPAN 1981
Cdd:cd11778 4 ALYDYEAQGDDEISIRVGDRIAVIRGDDG---SGWTYGEINGVKGLFPTS 50
|
|
| SH3_Bzz1_1 |
cd11912 |
First Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP ... |
1930-1985 |
2.29e-03 |
|
First Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP/Las17-interacting protein involved in endocytosis and trafficking to the vacuole. It physically interacts with type I myosins and functions in the early steps of endocytosis. Together with other proteins, it induces membrane scission in yeast. Bzz1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. This model represents the first C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212845 [Multi-domain] Cd Length: 55 Bit Score: 38.36 E-value: 2.29e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGAGgldGWCLCSL-HGQQGIVPANRVKL 1985
Cdd:cd11912 2 AKVLYDYTASGDDEVSISEGEEVTVLEPDDGS---GWTKVRNgSGEEGLVPTSYIEI 55
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1369-1798 |
2.32e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 43.30 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1369 EVAQWRTKYETDAIQRTEELEEAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMvdversnaaaaaldKKQRNFDKI 1448
Cdd:pfam06160 71 EAEELNDKYRFKKAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELK--------------DKYRELRKT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1449 LAEWKQKYEESQSELESSQKEARSLSTELFKLKNA--YEESLEHLEtfkrenkNLQEEISDLTEQLGEGGKNVHELEKV- 1525
Cdd:pfam06160 137 LLANRFSYGPAIDELEKQLAEIEEEFSQFEELTESgdYLEAREVLE-------KLEEETDALEELMEDIPPLYEELKTEl 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1526 RKQLEaeklELQSALEEAEAS---LEHeegkiLRAQLEFNQIKAEIERKLAE----KDEEMEQAKRNHLRVVDSLQTSLD 1598
Cdd:pfam06160 210 PDQLE----ELKEGYREMEEEgyaLEH-----LNVDKEIQQLEEQLEENLALlenlELDEAEEALEEIEERIDQLYDLLE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1599 AETRSRNEalrVKKKMEgdlnEMEIQLSQANrtasEAQKHLKIAQAHLKDT-QLQMDDAVRANdDLKENIAIVERRNNLL 1677
Cdd:pfam06160 281 KEVDAKKY---VEKNLP----EIEDYLEHAE----EQNKELKEELERVQQSyTLNENELERVR-GLEKQLEELEKRYDEI 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1678 QAELE-------ELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEavqecRN---A 1747
Cdd:pfam06160 349 VERLEekevaysELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEK-----SNlpgL 423
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 431907173 1748 EEKAKKAITDAAMMAEELKKEqdtsahLERMKKNMEQtikdLQHRLDEAEQ 1798
Cdd:pfam06160 424 PESYLDYFFDVSDEIEDLADE------LNEVPLNMDE----VNRLLDEAQD 464
|
|
| PRK15374 |
PRK15374 |
type III secretion system needle tip complex protein SipB; |
916-1117 |
2.33e-03 |
|
type III secretion system needle tip complex protein SipB;
Pssm-ID: 185272 [Multi-domain] Cd Length: 593 Bit Score: 43.03 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 916 QLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT 995
Cdd:PRK15374 103 QLESRLAVWQAMIESQKEMGIQVSKEFQTALGEAQEATDLYEASIKKTDTAKSVYDAAEKKLTQAQNKLQSLDPADPGYA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 996 KEKKALQEAHQQALDDLQAEEDK----VNTLTKSKVKLEQQvDDLEGSLEQEKKVRMDLERAK---RKLEGDLKLTQESI 1068
Cdd:PRK15374 183 QAEAAVEQAGKEATEAKEALDKAtdatVKAGTDAKAKAEKA-DNILTKFQGTANAASQNQVSQgeqDNLSNVARLTMLMA 261
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 431907173 1069 MDLENDKLQLEEKLKKkefDISQQNSKIEDEQAlalQLQKKLKENQARI 1117
Cdd:PRK15374 262 MFIEIVGKNTEESLQN---DLALFNALQEGRQA---EMEKKSAEFQEET 304
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
926-1155 |
2.33e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.14 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 926 ERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATEnkvKNLTEEM---------AGLDEIIAKLTK 996
Cdd:PRK11637 75 AQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQE---RLLAAQLdaafrqgehTGLQLILSGEES 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 997 EKKALQEAHQQALDdlQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENdkl 1076
Cdd:PRK11637 152 QRGERILAYFGYLN--QARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLES--- 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 431907173 1077 qleeKLKKkefdisqqnskieDEQALAlqlqkKLKENQARIEELEEELEAERTARAKVEklrsdlSRELEEISERLEEA 1155
Cdd:PRK11637 227 ----SLQK-------------DQQQLS-----ELRANESRLRDSIARAEREAKARAERE------AREAARVRDKQKQA 277
|
|
| GGN |
pfam15685 |
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ... |
2001-2242 |
2.38e-03 |
|
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the maturation of sperm and is expressed virtually only in the testis. It is found to be associated with the intracellular membrane, binds with GGNBP1 and may be involved in vesicular trafficking.
Pssm-ID: 434857 [Multi-domain] Cd Length: 668 Bit Score: 43.22 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2001 PAEPGSPYPAPEHSNEDQEVYVVPPPARPCltSESPAGP-----CLPSPdPIYKVPrgsGTQPATpgDALEVYDVPPAAL 2075
Cdd:pfam15685 296 PLAPGAARPLGEVPRAALETEGGEGDGEGC--SGGPAAPasharALPPP-AYTTFP---GSKPKF--DWVSPPDGPERHF 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2076 RVSASG-----PYDTPASFShllarvapqppgedeAPYDVPlaPKPPSELEPDlewEGGREPGPPLYAAPSNLKRASALL 2150
Cdd:pfam15685 368 RFNGAGggigaPRRRAAALS---------------GPWGSP--PPPPGKAHPI---PGPRRPAPALLAPPMFIFPAPTNG 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2151 NLYE----APEELLADGEEGGSDEGIYDVPLLGPETP-PSPEPLGALASNDPDTLALLLARSPPPSHRPRLPSAESLSRR 2225
Cdd:pfam15685 428 EPVRpgppAPQALLPRPPPPTPPATPPPVPPPIPQLPaLQPMPLAAARPPTPRPCPGHGESALAPAPTAPLPPALAADQA 507
|
250
....*....|....*..
gi 431907173 2226 PLPALpvpeapSPSPVP 2242
Cdd:pfam15685 508 PAPAL------AAAPAP 518
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1518-1702 |
2.49e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.41 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1518 NVHELEKVRK-----QLEAEKLelQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKdeemeqakrnhlRVVDS 1592
Cdd:pfam00529 35 LVKEGDRVKAgdvlfQLDPTDY--QAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISR------------QDYDG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1593 LQTSLDAETRSRNEALRVKKKMEGDLNEMEIqLSQAN----RTASEAQKHLKIAQAHLKDTQLQMdDAVRANDDLKENIA 1668
Cdd:pfam00529 101 ATAQLRAAQAAVKAAQAQLAQAQIDLARRRV-LAPIGgisrESLVTAGALVAQAQANLLATVAQL-DQIYVQITQSAAEN 178
|
170 180 190
....*....|....*....|....*....|....
gi 431907173 1669 IVERRNNLLQAELEelravVEQTERSRKLAEQEL 1702
Cdd:pfam00529 179 QAEVRSELSGAQLQ-----IAEAEAELKLAKLDL 207
|
|
| SH3_Intersectin_2 |
cd11837 |
Second Src homology 3 domain (or SH3B) of Intersectin; Intersectins (ITSNs) are adaptor ... |
1930-1985 |
2.59e-03 |
|
Second Src homology 3 domain (or SH3B) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The second SH3 domain (or SH3B) of ITSN1 has been shown to bind WNK and CdGAP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212771 [Multi-domain] Cd Length: 53 Bit Score: 38.12 E-value: 2.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREgagglDGWCLCSLH-GQQGIVPANRVKL 1985
Cdd:cd11837 2 ATALYPWRAKKENHLSFAKGDIITVLEQQ-----EMWWFGELEgGEEGWFPKSYVKE 53
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1170-1454 |
2.75e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.21 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1170 EAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKanlek 1249
Cdd:pfam00038 24 EQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLR----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1250 vsRTLEDQANEYRTKLEEAQRSLNDFttqQAKLQTENGELARQLEEKEALISQLtRGKLSYTQqtedlkRQLEEEGKAKN 1329
Cdd:pfam00038 99 --TSAENDLVGLRKDLDEATLARVDL---EAKIESLKEELAFLKKNHEEEVREL-QAQVSDTQ------VNVEMDAARKL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1330 ALAHALQSarhdcdlLREQYEEeteakaelQRVLSKANSEvAQWRTKYE---TDAIQRTEELEEAK--LQDAEEAVEAVN 1404
Cdd:pfam00038 167 DLTSALAE-------IRAQYEE--------IAAKNREEAE-EWYQSKLEelqQAAARNGDALRSAKeeITELRRTIQSLE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 431907173 1405 AKCSSLEKTKHRLQNEIEDLMvdvERSNAAAAALDKKQRNFDKILAEWKQ 1454
Cdd:pfam00038 231 IELQSLKKQKASLERQLAETE---ERYELQLADYQELISELEAELQETRQ 277
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1382-1792 |
2.82e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1382 IQRTEELEEAKLQDAEEAVEavnakcsslektKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKyeesqs 1461
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKME------------QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQ------ 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1462 elessQKEARSLSTELFKLKNayEESLEHLETFKRENknLQEEISDLTE----QLGEGGKNvhelEKVRKQLEA-EKLEL 1536
Cdd:pfam17380 340 -----ERMAMERERELERIRQ--EERKRELERIRQEE--IAMEISRMRElerlQMERQQKN----ERVRQELEAaRKVKI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1537 QSALEEAEASLEHEEGKILRAQLEfNQIKAEIERKLAEKDEEMEQAKRnhlrvvDSLQTSLDAETRSRNEALRVKKKMEG 1616
Cdd:pfam17380 407 LEEERQRKIQQQKVEMEQIRAEQE-EARQREVRRLEEERAREMERVRL------EEQERQQQVERLRQQEEERKRKKLEL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1617 DLNEMEIQLSQanrtaseaqkhlkiaqahlkdtqlqmddavranddlkeniaivERRNNLLQAELEELRAVVEQTERSRK 1696
Cdd:pfam17380 480 EKEKRDRKRAE-------------------------------------------EQRRKILEKELEERKQAMIEEERKRK 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1697 LAEQELIEtservqllhSQNTSLINQKKKMESDLTQLQSEVEEavqecrnaeekaKKAITDAAMMAEELKKEQDTsahLE 1776
Cdd:pfam17380 517 LLEKEMEE---------RQKAIYEEERRREAEEERRKQQEMEE------------RRRIQEQMRKATEERSRLEA---ME 572
|
410
....*....|....*.
gi 431907173 1777 RMKKNMEQTIKDLQHR 1792
Cdd:pfam17380 573 REREMMRQIVESEKAR 588
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1468-1649 |
2.85e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1468 KEARSLSTE-LFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQ--------- 1537
Cdd:PHA02562 205 EEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQkvikmyekg 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1538 -------SALEEAEASLEHEEGKILRAQLEFNQIKAEIErKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRV 1610
Cdd:PHA02562 285 gvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAID-ELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKV 363
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 431907173 1611 KKKME----------GDLNEMEIQLSQANRTASEAQK---HLKIAQAHLKDT 1649
Cdd:PHA02562 364 KAAIEelqaefvdnaEELAKLQDELDKIVKTKSELVKekyHRGIVTDLLKDS 415
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1722-1942 |
2.85e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1722 QKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDaammAEELKKEQDTSahlermkknmEQTIKDLQHRLDEAEqial 1801
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEE----YNELQAELEAL----------QAEIDKLQAEIAEAE---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1802 kggkkqlQKLEARVRELENELEAEQKR-----------NAES-------VKGMRKSERRIKELTYQTEEDKKNLLRLQDL 1863
Cdd:COG3883 79 -------AEIEERREELGERARALYRSggsvsyldvllGSESfsdfldrLSALSKIADADADLLEELKADKAELEAKKAE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 431907173 1864 VDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKAQLARALYDNTAESPQ 1942
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
875-1112 |
2.90e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.99 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 875 LEEKMVSLLQEKNDLQLqVQAEQDNLNDAEERcdqlIKNKIQLEAKVKEMNERLEDEeeMNAELTAKKRKLEDECSELKR 954
Cdd:PRK05771 14 LKSYKDEVLEALHELGV-VHIEDLKEELSNER----LRKLRSLLTKLSEALDKLRSY--LPKLNPLREEKKKVSVKSLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 955 DIDDLELTLAKVEKEkhatenkVKNLTEEMAGLDEIIAKLTKEKKALQ--EAHQQALDDLQAEED---KVNTLTKSKVKL 1029
Cdd:PRK05771 87 LIKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYvsvFVGTVPEDKLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1030 EQQVDDLEGSLEQEKK------VRMDLERAKRKLEGDLKLTQESIMDLENDKLqLEEKLKKKEFDISQQNSKIEDeqala 1103
Cdd:PRK05771 160 LKLESDVENVEYISTDkgyvyvVVVVLKELSDEVEEELKKLGFERLELEEEGT-PSELIREIKEELEEIEKERES----- 233
|
....*....
gi 431907173 1104 lqLQKKLKE 1112
Cdd:PRK05771 234 --LLEELKE 240
|
|
| SH3_SH3RF3_1 |
cd11928 |
First Src Homology 3 domain of SH3 domain containing ring finger 3, an E3 ubiquitin-protein ... |
1931-1985 |
2.98e-03 |
|
First Src Homology 3 domain of SH3 domain containing ring finger 3, an E3 ubiquitin-protein ligase; SH3RF3 is also called POSH2 (Plenty of SH3s 2) or SH3MD4 (SH3 multiple domains protein 4). It is a scaffold protein with E3 ubiquitin-protein ligase activity. It was identified in the screen for interacting partners of p21-activated kinase 2 (PAK2). It may play a role in regulating JNK mediated apoptosis in certain conditions. It also interacts with GTP-loaded Rac1. SH3RF3 is highly homologous to SH3RF1; it also contains an N-terminal RING finger domain and four SH3 domains. This model represents the first SH3 domain, located at the N-terminal half, of SH3RF3. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212861 Cd Length: 54 Bit Score: 37.98 E-value: 2.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLrVLQREGAgglDGWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd11928 4 KALYSYEGKEPGDLKFNKGDII-ILRRKVD---ENWYHGELNGCHGFLPASYIQC 54
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1978-2101 |
3.00e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.94 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1978 VPANRVKLLPAGPTPKPSLSQVPPAePGSPYPAPEHSNEDqevyvvPPParpclTSESPAGPCLPSPDPIYKVPRGSGTQ 2057
Cdd:PRK12323 457 APAAAARPAAAGPRPVAAAAAAAPA-RAAPAAAPAPADDD------PPP-----WEELPPEFASPAPAQPDAAPAGWVAE 524
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 431907173 2058 PAT-PGDALEVYDVPPAALRVSASgpyDTPASFSHLLARVAPQPP 2101
Cdd:PRK12323 525 SIPdPATADPDDAFETLAPAPAAA---PAPRAAAATEPVVAPRPP 566
|
|
| SH3_CIP4-like |
cd11911 |
Src Homology 3 domain of Cdc42-Interacting Protein 4; This subfamily is composed of ... |
1930-1985 |
3.02e-03 |
|
Src Homology 3 domain of Cdc42-Interacting Protein 4; This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4), Formin Binding Protein 17 (FBP17), FormiN Binding Protein 1-Like (FNBP1L), and similar proteins. CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. CIP4 and FBP17 bind to the Fas ligand and may be implicated in the inflammatory response. CIP4 may also play a role in phagocytosis. It functions downstream of Cdc42 in PDGF-dependent actin reorganization and cell migration, and also regulates the activity of PDGFRbeta. It uses Src as a substrate in regulating the invasiveness of breast tumor cells. CIP4 may also play a role in the pathogenesis of Huntington's disease. Members of this subfamily typically contain an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain, a central Cdc42-binding HR1 domain, and a C-terminal SH3 domain. The SH3 domain of CIP4 associates with Gapex-5, a Rab31 GEF. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212844 [Multi-domain] Cd Length: 55 Bit Score: 38.01 E-value: 3.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGAgglDGWC-LCSLHGQQGIVPANRVKL 1985
Cdd:cd11911 2 CTALYDFDGTSEGTLSMEEGEILLVLEEDGG---DGWTrVRKNNGDEGYVPTSYIEV 55
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
875-1115 |
3.05e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.21 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 875 LEEKMVSLLQEKNDLQLQVQAEQDN--------LNDAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLE 946
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGAEPSRlyslyekeIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 947 DECSELKRDIDdlELTLAKVEkekhaTENKVKNLTEEMAGL----DEIIAKLTKEkkaLQEAHQQALDDLQAEEDKVNTL 1022
Cdd:pfam00038 103 NDLVGLRKDLD--EATLARVD-----LEAKIESLKEELAFLkknhEEEVRELQAQ---VSDTQVNVEMDAARKLDLTSAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1023 TKSKVKLEQQVDDLEGSLEQEKKVRM-DLERAKRKLEGDLKLTQESIMDL----ENDKLQLEEKLKKKEfdiSQQNSKIE 1097
Cdd:pfam00038 173 AEIRAQYEEIAAKNREEAEEWYQSKLeELQQAAARNGDALRSAKEEITELrrtiQSLEIELQSLKKQKA---SLERQLAE 249
|
250 260
....*....|....*....|.
gi 431907173 1098 DEQALALQL---QKKLKENQA 1115
Cdd:pfam00038 250 TEERYELQLadyQELISELEA 270
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1167-1322 |
3.10e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 43.13 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1167 KKREAEFQKMRRDLEEATLQheATAAALRKKHADS-VAELGEQIDNLqrvkqkleKEKSEFKLElDDVTSNMEQIIKAKA 1245
Cdd:pfam05911 20 EKAEAEALALKQQLESVTLQ--KLTAEERAAHLDGaLKECMQQLRNV--------KEEQEQKIH-DVVLKKTKEWEKIKA 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1246 NLEKvsrtledqaneyrtKLEEAQRSLndfttqqAKLQTENGELARQLEEKEALISQLTRGKLSYTQQTEDLKRQLE 1322
Cdd:pfam05911 89 ELEA--------------KLVETEQEL-------LRAAAENDALSRSLQERENLLMKLSEEKSQAEAEIEALKSRLE 144
|
|
| SH3_p40phox |
cd11869 |
Src Homology 3 domain of the p40phox subunit of NADPH oxidase; p40phox, also called Neutrophil ... |
1930-1986 |
3.11e-03 |
|
Src Homology 3 domain of the p40phox subunit of NADPH oxidase; p40phox, also called Neutrophil cytosol factor 4 (NCF-4), is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) which plays a crucial role in the cellular response to bacterial infection. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p40phox positively regulates NADPH oxidase in both phosphatidylinositol-3-phosphate (PI3P)-dependent and PI3P-independent manner. It contains an N-terminal PX domain, a central SH3 domain, and a C-terminal PB1 domain that interacts with p67phox. The SH3 domain of p40phox binds to canonical polyproline and noncanonical motifs at the C-terminus of p47phox. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212802 Cd Length: 54 Bit Score: 37.86 E-value: 3.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGAGGLDGwclcSLHGQQGIVPANRVKLL 1986
Cdd:cd11869 2 AEALFDFTGNSKLELNFKAGDVIFLLSRVNKDWLEG----TVRGATGIFPLSFVKII 54
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
854-1082 |
3.12e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.92 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 854 MKEEFGRLKETLEKSEARRK----ELEEKMVSLLQEKND------LQLQVQAEQDNLNDAEeRCDQLIKNKIQLEAKVKE 923
Cdd:PLN03229 484 LQERLENLREEFSKANSQDQlmhpVLMEKIEKLKDEFNKrlsrapNYLSLKYKLDMLNEFS-RAKALSEKKSKAEKLKAE 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 924 MNERLEdEEEMNAELTAKKRKLEDECSELK-RDIDDL-ELTLAKVEKEKHATENKVKNLTEEMaGLDEIIAKltkeKKAL 1001
Cdd:PLN03229 563 INKKFK-EVMDRPEIKEKMEALKAEVASSGaSSGDELdDDLKEKVEKMKKEIELELAGVLKSM-GLEVIGVT----KKNK 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1002 QEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKkvrmdLERAKRKLEGDLKlTQESIMDLENdklQLEEK 1081
Cdd:PLN03229 637 DTAEQTPPPNLQEKIESLNEEINKKIERVIRSSDLKSKIELLK-----LEVAKASKTPDVT-EKEKIEALEQ---QIKQK 707
|
.
gi 431907173 1082 L 1082
Cdd:PLN03229 708 I 708
|
|
| SH3_Abp1_fungi_C2 |
cd11961 |
Second C-terminal Src homology 3 domain of Fungal Actin-binding protein 1; Abp1 is an adaptor ... |
1930-1985 |
3.12e-03 |
|
Second C-terminal Src homology 3 domain of Fungal Actin-binding protein 1; Abp1 is an adaptor protein that functions in receptor-mediated endocytosis and vesicle trafficking. It contains an N-terminal actin-binding module, the actin-depolymerizing factor (ADF) homology domain, a central proline-rich region, and a C-terminal SH3 domain (many yeast Abp1 proteins contain two C-terminal SH3 domains). Yeast Abp1 also contains two acidic domains that bind directly to the Arp2/3 complex, which is required to initiate actin polymerization. The SH3 domain of yeast Abp1 binds and localizes the kinases, Ark1p and Prk1p, which facilitate actin patch disassembly following vesicle internalization. It also mediates the localization to the actin patch of the synaptojanin-like protein, Sjl2p, which plays a key role in endocytosis. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212894 [Multi-domain] Cd Length: 53 Bit Score: 37.89 E-value: 3.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSLHGQQGIVPANRVKL 1985
Cdd:cd11961 2 AKALYDYDAAEDNELSFFENDKIINIEFVD----DDWWLGECHGSRGLFPSNYVEL 53
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1094-1244 |
3.19e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1094 SKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEA----GGATSV-------- 1161
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeqlGNVRNNkeyealqk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1162 QIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQII 1241
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPEL 176
|
...
gi 431907173 1242 KAK 1244
Cdd:COG1579 177 LAL 179
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1128-1336 |
3.21e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1128 RTARAKVEKLRSDLSRELEEISERLEEaggatsvqIEMNKKREA--EFQKMRRDLEEatlqheataaalrkkhadsvaEL 1205
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEAEA--------IKKEALLEAkeEIHKLRNEFEK---------------------EL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1206 GEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLND---FTTQQAKl 1282
Cdd:PRK12704 78 RERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgLTAEEAK- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1283 qtenGELARQLEEKealisqLTRGKLSYTQQTEDlKRQLEEEGKAKNALAHALQ 1336
Cdd:PRK12704 157 ----EILLEKVEEE------ARHEAAVLIKEIEE-EAKEEADKKAKEILAQAIQ 199
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
918-1087 |
3.24e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 918 EAKvKEMNERLEDEEEMNAELTAKKRKLEDEcselkrdiddleltLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLtke 997
Cdd:PRK00409 506 EAK-KLIGEDKEKLNELIASLEELERELEQK--------------AEEAEALLKEAEKLKEELEEKKEKLQEEEDKL--- 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 998 KKALQEAHQQALDDLQAEEDKVntltkskVKLEQQVDDLEGSLEQEKkvrmDLERAKRKLEGDLKLTQESimdlendklQ 1077
Cdd:PRK00409 568 LEEAEKEAQQAIKEAKKEADEI-------IKELRQLQKGGYASVKAH----ELIEARKRLNKANEKKEKK---------K 627
|
170
....*....|
gi 431907173 1078 LEEKLKKKEF 1087
Cdd:PRK00409 628 KKQKEKQEEL 637
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
952-1117 |
3.24e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 41.05 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 952 LKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKAlQEAHQQALDDLQAeedKVNTLTKSKVKLEQ 1031
Cdd:pfam13851 31 LKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN-YEKDKQSLKNLKA---RLKVLEKELKDLKW 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1032 QVDDLEgslEQEKKVRMDLERAKRKLEGDLKLTQESImDLENDKLQ-----LEEKLKKKEFDISQ--QNSKIEDE--QAL 1102
Cdd:pfam13851 107 EHEVLE---QRFEKVERERDELYDKFEAAIQDVQQKT-GLKNLLLEkklqaLGETLEKKEAQLNEvlAAANLDPDalQAV 182
|
170
....*....|....*
gi 431907173 1103 ALQLQKKLKENQARI 1117
Cdd:pfam13851 183 TEKLEDVLESKNQLI 197
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1429-1726 |
3.28e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1429 ERSNAAAAALDKKQRNFDKILAEWKQKyeesQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDL 1508
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQA----REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1509 TEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKI--LRAQLEFNQIK-AEIERKLAEKDEEMEQAKRN 1585
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELkeLEEQLESLQEElAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1586 HLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKE 1665
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 431907173 1666 NIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKM 1726
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| SH3_Amphiphysin |
cd11790 |
Src Homology 3 domain of Amphiphysin and related domains; Amphiphysins function primarily in ... |
1930-1981 |
3.33e-03 |
|
Src Homology 3 domain of Amphiphysin and related domains; Amphiphysins function primarily in endocytosis and other membrane remodeling events. They exist in several isoforms and mammals possess two amphiphysin proteins from distinct genes. Amphiphysin I proteins, enriched in the brain and nervous system, contain domains that bind clathrin, Adaptor Protein complex 2 (AP2), dynamin, and synaptojanin. They function in synaptic vesicle endocytosis. Human autoantibodies to amphiphysin I hinder GABAergic signaling and contribute to the pathogenesis of paraneoplastic stiff-person syndrome. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), are localized in many different tissues and may function in intracellular vesicle trafficking. In skeletal muscle, Bin1 plays a role in the organization and maintenance of the T-tubule network. Mutations in Bin1 are associated with autosomal recessive centronuclear myopathy. Amphiphysins contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. The SH3 domain of amphiphysins bind proline-rich motifs present in binding partners such as dynamin, synaptojanin, and nsP3. It also belongs to a subset of SH3 domains that bind ubiquitin in a site that overlaps with the peptide binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212724 [Multi-domain] Cd Length: 64 Bit Score: 38.08 E-value: 3.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1930 ARALYDNTAESPQELSFRRGDVLRVLQREGAGGLD-GWCLCSLH--GQQGIVPAN 1981
Cdd:cd11790 5 VRATHDYTAEDTDELTFEKGDVILVIPFDDPEEQDeGWLMGVKEstGCRGVFPEN 59
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
1758-1922 |
3.35e-03 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 42.66 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1758 AAMMAEELKKEQDTSAHLERMKKNMEQTikdlQHRLDEAEQI--ALKGGKKQLQKLEARVRELENELEAEQKRNAESVKG 1835
Cdd:PRK10361 28 AQQKAEQLAEREEMVAELSAAKQQITQS----EHWRAECELLnnEVRSLQSINTSLEADLREVTTRMEAAQQHADDKIRQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1836 MRKSERRIKE----LTYQTEE------DKKNLLRLQDLVDKLQLKVKAYKRQAEEA---EEQANTNLSkfrkvqHELDEA 1902
Cdd:PRK10361 104 MINSEQRLSEqfenLANRIFEhsnrrvDEQNRQSLNSLLSPLREQLDGFRRQVQDSfgkEAQERHTLA------HEIRNL 177
|
170 180
....*....|....*....|.
gi 431907173 1903 EE-RADIAESQVNKLRAKSRD 1922
Cdd:PRK10361 178 QQlNAQMAQEAINLTRALKGD 198
|
|
| SH3_Intersectin2_1 |
cd11988 |
First Src homology 3 domain (or SH3A) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor ... |
1931-1984 |
3.40e-03 |
|
First Src homology 3 domain (or SH3A) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The first SH3 domain (or SH3A) of ITSN2 is expected to bind many protein partners, similar to ITSN1 which has been shown to bind Sos1, dynamin1/2, CIN85, c-Cbl, PI3K-C2, SHIP2, N-WASP, and CdGAP, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212921 [Multi-domain] Cd Length: 57 Bit Score: 37.93 E-value: 3.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVlqREGAGGLDGWCLCSLHGQQGIVPANRVK 1984
Cdd:cd11988 5 RALYPFEARNHDEMSFNAGDIIQV--DEKTVGEPGWLYGSFQGNFGWFPCNYVE 56
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1517-1792 |
3.41e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.11 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1517 KNVHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKI---LRAQLEFNQIKAEIERKLAE--KDEEMEQAKRNHLRVVD 1591
Cdd:pfam15905 73 KDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLnaaVREKTSLSASVASLEKQLLEltRVNELLKAKFSEDGTQK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1592 SLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSqanrtasEAQKHLKIAQAHLKDTQLQMDDAVRANDDLKENiaive 1671
Cdd:pfam15905 153 KMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQ-------VTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSE----- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1672 rrNNLLQAELEELRAVVEQTERSRKlaeqeliETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEKA 1751
Cdd:pfam15905 221 --TEKLLEYITELSCVSEQVEKYKL-------DIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEK 291
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 431907173 1752 KKaitdaaMMAEELKKEQDTSAHLERMKKNM---EQTIKDLQHR 1792
Cdd:pfam15905 292 EE------LLREYEEKEQTLNAELEELKEKLtleEQEHQKLQQK 329
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
940-1363 |
3.54e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.87 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 940 AKKRKLEDECSELKRDID---DLELTLAKVE-KEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAE 1015
Cdd:PRK10246 380 EQLRQWQQQLTHAEQKLNalpAITLTLTADEvAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1016 EDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRmDLERAKRKLEG---------------------DLKLTQESIMDLEND 1074
Cdd:PRK10246 460 NAALNEMRQRYKEKTQQLADVKTICEQEARIK-DLEAQRAQLQAgqpcplcgstshpaveayqalEPGVNQSRLDALEKE 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1075 KLQLEEK-----------LKKKEFDISQQNSKIEDEQALALQLQkKLKENQARIEELEEELEAERTARAKVEKLRSDLSR 1143
Cdd:PRK10246 539 VKKLGEEgaalrgqldalTKQLQRDESEAQSLRQEEQALTQQWQ-AVCASLNITLQPQDDIQPWLDAQEEHERQLRLLSQ 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1144 ELEEISERLEEAGGATSVQIEMNKKREAEFQKMRR--------DLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRV 1215
Cdd:PRK10246 618 RHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGyaltlpqeDEEASWLATRQQEAQSWQQRQNELTALQNRIQQLTPL 697
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1216 KQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKVSRTLEDQANEYRTKLEEAQRSLND------FTTQQAKLQT-ENGE 1288
Cdd:PRK10246 698 LETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTalqasvFDDQQAFLAAlLDEE 777
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1289 LARQLEE-KEALISQLTRGKLSYTQQTEDLKR--QLEEEGKAKNALAHALQSARHdcdLLREQYEEETEAKAELQRVL 1363
Cdd:PRK10246 778 TLTQLEQlKQNLENQRQQAQTLVTQTAQALAQhqQHRPDGLDLTVTVEQIQQELA---QLAQQLRENTTRQGEIRQQL 852
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
849-1152 |
3.63e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 42.63 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 849 KEMANMKEEFGRLKETLEKS-----EARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKVKE 923
Cdd:pfam15818 38 QELKWQKETLQNQKETLAKQhkeamAVFKKQLQMKMCALEEEKGKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 924 MnerledEEEMNAELTAKkrkledecselkrdiDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIA---KLTKEKKA 1000
Cdd:pfam15818 118 M------EQKLQLHLLAK---------------EDHHKQLNEIEKYYATITGQFGLVKENHGKLEQNVQeaiQLNKRLSA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1001 LQEAHQQALDDLQAEEDKVNT-LTKSKVKLEQQVDDLEGSL--------EQEKKVRMDLERAKrKLEGDLKLTQESIMDL 1071
Cdd:pfam15818 177 LNKKQESEICSLKKELKKVTSdLIKSKVTCQYKMGEENINLtikeqkfqELQERLNMELELNK-KINEEITHIQEEKQDI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1072 ENDKLQLEEKLKKkefdISQQNSKIEDE--------QALAL--QLQ-KKLKENQAR-IEELEEELEAERTARAKVEKLRs 1139
Cdd:pfam15818 256 IISFQHMQQLLQQ----QTQANTEMEAElkalkennQTLERdnELQrEKVKENEEKfLNLQNEHEKALGTWKKHVEELN- 330
|
330
....*....|...
gi 431907173 1140 dlsRELEEISERL 1152
Cdd:pfam15818 331 ---GEINEIKNEL 340
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
1650-1750 |
3.63e-03 |
|
Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.
Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 40.72 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1650 QLQMDDAVRANDDLKENIAIVE-----------RRNNLL---------QAELEELRAVVEQTERSRKLAEQELIETSERV 1709
Cdd:pfam05266 60 KLQVDDSRSVFESLMESFAELEkhgfdvkapqsRINKLLslkdrqtklLEELKKLEKKIAEEESEKRKLEEEIDELEKKI 139
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 431907173 1710 QLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQECRNAEEK 1750
Cdd:pfam05266 140 LELERQLALAKEKKEAADKEIARLKSEAEKLEQEIQDVELE 180
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
2053-2229 |
3.74e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.56 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2053 GSGTQPATPGDALEVYDVPPAALRVSASGPYDTPASFSHLLARVAP--QPPGEDEAPYDVPLAPKPPSELEPDLEWEGGR 2130
Cdd:PRK12323 369 GGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAaaRAVAAAPARRSPAPEALAAARQASARGPGGAP 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2131 EPGPPLYAAPSNLKRASAllnlyEAPEELLADGEEGGSDEGIYDVPLLGPETPPSPE------PLGALASNDPDTLALLL 2204
Cdd:PRK12323 449 APAPAPAAAPAAAARPAA-----AGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEelppefASPAPAQPDAAPAGWVA 523
|
170 180
....*....|....*....|....*
gi 431907173 2205 ARSPPPSHRPRLPSAESLSRRPLPA 2229
Cdd:PRK12323 524 ESIPDPATADPDDAFETLAPAPAAA 548
|
|
| SH3_Nebulin_family_C |
cd11789 |
C-terminal Src Homology 3 domain of the Nebulin family of proteins; Nebulin family proteins ... |
1931-1985 |
3.94e-03 |
|
C-terminal Src Homology 3 domain of the Nebulin family of proteins; Nebulin family proteins contain multiple nebulin repeats, and may contain an N-terminal LIM domain and/or a C-terminal SH3 domain. They have molecular weights ranging from 34 to 900 kD, depending on the number of nebulin repeats, and they all bind actin. They are involved in the regulation of actin filament architecture and function as stabilizers and scaffolds for cytoskeletal structures with which they associate, such as long actin filaments or focal adhesions. Nebulin family proteins that contain a C-terminal SH3 domain include the giant filamentous protein nebulin, nebulette, Lasp1, and Lasp2. Lasp2, also called LIM-nebulette, is an alternatively spliced variant of nebulette. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212723 [Multi-domain] Cd Length: 55 Bit Score: 37.68 E-value: 3.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1931 RALYDNTAESPQELSFRRGDVLRVLQREGAGGLDGwcLCSLHGQQGIVPANRVKL 1985
Cdd:cd11789 3 RAMYDYAAADDDEVSFQEGDVIINVEIIDDGWMEG--TVQRTGQSGMLPANYVEL 55
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1987-2155 |
4.20e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.67 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1987 PAGPTPKPSLSQVPPAEPGSPYPAPEHSnedqevyvvPPPARPCLTSESPAGPCLPSPDPIYKVPRGSGTQPATPGDAle 2066
Cdd:PRK07764 401 AAAAAPAAAPAPAAAAPAAAAAPAPAAA---------PQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPA-- 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 2067 vydVPPAALRVSASGPydtpasfshllarvAPQPPGEDEAPYDVPLAPKPPSelePDLEWEGGREPGPPLYAAPSNLKRA 2146
Cdd:PRK07764 470 ---PAAAPEPTAAPAP--------------APPAAPAPAAAPAAPAAPAAPA---GADDAATLRERWPEILAAVPKRSRK 529
|
....*....
gi 431907173 2147 SALLNLYEA 2155
Cdd:PRK07764 530 TWAILLPEA 538
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
914-1099 |
4.44e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 914 KIQLEAKVKEMNERLE---DEEEMNAELTAKKRKLE--DECSELKRDiddleltlakVEKEKHATENKVKNLteemagld 988
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKrilEEAKKEAEAIKKEALLEakEEIHKLRNE----------FEKELRERRNELQKL-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 989 eiiakltkEKKALQeaHQQALDDlqaeedKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLkltqESI 1068
Cdd:PRK12704 88 --------EKRLLQ--KEENLDR------KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL----ERI 147
|
170 180 190
....*....|....*....|....*....|....
gi 431907173 1069 MDL--ENDKLQLEEKLKKK-EFDISQQNSKIEDE 1099
Cdd:PRK12704 148 SGLtaEEAKEILLEKVEEEaRHEAAVLIKEIEEE 181
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1194-1418 |
4.51e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1194 LRKKHADSVAELGEQIDNLqrvkqkLEKEKsEFKLELDDVTsnmEQIIKAKANLEKVSRTLedqaNEYRTKLEEAQRSLN 1273
Cdd:PHA02562 207 QRKKNGENIARKQNKYDEL------VEEAK-TIKAEIEELT---DELLNLVMDIEDPSAAL----NKLNTAAAKIKSKIE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1274 DFTtQQAKLQTENGEL---ARQLEEKEALISQLTRGKLSYTQQTEDLKRQLEEEGKAKNALAhALQSARHDcdlLREQYE 1350
Cdd:PHA02562 273 QFQ-KVIKMYEKGGVCptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFN-EQSKKLLE---LKNKIS 347
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 1351 EEteaKAELQRVLSKAnSEVAQWRTKYETDAIQRTEELeeAKLQDAEeavEAVNAKCSSLEKTKHRLQ 1418
Cdd:PHA02562 348 TN---KQSLITLVDKA-KKVKAAIEELQAEFVDNAEEL--AKLQDEL---DKIVKTKSELVKEKYHRG 406
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1530-1773 |
4.66e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1530 EAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIER---KLAEKDEEMEQAKRNhlrvVDSLQTSLDAETRSRNE 1606
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNElqaELEALQAEIDKLQAE----IAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1607 ALRVKKKMEGDLNEMEIQLSQANrtASEAqkhlkIAQAHLkdtqlqMDDAVRANDDLKENIaiverrnNLLQAELEELRA 1686
Cdd:COG3883 91 RARALYRSGGSVSYLDVLLGSES--FSDF-----LDRLSA------LSKIADADADLLEEL-------KADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1687 VVEQTERSRKLAEQELIETSERVQLLHSQNTSLIN----QKKKMESDLTQLQSEVEEAVQECRNAEEKAKKAITDAAMMA 1762
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAqlsaEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250
....*....|.
gi 431907173 1763 EELKKEQDTSA 1773
Cdd:COG3883 231 AAAAAAAAAAA 241
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1496-1935 |
4.76e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1496 RENKNLQEEIS------DLTEQLGEGGKNVHELEKVRKQLEAEKLeLQSALEeAEASLEHEEGKILRAQLEFNQIKAEIE 1569
Cdd:COG3096 239 RENRMTLEAIRvtqsdrDLFKHLITEATNYVAADYMRHANERREL-SERALE-LRRELFGARRQLAEEQYRLVEMARELE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1570 RK-LAEKDEEME-QAKRNHLRVVdslQTsldaetrsrneALRVKKKME---GDLNEMEIQLSQANRTASEAQKHLKIAQA 1644
Cdd:COG3096 317 ELsARESDLEQDyQAASDHLNLV---QT-----------ALRQQEKIEryqEDLEELTERLEEQEEVVEEAAEQLAEAEA 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1645 HLKDTQLQMDDAVRANDDLKENIAIVERRN----NLLQAeLEELRAVVEQTERSRKLAEQELIETSERVQLLHSqntSLI 1720
Cdd:COG3096 383 RLEAAEEEVDSLKSQLADYQQALDVQQTRAiqyqQAVQA-LEKARALCGLPDLTPENAEDYLAAFRAKEQQATE---EVL 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1721 NQKKKMesdltqlqSEVEEAVQECRNAEEKAKKaitdaamMAEELKKEQdtsAHlermkknmeQTIKDL--QHRldeaEQ 1798
Cdd:COG3096 459 ELEQKL--------SVADAARRQFEKAYELVCK-------IAGEVERSQ---AW---------QTARELlrRYR----SQ 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1799 IALKGgkkQLQKLEARVRELENELEAEQKrnaesvkgmrkSERRIKELTYQTEEDkknlLRLQDLVDKLQLKVKAykrQA 1878
Cdd:COG3096 508 QALAQ---RLQQLRAQLAELEQRLRQQQN-----------AERLLEEFCQRIGQQ----LDAAEELEELLAELEA---QL 566
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 431907173 1879 EEAEEQANTNLSKFRKVQHELDEaeeradiaesqvnkLRAKSRDIGAKAQLARALYD 1935
Cdd:COG3096 567 EELEEQAAEAVEQRSELRQQLEQ--------------LRARIKELAARAPAWLAAQD 609
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
1479-1591 |
4.97e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 41.25 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1479 KLKNAYEESLEHL--ETFKRENKN---------LQ--EEISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEA 1545
Cdd:COG4026 91 RMKLPLGHDVEYVdvELVRKEIKNaiiraglksLQniPEYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELRE 170
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 431907173 1546 SLEHEEGKILRAQLEFNQIKAEIERkLAEKDEEMEqaKRNHLRVVD 1591
Cdd:COG4026 171 EYKKLREENSILEEEFDNIKSEYSD-LKSRFEELL--KKRLLEVFS 213
|
|
| SH3_FCHSD_1 |
cd11761 |
First Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of ... |
1932-1985 |
5.00e-03 |
|
First Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of FCH and double SH3 domains protein 1 (FCHSD1) and FCHSD2. These proteins have a common domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. They have only been characterized in silico and their functions remain unknown. This group also includes the insect protein, nervous wreck, which acts as a regulator of synaptic growth signaling. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212695 [Multi-domain] Cd Length: 57 Bit Score: 37.34 E-value: 5.00e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQregAGGLDGWCLC-SLHGQQGIVPANRVKL 1985
Cdd:cd11761 6 VLYSYEAQRPDELTITEGEELEVIE---DGDGDGWVKArNKSGEVGYVPENYLQF 57
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
932-1806 |
5.17e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 932 EEMNAELTAKKRKL--EDECSELKRDIDDLELTLAKVEKEKHATenkVKNLTEEMaglDEIIAKLTKEKKALQ-EAHQQA 1008
Cdd:NF041483 344 EKLVAEAAEKARTVaaEDTAAQLAKAARTAEEVLTKASEDAKAT---TRAAAEEA---ERIRREAEAEADRLRgEAADQA 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1009 LDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQekkVRMDLERAKRKLEGDLKltQESIMDLENDKLQLEEKLKKKEFD 1088
Cdd:NF041483 418 EQLKGAAKDDTKEYRAKTVELQEEARRLRGEAEQ---LRAEAVAEGERIRGEAR--REAVQQIEEAARTAEELLTKAKAD 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1089 ISQQNSKIEDEQalalqlqkklkeNQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATsvqiemnkk 1168
Cdd:NF041483 493 ADELRSTATAES------------ERVRTEAIERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAA--------- 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1169 rEAEFQKMRRDLEEATLQHEATAA-ALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDV-TSNMEQIIKAKAN 1246
Cdd:NF041483 552 -ERAARELREETERAIAARQAEAAeELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETERLrTEAAERIRTLQAQ 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1247 LEKVSRTLEDQA----NEYRTKLEE-AQRSLNDFTTQQAKLQTENGELARQLEEKEALISQLTRgklsyTQQTEDLKRQL 1321
Cdd:NF041483 631 AEQEAERLRTEAaadaSAARAEGENvAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERVG-----TEAAEALAAAQ 705
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1322 EEEGKAKNALAHALQSARHDCDLLREQYEEETE------------AKAELQRVLSKANSEVAQWRTKYETDAIQRTEELE 1389
Cdd:NF041483 706 EEAARRRREAEETLGSARAEADQERERAREQSEellasarkrveeAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVA 785
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1390 EAKLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDV--ERSNAAAAALDKKQRNFD-----KILAEW--KQKYEESQ 1460
Cdd:NF041483 786 GLQEQAEEEIAGLRSAAEHAAERTRTEAQEEADRVRSDAyaERERASEDANRLRREAQEeteaaKALAERtvSEAIAEAE 865
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1461 SELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKN------------LQEEISDLTEQLGEGGKNVHELEKVRKQ 1528
Cdd:NF041483 866 RLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANrirsdaaaqadrLIGEATSEAERLTAEARAEAERLRDEAR 945
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1529 LEAEKLELQSALEE----AEASLEHEEGK------ILRAQLEFNQIKAEIERKLAEKDEEMEQ----AKRNHLRVVDSLQ 1594
Cdd:NF041483 946 AEAERVRADAAAQAeqliAEATGEAERLRaeaaetVGSAQQHAERIRTEAERVKAEAAAEAERlrteAREEADRTLDEAR 1025
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1595 TslDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRTA------SEAQKHLKIAQAHLKDTQLQMDDAVRAN-------- 1660
Cdd:NF041483 1026 K--DANKRRSEAAEQADTLITEAAAEADQLTAKAQEEAlrttteAEAQADTMVGAARKEAERIVAEATVEGNslvekart 1103
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1661 --DDL-----KENIAIVERRNNL---LQAELEEL--RAVVEQTERSR----------KLAEQELIETSERVQLLHSQNTS 1718
Cdd:NF041483 1104 daDELlvgarRDATAIRERAEELrdrITGEIEELheRARRESAEQMKsagercdalvKAAEEQLAEAEAKAKELVSDANS 1183
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1719 -----LINQKKKMESDLTQLQSEVEEAVQEcrnAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQHRL 1793
Cdd:NF041483 1184 easkvRIAAVKKAEGLLKEAEQKKAELVRE---AEKIKAEAEAEAKRTVEEGKRELDV---LVRRREDINAEISRVQDVL 1257
|
970
....*....|...
gi 431907173 1794 DEAEQIALKGGKK 1806
Cdd:NF041483 1258 EALESFEAPSGGG 1270
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
861-1377 |
5.22e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.98 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 861 LKETLEKSEA---RRKELEEKMVSLLQEKNDLQLQ---VQAEQDNLNDAEERCDQLIKNKIQLEAKV---KEMNERLE-- 929
Cdd:pfam05622 2 LSEAQEEKDElaqRCHELDQQVSLLQEEKNSLQQEnkkLQERLDQLESGDDSGTPGGKKYLLLQKQLeqlQEENFRLEta 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 930 -DEEEMNAELtakkrkLEDECSELKRDIDDLEltlakvekekhatenkvkNLTEEMAGL-DEIiakltkekkalqeahqq 1007
Cdd:pfam05622 82 rDDYRIKCEE------LEKEVLELQHRNEELT------------------SLAEEAQALkDEM----------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1008 alDDLQAEEDKVNtltkskvKLEQQVDDLEGSLEqekkvrmDLERAKRKLegdlKLTQESIMDLENDKLQLEEKLKKkef 1087
Cdd:pfam05622 121 --DILRESSDKVK-------KLEATVETYKKKLE-------DLGDLRRQV----KLLEERNAEYMQRTLQLEEELKK--- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1088 disqqnskiedeqalalqlqkklkenqarieeleeeleaERTARAKVEKLRsdlsRELEEISERL-EEAGGATSVQIEMN 1166
Cdd:pfam05622 178 ---------------------------------------ANALRGQLETYK----RQVQELHGKLsEESKKADKLEFEYK 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1167 KKRE-------------AEFQKMRRDLEE---ATLQ--HEATAAALRKKHADSVAELGEQIDNLQrVKQKLEKEKSEfkl 1228
Cdd:pfam05622 215 KLEEklealqkekerliIERDTLRETNEElrcAQLQqaELSQADALLSPSSDPGDNLAAEIMPAE-IREKLIRLQHE--- 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1229 elddvtsnmeqiikAKANLEKVSRTLEDQANEYRTKLEEAQRSLNDFTTQQAKLQTENGELARQLEEkealisqLTRGKL 1308
Cdd:pfam05622 291 --------------NKMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEE-------LQKALQ 349
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1309 SYTQQTED---LKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEETEAK-AELQRVLSKANSEVAQWRTKY 1377
Cdd:pfam05622 350 EQGSKAEDsslLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKiDELQEALRKKDEDMKAMEERY 422
|
|
| SH3_Brk |
cd11847 |
Src homology 3 domain of Brk (Breast tumor kinase) Protein Tyrosine Kinase (PTK), also called ... |
1932-1981 |
5.51e-03 |
|
Src homology 3 domain of Brk (Breast tumor kinase) Protein Tyrosine Kinase (PTK), also called PTK6; Brk is a cytoplasmic (or non-receptor) PTK with limited homology to Src kinases. It has been found to be overexpressed in a majority of breast tumors. It plays roles in normal cell differentiation, proliferation, survival, migration, and cell cycle progression. Brk substrates include RNA-binding proteins (SLM-1/2, Sam68), transcription factors (STAT3/5), and signaling molecules (Akt, paxillin, IRS-4). Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). However, Brk lacks the N-terminal myristoylation site. The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212781 [Multi-domain] Cd Length: 58 Bit Score: 37.15 E-value: 5.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSLHGQ-----QGIVPAN 1981
Cdd:cd11847 4 ALWDFKARGDEELSFQAGDQFRIAERSG----DWWTALKLDRAggvvaQGFVPNN 54
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
869-965 |
5.61e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 39.09 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 869 EARRKELEEKMVSLLQEKNDLQlqvqAEQDNLNDAEERCDQLIKnkiQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDE 948
Cdd:pfam13863 16 DAKREEIERLEELLKQREEELE----KKEQELKEDLIKFDKFLK---ENDAKRRRALKKAEEETKLKKEKEKEIKKLTAQ 88
|
90
....*....|....*..
gi 431907173 949 CSELKRDIDDLELTLAK 965
Cdd:pfam13863 89 IEELKSEISKLEEKLEE 105
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
860-1000 |
5.67e-03 |
|
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.
Pssm-ID: 462986 [Multi-domain] Cd Length: 347 Bit Score: 41.67 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 860 RLKETLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAeercdQLIKNKI-QLEAKVKEMNERLEdeeEMNAEL 938
Cdd:pfam10186 23 ELRVDLARLLSEKDSLKKKVEEALEGKEEGEQLEDNIGNKKLKL-----RLLKSEVaISNERLNEIKDKLD---QLRREI 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 431907173 939 TAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKA 1000
Cdd:pfam10186 95 AEKKKKIEKLRSSLKQRRSDLESASYQLEERRASQLAKLQNSIKRIKQKWTALHSKTAESRS 156
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
845-1042 |
5.72e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 845 AETEKEMANMKE---EFGRLKETLEKSEARRKELEEkmvsllqEKNDLQLQVQAEQDNLNDAEERCDQLIKNKIQLEAKV 921
Cdd:COG4913 671 AELEAELERLDAssdDLAALEEQLEELEAELEELEE-------ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 922 K-EMNERLED--EEEMNAELTAKKRK-LEDECSELKRDIDDLELTLAKVEKE-KHATENKVKNLTEEMAGLDEIIAKLT- 995
Cdd:COG4913 744 RlELRALLEErfAAALGDAVERELREnLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALLDr 823
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 431907173 996 -----------KEKKALQEAHQQALDDLQAEedkvntLTKSKVKLEQQVDDLEGSLEQ 1042
Cdd:COG4913 824 leedglpeyeeRFKELLNENSIEFVADLLSK------LRRAIREIKERIDPLNDSLKR 875
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1677-1771 |
6.10e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1677 LQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEAVQEcrnaEEKAKKAIT 1756
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQE----RKQKRKEIT 222
|
90
....*....|....*
gi 431907173 1757 DAAMMAEELkKEQDT 1771
Cdd:PRK11448 223 DQAAKRLEL-SEEET 236
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1521-1784 |
6.28e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.96 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1521 ELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQlefnqikaeierklaekdeEMEQAKRNHLRVVDSLQTSLDAE 1600
Cdd:PRK10929 31 ELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERAK-------------------QYQQVIDNFPKLSAELRQQLNNE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1601 trsRNEALRVKKKME-GDLNEMEIQLS-----QANRTASEAQKHLKIAQAHLKDTQLQmDDAVRANDDLKENIAIV---- 1670
Cdd:PRK10929 92 ---RDEPRSVPPNMStDALEQEILQVSsqlleKSRQAQQEQDRAREISDSLSQLPQQQ-TEARRQLNEIERRLQTLgtpn 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1671 ----ERRNNLLQAELEELRAVVEQTERSRKLA--EQELIETseRVQLLHSQNTSLINQKKKMESDL-TQLQSEVEEAVQe 1743
Cdd:PRK10929 168 tplaQAQLTALQAESAALKALVDELELAQLSAnnRQELARL--RSELAKKRSQQLDAYLQALRNQLnSQRQREAERALE- 244
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 431907173 1744 crNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQ 1784
Cdd:PRK10929 245 --STELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRMDL 283
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1527-1643 |
6.53e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1527 KQLEAEKlELQSALEEAEASLE-HEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRN 1605
Cdd:PRK12704 32 KIKEAEE-EAKRILEEAKKEAEaIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE 110
|
90 100 110
....*....|....*....|....*....|....*....
gi 431907173 1606 EALRVKKKMEGDLNEMEIQLSQANRTASEAQKHL-KIAQ 1643
Cdd:PRK12704 111 ELEKKEKELEQKQQELEKKEEELEELIEEQLQELeRISG 149
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1501-1683 |
6.74e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1501 LQE---EISDLTEQLGEGGKNVHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKIlraqlefnqikAEIERKLAEKDE 1577
Cdd:COG1579 12 LQEldsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI-----------EEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1578 EMEQAKRNhlRVVDSLQTSLDAETRSRNEAlrvkkkmEGDLNEMEIQLSQANRTASEAQKHLKIAQAHLKDTQLQMDDAV 1657
Cdd:COG1579 81 QLGNVRNN--KEYEALQKEIESLKRRISDL-------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170 180
....*....|....*....|....*.
gi 431907173 1658 ranDDLKENIAIVERRNNLLQAELEE 1683
Cdd:COG1579 152 ---AELEAELEELEAEREELAAKIPP 174
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1661-1923 |
6.79e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1661 DDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMESDLTQLQSEVEEA 1740
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1741 VQECRNAEEKAKKA------ITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAlkggkkqlqKLEAR 1814
Cdd:COG1340 91 REELDELRKELAELnkaggsIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKAL---------EKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1815 VRELENELEAEQKRnaesvkgMRKSERRIKELTYQTEEDKKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRK 1894
Cdd:COG1340 162 LKELRAELKELRKE-------AEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIE 234
|
250 260
....*....|....*....|....*....
gi 431907173 1895 VQHELDEAEEradiaesQVNKLRAKSRDI 1923
Cdd:COG1340 235 LQKELRELRK-------ELKKLRKKQRAL 256
|
|
| T3SSipB |
pfam16535 |
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial ... |
916-1042 |
7.14e-03 |
|
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial proteins that invade human intestinal cells via the type III secretion system translocators. T3SSipB represents the coiled -coil region of the proteins and is shown to be homologous in activity to the pore-forming toxins of other Gram-negative pathogens, such as colicin Ia.
Pssm-ID: 435406 [Multi-domain] Cd Length: 155 Bit Score: 39.56 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 916 QLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKrdiDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIiAKLT 995
Cdd:pfam16535 22 QLESRIAAWKAMQEAQQQKGLELSDEFQTALSEAEEAT---DAYEKAINKLKNAKSKAKAAEKKIDQAQTRLQSL-APDS 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 996 KEKKALQEAHQQA---LDDLQAEE------DKVNTLTKSKVKLEQQVDDLEGSLEQ 1042
Cdd:pfam16535 98 PGKAKLEAAEQQAgikKDALQADRtldkalDAASKLTTKAMAKEKEADDFSAKFQG 153
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1127-1957 |
7.30e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.74 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1127 ERTARAKVEKLRSDLSRELEEISERLEEA-----------GGATSVQIEmNKKREAEFQ--KMRRDLEEATLQHEATAAA 1193
Cdd:NF041483 27 LKTEREKAVQHAEDLGYQVEVLRAKLHEArrslasrpaydGADIGYQAE-QLLRNAQIQadQLRADAERELRDARAQTQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1194 LRKKHADSVAEL-----GEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIikaKANLEKVSRTLEDQANEYRTKLEEA 1268
Cdd:NF041483 106 ILQEHAEHQARLqaelhTEAVQRRQQLDQELAERRQTVESHVNENVAWAEQL---RARTESQARRLLDESRAEAEQALAA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1269 QRSLNDFTTQQAKLQ-TENGELARQleEKEALI-------SQLTRGKLSYTQQTEDLKRQLEEEGKAKN--ALAHALQSA 1338
Cdd:NF041483 183 ARAEAERLAEEARQRlGSEAESARA--EAEAILrrarkdaERLLNAASTQAQEATDHAEQLRSSTAAESdqARRQAAELS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1339 RHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKLQDAEEAVEAVNAKCSSLEKTKHRLQ 1418
Cdd:NF041483 261 RAAEQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQALADAR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1419 NEIEDLMVDVE---RSNAA---AAALDKKQRNFDKILAEwkqkyeesqselesSQKEARSLStelfklKNAYEESLEHLE 1492
Cdd:NF041483 341 AEAEKLVAEAAekaRTVAAedtAAQLAKAARTAEEVLTK--------------ASEDAKATT------RAAAEEAERIRR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1493 TFKRENKNLQEEISDLTEQLGEGGKN---VHELEKVRKQLEAEKLELQSALEEAEASlehEEGKILRAQLEFNQIKaEIE 1569
Cdd:NF041483 401 EAEAEADRLRGEAADQAEQLKGAAKDdtkEYRAKTVELQEEARRLRGEAEQLRAEAV---AEGERIRGEARREAVQ-QIE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1570 RKLAEKDEEMEQAKRNhlrvVDSLQTSLDAET-RSRNEALR----VKKKMEGDLnemeiqlsqaNRTASEAQKHLKIAQA 1644
Cdd:NF041483 477 EAARTAEELLTKAKAD----ADELRSTATAESeRVRTEAIErattLRRQAEETL----------ERTRAEAERLRAEAEE 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1645 HLKDTQLQMDDAVRANDDLKENiAIVERRNNL------LQAELEELRAVVEQT--------ERSRKLAEQEL----IETS 1706
Cdd:NF041483 543 QAEEVRAAAERAARELREETER-AIAARQAEAaeeltrLHTEAEERLTAAEEAladaraeaERIRREAAEETerlrTEAA 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1707 ERVQLLHSQntslinqkkkMESDLTQLQSE-VEEAVQECRNAEEKAKKAITDAAMMAEELKKE-QDTS--------AHLE 1776
Cdd:NF041483 622 ERIRTLQAQ----------AEQEAERLRTEaAADASAARAEGENVAVRLRSEAAAEAERLKSEaQESAdrvraeaaAAAE 691
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1777 RMKKNMEQTIKDLQH----RLDEAEQIaLKGGKKQLQKLEARVRELENELEAEQKR-----NAESVKGMRKSERRIKELT 1847
Cdd:NF041483 692 RVGTEAAEALAAAQEeaarRRREAEET-LGSARAEADQERERAREQSEELLASARKrveeaQAEAQRLVEEADRRATELV 770
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1848 YQTEEDKKNLL-RLQDLVDKLQLKVKAYKRQAEEAEEQANTnlskfrKVQHELD----EAEERADIAESQVNKLRAKSRD 1922
Cdd:NF041483 771 SAAEQTAQQVRdSVAGLQEQAEEEIAGLRSAAEHAAERTRT------EAQEEADrvrsDAYAERERASEDANRLRREAQE 844
|
890 900 910
....*....|....*....|....*....|....*.
gi 431907173 1923 igaKAQLARALYDNT-AESPQELSFRRGDVLRVLQR 1957
Cdd:NF041483 845 ---ETEAAKALAERTvSEAIAEAERLRSDASEYAQR 877
|
|
| SH3_NoxO1_2 |
cd12024 |
Second or C-terminal Src homology 3 domain of NADPH oxidase (Nox) Organizing protein 1; Nox ... |
1937-1980 |
7.44e-03 |
|
Second or C-terminal Src homology 3 domain of NADPH oxidase (Nox) Organizing protein 1; Nox Organizing protein 1 (NoxO1) is a critical regulator of enzyme kinetics of the nonphagocytic NADPH oxidase Nox1, which catalyzes the transfer of electrons from NADPH to molecular oxygen to form superoxide. Nox1 is expressed in colon, stomach, uterus, prostate, and vascular smooth muscle cells. NoxO1 is involved in targeting activator subunits (such as NoxA1) to Nox1. It is co-localized with Nox1 in the membranes of resting cells and directs the subcellular localization of Nox1. NoxO1 contains an N-terminal Phox homology (PX) domain, tandem SH3 domains (N-SH3 and C-SH3), and a C-terminal proline-rich region (PRR). This model characterizes the second SH3 domain (or C-SH3) of NoxO1. The tandem SH3 domains of NoxO1 interact with the PRR of p22phox, which also complexes with Nox1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212957 Cd Length: 53 Bit Score: 36.55 E-value: 7.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 431907173 1937 TAESPQELSFRRGDVLRVLQREGagglDGWCLCSLHGQQGIVPA 1980
Cdd:cd12024 9 EAQKEDELSVPAGVVVEVLQKSD----NGWWLIRYNGRAGYVPS 48
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
862-1184 |
7.63e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.81 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 862 KETLEKSEARRKELE---EKMVSLLQ--EKNDLQLQvQAEQDNLNDAEercdQLIKNKIQLEAKVKEMnerledeeEMNA 936
Cdd:PLN02939 113 NEQQTNSKDGEQLSDfqlEDLVGMIQnaEKNILLLN-QARLQALEDLE----KILTEKEALQGKINIL--------EMRL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 937 ELTAKKRKLedeCSELKRDIDDLELTLAKVEKEkhatenkvknLTEEMAGLDEIIAKLTKEKKALQEAHQQALDD---LQ 1013
Cdd:PLN02939 180 SETDARIKL---AAQEKIHVEILEEQLEKLRNE----------LLIRGATEGLCVHSLSKELDVLKEENMLLKDDiqfLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1014 AEEDKVNTLTKSKVKLEQQVDDLEGSLeqekkvrmdlerakRKLEGDLKLTQESIMDLenDKLQLEEKLKKKEF--DISQ 1091
Cdd:PLN02939 247 AELIEVAETEERVFKLEKERSLLDASL--------------RELESKFIVAQEDVSKL--SPLQYDCWWEKVENlqDLLD 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1092 QNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRsdlsRELEEISERLEEAGGATSVQIEMNKKREA 1171
Cdd:PLN02939 311 RATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVELLQ----QKLKLLEERLQASDHEIHSYIQLYQESIK 386
|
330
....*....|...
gi 431907173 1172 EFQKMRRDLEEAT 1184
Cdd:PLN02939 387 EFQDTLSKLKEES 399
|
|
| SH3_SH3RF_3 |
cd11783 |
Third Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and ... |
1932-1985 |
7.68e-03 |
|
Third Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and similar domains; SH3RF1 (or POSH) and SH3RF3 (or POSH2) are scaffold proteins that function as E3 ubiquitin-protein ligases. They contain an N-terminal RING finger domain and four SH3 domains. This model represents the third SH3 domain, located in the middle of SH3RF1 and SH3RF3, and similar domains. SH3RF1 plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF3 interacts with p21-activated kinase 2 (PAK2) and GTP-loaded Rac1. It may play a role in regulating JNK mediated apoptosis in certain conditions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212717 [Multi-domain] Cd Length: 55 Bit Score: 36.60 E-value: 7.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQRegagGLDGWCL-CSLH-GQQGIVPANRVKL 1985
Cdd:cd11783 4 ALYPYKPQKPDELELRKGEMYTVTEK----CQDGWFKgTSLRtGQSGVFPGNYVQP 55
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
837-996 |
7.98e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 40.84 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 837 KIKPLLKSAETE---KEMANMKEEFGRLKEtlekseaRRKELEEKMVSLLQEKNDLQLQVQAEQDNLNDAEERCDQLIKN 913
Cdd:pfam15294 118 KLEPLNEGGGSAllhMEIERLKEENEKLKE-------RLKTLESQATQALDEKSKLEKALKDLQKEQGAKKDVKSNLKEI 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 914 KiQLEAKVKEMNERLEDEEEMNAELTAkkrKLEDECSELKRDIDDL--ELTLAKVEKEKHATE-NKVKNLTEEMAGLDEI 990
Cdd:pfam15294 191 S-DLEEKMAALKSDLEKTLNASTALQK---SLEEDLASTKHELLKVqeQLEMAEKELEKKFQQtAAYRNMKEMLTKKNEQ 266
|
....*.
gi 431907173 991 IAKLTK 996
Cdd:pfam15294 267 IKELRK 272
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
1989-2123 |
8.25e-03 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 40.91 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431907173 1989 GPTPKPSLSQVPPAEPGSPYPAPEHSNEDQEVyvvPPPARPCLTSESPAGPCLPSPDPIYKVPRGSGTQPATPGDALEVY 2068
Cdd:NF040712 189 DPDFGRPLRPLATVPRLAREPADARPEEVEPA---PAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAA 265
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 431907173 2069 DVPPAALRVSASGPYDTPASFShllARVAPQPPGEDEAPYDVPLAPKPPSELEPD 2123
Cdd:NF040712 266 PAAEPDEATRDAGEPPAPGAAE---TPEAAEPPAPAPAAPAAPAAPEAEEPARPE 317
|
|
| SH3_PRMT2 |
cd11806 |
Src homology 3 domain of Protein arginine N-methyltransferase 2; PRMT2, also called HRMT1L1, ... |
1932-1983 |
8.82e-03 |
|
Src homology 3 domain of Protein arginine N-methyltransferase 2; PRMT2, also called HRMT1L1, belongs to the arginine methyltransferase protein family. It functions as a coactivator to both estrogen receptor alpha (ER-alpha) and androgen receptor (AR), presumably through arginine methylation. The ER-alpha transcription factor is involved in cell proliferation, differentiation, morphogenesis, and apoptosis, and is also implicated in the development and progression of breast cancer. PRMT2 and its variants are upregulated in breast cancer cells and may be involved in modulating the ER-alpha signaling pathway during formation of breast cancer. PRMT2 also plays a role in regulating the function of E2F transcription factors, which are critical cell cycle regulators, by binding to the retinoblastoma gene product (RB). It contains an N-terminal SH3 domain and an AdoMet binding domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212740 [Multi-domain] Cd Length: 53 Bit Score: 36.60 E-value: 8.82e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 431907173 1932 ALYDNTAESPQELSFRRGDVLRVLQREGagglDGWCLCSLHGQQGIVPANRV 1983
Cdd:cd11806 4 AIADFVATDDSQLSFESGDKLLVLRKPS----VDWWWAEHNGCCGYIPASHL 51
|
|
| SH3_RIM-BP_3 |
cd12013 |
Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ... |
1934-1981 |
9.99e-03 |
|
Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212946 Cd Length: 61 Bit Score: 36.59 E-value: 9.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 431907173 1934 YDNTAESPQ-----ELSFRRGDVLRVLqreGAGGLDGWCLCSLHGQQGIVPAN 1981
Cdd:cd12013 8 YDPRESSPNvdaevELSFRAGDIITVF---GEMDEDGFYYGELNGQRGLVPSN 57
|
|
| |
