|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
98-773 |
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: 1459.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITG 177
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 178 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 257
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 258 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDH 337
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 338 AMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKG 417
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 418 QSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMF 497
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 498 VLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPDKKRKY 577
Cdd:cd14927 401 ILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRKY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 578 QAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKKAASFQTVSQL 657
Cdd:cd14927 481 EAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDSTEDPKSGVKEKRKKAASFQTVSQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 658 HKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAI 737
Cdd:cd14927 561 HKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAI 640
|
650 660 670
....*....|....*....|....*....|....*.
gi 1622840248 738 PDDTFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14927 641 PDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
98-773 |
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: 1356.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITG 177
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 178 ESGAGKTVNTKRVIQYFAIVAALGdgpgkKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 257
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASS-----KKKKESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 258 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDH 337
Cdd:cd01377 156 TGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 338 AMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKG 417
Cdd:cd01377 236 AFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 418 QSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMF 497
Cdd:cd01377 316 QNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 498 VLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKP-LGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPrpdKKRK 576
Cdd:cd01377 396 VLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKP---KPKK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 577 YQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGScsteppKSGVKEKRKKAASFQTVSQ 656
Cdd:cd01377 473 SEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEES------GGGGGKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 657 LHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSA 736
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*..
gi 1622840248 737 IPDDtFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd01377 627 IPKG-FDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
98-773 |
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: 1150.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITG 177
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 178 ESGAGKTVNTKRVIQYFAIVAALGDgPGKKAqflatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 257
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIE-SKKKL--------GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 258 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKpELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDH 337
Cdd:cd14929 152 RGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 338 AMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKG 417
Cdd:cd14929 231 AMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 418 QSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMF 497
Cdd:cd14929 311 QNIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 498 VLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPDKKrKY 577
Cdd:cd14929 391 VLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKK-KF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 578 QAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPpkSGVKeKRKKAASFQTVSQL 657
Cdd:cd14929 470 EAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSAIQ--FGEK-KRKKGASFQTVASL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 658 HKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAI 737
Cdd:cd14929 547 HKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTF 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 1622840248 738 PDDTFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14929 627 PKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
99-773 |
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: 1139.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 99 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITGE 178
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 179 SGAGKTVNTKRVIQYFAIVAALGDgPGKKAQflaTKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 258
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGD-LAKKKD---SKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 259 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDHA 338
Cdd:cd14913 158 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 339 MDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQ 418
Cdd:cd14913 238 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 419 SVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFV 498
Cdd:cd14913 318 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 499 LEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPDKKRKyQ 578
Cdd:cd14913 398 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRA-E 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 579 AHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAgscSTEPPKSGVKEKRKKAASFQTVSQLH 658
Cdd:cd14913 477 AHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFA---TADADSGKKKVAKKKGSSFQTVSALF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 659 KENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIP 738
Cdd:cd14913 554 RENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIP 633
|
650 660 670
....*....|....*....|....*....|....*
gi 1622840248 739 DDTFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14913 634 EGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
99-773 |
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: 1076.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 99 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITGE 178
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 179 SGAGKTVNTKRVIQYFAIVAALGDgPGKKAQflaTKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 258
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGD-RSKKDQ---TPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 259 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDHA 338
Cdd:cd14917 158 GKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 339 MDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQ 418
Cdd:cd14917 238 FDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 419 SVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFV 498
Cdd:cd14917 318 NVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 499 LEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRpDKKRKYQ 578
Cdd:cd14917 398 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPR-NIKGKPE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 579 AHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGScstEPPKSGVKEKRKKAASFQTVSQLH 658
Cdd:cd14917 477 AHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGA---DAPIEKGKGKAKKGSSFQTVSALH 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 659 KENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIP 738
Cdd:cd14917 554 RENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 633
|
650 660 670
....*....|....*....|....*....|....*
gi 1622840248 739 DDTFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14917 634 EGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
99-773 |
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: 1056.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 99 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITGE 178
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 179 SGAGKTVNTKRVIQYFAIVAALGDGPGKKaqfLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 258
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAIGDRSKKE---NPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 259 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDHA 338
Cdd:cd14916 159 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 339 MDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQ 418
Cdd:cd14916 239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 419 SVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFV 498
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 499 LEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRpDKKRKYQ 578
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPR-NVKGKQE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 579 AHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSgvKEKRKKAASFQTVSQLH 658
Cdd:cd14916 478 AHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKG--KGGKKKGSSFQTVSALH 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 659 KENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIP 738
Cdd:cd14916 556 RENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 635
|
650 660 670
....*....|....*....|....*....|....*
gi 1622840248 739 DDTFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14916 636 EGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-773 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1055.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 87 EDMAMMTHLNEASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLR 166
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 167 NRDNQSMLITGESGAGKTVNTKRVIQYFAIVAALGDGpgkkaqflatKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSR 246
Cdd:pfam00063 82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSGSA----------GNVGRLEEQILQSNPILEAFGNAKTVRNNNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 247 FGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSmNPYDYHFCSQ-GVITVDN 325
Cdd:pfam00063 152 FGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT-NPKDYHYLSQsGCYTIDG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 326 MNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHP 405
Cdd:pfam00063 231 IDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 406 RVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFT 484
Cdd:pfam00063 311 RIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDvKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 485 NEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIE-KPLGILSILEEECMFPKASDASFRAKLYDNHaGKS 563
Cdd:pfam00063 391 NEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKH 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 564 PNFQQPRPdkkrKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVK- 642
Cdd:pfam00063 469 PHFQKPRL----QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSt 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 643 EKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLY 722
Cdd:pfam00063 545 PKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITF 624
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1622840248 723 TDFRQRYRILNPSAIPDDtFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:pfam00063 625 QEFVQRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
99-773 |
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: 1030.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 99 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITGE 178
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 179 SGAGKTVNTKRVIQYFAIVAALGDgpgKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 258
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGD---KKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 259 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDHA 338
Cdd:cd14923 159 GKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 339 MDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQ 418
Cdd:cd14923 239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 419 SVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFV 498
Cdd:cd14923 319 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 499 LEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPdKKRKYQ 578
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKP-AKGKAE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 579 AHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGscsTEPPKSGVKEK--RKKAASFQTVSQ 656
Cdd:cd14923 478 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAG---AEAGDSGGSKKggKKKGSSFQTVSA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 657 LHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSA 736
Cdd:cd14923 555 VFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASA 634
|
650 660 670
....*....|....*....|....*....|....*..
gi 1622840248 737 IPDDTFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14923 635 IPEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
79-785 |
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: 1020.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 79 NPPRFDLLEDMAMMTHLNEASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVAD 158
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 159 NAYNDMLRNRDNQSMLITGESGAGKTVNTKRVIQYFAivaALGDGPGKKaqflatktgGTLEDQIIEANPAMEAFGNAKT 238
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLA---SVSGSNTEV---------GSVEDQILESNPILEAFGNAKT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 239 LRNDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMnPYDYHFCSQ 318
Cdd:smart00242 149 LRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 319 G-VITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEA-DGTESADKAAYLMGVSSG 396
Cdd:smart00242 228 GgCLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTvKDKEELSNAAELLGVDPE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 397 DLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSF 476
Cdd:smart00242 308 ELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 477 EQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIE-KPLGILSILEEECMFPKASDASFRAKL 555
Cdd:smart00242 388 EQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 556 YDNHaGKSPNFQQPRpdkkRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGScste 635
Cdd:smart00242 467 NQHH-KKHPHFSKPK----KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSN---- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 636 ppksgvKEKRKKaasFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQG 715
Cdd:smart00242 538 ------AGSKKR---FQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAG 608
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 716 FPNRLLYTDFRQRYRILNPSAIPDDTfMDSRKATEKLLGSLDLDHAQYQFGHTKVFFKAGLLGVLEELRD 785
Cdd:smart00242 609 FPYRLPFDEFLQRYRVLLPDTWPPWG-GDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-773 |
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: 1018.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 99 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITGE 178
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 179 SGAGKTVNTKRVIQYFAIVAALGDGpgKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 258
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEK--KKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 259 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDHA 338
Cdd:cd14910 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 339 MDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQ 418
Cdd:cd14910 240 IEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 419 SVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFV 498
Cdd:cd14910 320 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 499 LEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPdKKRKYQ 578
Cdd:cd14910 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKVE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 579 AHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLyenYAGSCSTEPPKSGVKE-KRKKAASFQTVSQL 657
Cdd:cd14910 479 AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALL---FSGAAAAEAEEGGGKKgGKKKGSSFQTVSAL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 658 HKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAI 737
Cdd:cd14910 556 FRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAI 635
|
650 660 670
....*....|....*....|....*....|....*.
gi 1622840248 738 PDDTFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14910 636 PEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
99-773 |
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: 1016.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 99 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITGE 178
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 179 SGAGKTVNTKRVIQYFAIVAALGDGpgKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 258
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEK--KKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 259 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDHA 338
Cdd:cd14915 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 339 MDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQ 418
Cdd:cd14915 240 VDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 419 SVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFV 498
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 499 LEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPdKKRKYQ 578
Cdd:cd14915 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 579 AHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYEnyAGSCSTEPPKSGVKEKRKKAASFQTVSQLH 658
Cdd:cd14915 479 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFS--GGQTAEAEGGGGKKGGKKKGSSFQTVSALF 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 659 KENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIP 738
Cdd:cd14915 557 RENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 636
|
650 660 670
....*....|....*....|....*....|....*
gi 1622840248 739 DDTFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14915 637 EGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
100-773 |
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: 1012.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 100 VLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITGES 179
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 180 GAGKTVNTKRVIQYFAIVAALGDgpgkKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPSG 259
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGE----KKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 260 KLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDHAM 339
Cdd:cd14918 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 340 DILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQS 419
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 420 VEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVL 499
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 500 EQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPdKKRKYQA 579
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKV-VKGKAEA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 580 HFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAgscSTEPPKSGVKEKRKKAASFQTVSQLHK 659
Cdd:cd14918 478 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYA---SAEADSGAKKGAKKKGSSFQTVSALFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 660 ENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPD 739
Cdd:cd14918 555 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPE 634
|
650 660 670
....*....|....*....|....*....|....
gi 1622840248 740 DTFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14918 635 GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
98-773 |
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: 1006.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITG 177
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 178 ESGAGKTVNTKRVIQYFAIVAALGdgpgkKAQFLATktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 257
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTG-----KQSSDGK---GSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 258 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDH 337
Cdd:cd14934 153 TGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 338 AMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKG 417
Cdd:cd14934 233 AFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 418 QSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMF 497
Cdd:cd14934 313 QNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 498 VLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPDKKRKY 577
Cdd:cd14934 393 VLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKGP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 578 QAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENyagscstEPPKSGVKeKRKKAASFQTVSQL 657
Cdd:cd14934 473 EAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKE-------EEAPAGSK-KQKRGSSFMTVSNF 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 658 HKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAI 737
Cdd:cd14934 545 YREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVI 624
|
650 660 670
....*....|....*....|....*....|....*.
gi 1622840248 738 PDDtFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14934 625 PQG-FVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-773 |
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: 1004.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 99 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITGE 178
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 179 SGAGKTVNTKRVIQYFAIVAALGDGpgKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 258
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEK--KKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 259 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDHA 338
Cdd:cd14912 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 339 MDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQ 418
Cdd:cd14912 240 IDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 419 SVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFV 498
Cdd:cd14912 320 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 499 LEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPdKKRKYQ 578
Cdd:cd14912 400 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKV-VKGKAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 579 AHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENyAGSCSTEPPKSGVKE-KRKKAASFQTVSQL 657
Cdd:cd14912 479 AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSG-AQTAEGASAGGGAKKgGKKKGSSFQTVSAL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 658 HKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAI 737
Cdd:cd14912 558 FRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAI 637
|
650 660 670
....*....|....*....|....*....|....*.
gi 1622840248 738 PDDTFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14912 638 PEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
98-773 |
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: 1003.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITG 177
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 178 ESGAGKTVNTKRVIQYFAIVAAlgdgPGKKAQflATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 257
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGA----SKKTDE--AAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 258 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDH 337
Cdd:cd14909 155 TGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 338 AMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKG 417
Cdd:cd14909 235 AFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 418 QSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMF 497
Cdd:cd14909 315 RNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 498 VLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPDKKRKY 577
Cdd:cd14909 395 VLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 578 QAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGscSTEPPKSGVKEKRKKAASFQTVSQL 657
Cdd:cd14909 475 AAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAG--QSGGGEQAKGGRGKKGGGFATVSSA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 658 HKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAI 737
Cdd:cd14909 553 YKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGI 632
|
650 660 670
....*....|....*....|....*....|....*.
gi 1622840248 738 PDDTfmDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14909 633 QGEE--DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
23-1107 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 880.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 23 KVHAIPW-DGKKRVWV--PDEQDAYVEAEVKSEATGGRVTVETKDQKVLTVREaelqpMNPPRFDLLEDMAMMTHLNEAS 99
Cdd:COG5022 7 EVGSGCWiPDEEKGWIwaEIIKEAFNKGKVTEEGKKEDGESVSVKKKVLGNDR-----IKLPKFDGVDDLTELSYLNEPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 100 VLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITGES 179
Cdd:COG5022 82 VLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 180 GAGKTVNTKRVIQYFAIVAAlGDGPGKkaqflatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPSG 259
Cdd:COG5022 162 GAGKTENAKRIMQYLASVTS-SSTVEI----------SSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 260 KLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSmNPYDYHFCSQG-VITVDNMNDGEELIATDHA 338
Cdd:COG5022 231 EICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQ-NPKDYIYLSQGgCDKIDGIDDAKEFKITLDA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 339 MDILGFSVDEKCACYKIVGALLHFGNMKFKqKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQ 418
Cdd:COG5022 310 LKTIGIDEEEQDQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 419 SVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFV 498
Cdd:COG5022 389 NLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 499 LEQEEYKREGIDWVFIDFgLDLQPCIDLIEK--PLGILSILEEECMFPKASDASFRAKLYDN-HAGKSPNFQqprpdKKR 575
Cdd:COG5022 469 LEQEEYVKEGIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFK-----KSR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 576 KYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYagscsteppksgvkEKRKKAASFQTVS 655
Cdd:COG5022 543 FRDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDE--------------ENIESKGRFPTLG 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 656 QLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPS 735
Cdd:COG5022 609 SRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPS 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 736 AIPDDTFM---DSRKATEKLLGSLDLDHAQYQFGHTKVFFKAGLLGVLEELRDQRLAKVLTLLQARSRGRLMRLEYQRLL 812
Cdd:COG5022 689 KSWTGEYTwkeDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQAL 768
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 813 GGRDALFTIQWNIRAFNAVKNWSWMKLFFKMKPLLRSAQAEEELAALRAELRGLRGALaAAEAKRQELEETHVSVTQEKN 892
Cdd:COG5022 769 KRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTI-KREKKLRETEEVEFSLKAEVL 847
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 893 DLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNAdLAARRRKLEDECTELKKDID-----DLELT 967
Cdd:COG5022 848 IQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISS-LKLVNLELESEIIELKKSLSsdlieNLEFK 926
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 968 LAKAEKEKQATEN-KVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLE 1046
Cdd:COG5022 927 TELIARLKKLLNNiDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSK 1006
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622840248 1047 QEKKLRMDTERAKRKLEGDLKLTQESVADATQD---KQQLEEKLKKKDSELSQLSLRVEDEQLL 1107
Cdd:COG5022 1007 QYGALQESTKQLKELPVEVAELQSASKIISSEStelSILKPLQKLKGLLLLENNQLQARYKALK 1070
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
98-773 |
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: 843.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRR-SEAPPHIYAVADNAYNDMLRNRDNQSMLIT 176
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 177 GESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQflatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 256
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSA-------SSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 257 PSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMNPYDYHF----CSQGVITVDNMNDGEEL 332
Cdd:cd00124 154 PTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylNSSGCDRIDGVDDAEEF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 333 IATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREE--QAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVG 410
Cdd:cd00124 234 QELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 411 NEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQF--FIGVLDIAGFEIFEFNSFEQLCINFTNEKL 488
Cdd:cd00124 314 GETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEStsFIGILDIFGFENFEVNSFEQLCINYANEKL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 489 QQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIE-KPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFq 567
Cdd:cd00124 394 QQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFF- 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 568 qprpDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSqnrllatlyenyagscsteppksgvkekrkk 647
Cdd:cd00124 472 ----SKKRKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSG------------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 648 aASFqtvsqlhKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQ 727
Cdd:cd00124 517 -SQF-------RSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLK 588
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1622840248 728 RYRILNPSAIPDDtFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd00124 589 RYRILAPGATEKA-SDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
98-773 |
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: 804.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITG 177
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 178 ESGAGKTVNTKRVIQYFAIVAAL---GDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIH 254
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkGSGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 255 FGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSmNPYDYHFCSQGVITVDNMNDGEELIA 334
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 335 TDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYV 414
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 415 TKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFN 493
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 494 QHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAgKSPNFqqprpdK 573
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS-MHPKF------M 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 574 KRKYQ--AHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVK-EKRKKAAS 650
Cdd:cd14911 473 KTDFRgvADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQfGARTRKGM 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 651 FQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYR 730
Cdd:cd14911 553 FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 632
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1622840248 731 ILNPSAIPDDtFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14911 633 LLTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
98-773 |
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: 785.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITG 177
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 178 ESGAGKTVNTKRVIQYFAIVAALGDGpGKKAQFLatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 257
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKG-RKDHNIP-----GELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 258 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQ-DMLLLSMNpyDYHFCSQGVITVDNMNDGEELIATD 336
Cdd:cd14920 155 TGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKsDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 337 HAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTK 416
Cdd:cd14920 233 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 417 GQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQH 495
Cdd:cd14920 313 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 496 MFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPL---GILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPRpd 572
Cdd:cd14920 393 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPR-- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 573 kKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENY-----AGSCSTEPPKSGVKEKRKK 647
Cdd:cd14920 470 -QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdrivgLDQVTGMTETAFGSAYKTK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 648 AASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQ 727
Cdd:cd14920 549 KGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1622840248 728 RYRILNPSAIPdDTFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14920 629 RYEILTPNAIP-KGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
98-773 |
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: 733.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITG 177
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 178 ESGAGKTVNTKRVIQYFAIVAAlgDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 257
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVAS--SFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 258 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSmNPYDYHFCSQGVITVDNMNDGEELIATDH 337
Cdd:cd14932 159 NGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLE-DYSKYRFLSNGNVTIPGQQDKELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 338 AMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKG 417
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 418 QSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHM 496
Cdd:cd14932 318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 497 FVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPL---GILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPrpdK 573
Cdd:cd14932 398 FILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQ-GNNPKFQKP---K 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 574 KRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENY---------AGSCSTEppkSGVKEK 644
Cdd:cd14932 474 KLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdrivgldkvAGMGESL---HGAFKT 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 645 RKkaASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTD 724
Cdd:cd14932 551 RK--GMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1622840248 725 FRQRYRILNPSAIPDDtFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14932 629 FRQRYEILTPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
99-773 |
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: 719.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 99 SVLHNLRQRYA-RWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITG 177
Cdd:cd01380 2 AVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 178 ESGAGKTVNTKRVIQYFAIVAALGDGpgkkaqflatKTGgtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 257
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG----------ETQ--VEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 258 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGK-KPELQDmLLLSMNPYDYHFCSQGVITVDNMNDGEELIATD 336
Cdd:cd01380 150 NYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAAsLPELKE-LHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 337 HAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTK 416
Cdd:cd01380 229 KALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 417 GQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQF--FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQ 494
Cdd:cd01380 309 PLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhsFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 495 HMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGK-SPNFQQPRPDK 573
Cdd:cd01380 389 HVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 574 KRkyqahFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRllatlyenyagscsteppksgvkekrKKaasfqT 653
Cdd:cd01380 468 TA-----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR--------------------------KK-----T 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 654 VSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILN 733
Cdd:cd01380 512 VGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLL 591
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1622840248 734 PSAipDDTFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd01380 592 PSK--EWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
98-773 |
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: 710.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITG 177
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 178 ESGAGKTVNTKRVIQYFAIVAAlgDGPGKKaqflATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 257
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVAS--SHKGKK----DTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 258 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQ-DMLLLSMNpyDYHFCSQGVITVDNMNDGEELIATD 336
Cdd:cd14921 155 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRsDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 337 HAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTK 416
Cdd:cd14921 233 EAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 417 GQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQH 495
Cdd:cd14921 313 AQTKEQADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 496 MFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPL---GILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPrpd 572
Cdd:cd14921 393 MFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKP--- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 573 KKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYEN---------YAGSCSTEPPKSgvke 643
Cdd:cd14921 469 KQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDvdrivgldqMAKMTESSLPSA---- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 644 KRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYT 723
Cdd:cd14921 545 SKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQ 624
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1622840248 724 DFRQRYRILNPSAIPDDtFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14921 625 EFRQRYEILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
98-773 |
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: 696.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITG 177
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 178 ESGAGKTVNTKRVIQYFAIVAAlgDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 257
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVAS--SHKTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 258 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSmNPYDYHFCSQGVITVDNMNDGEELIATDH 337
Cdd:cd15896 159 NGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLE-NYNNYRFLSNGNVTIPGQQDKDLFTETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 338 AMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKG 417
Cdd:cd15896 238 AFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 418 QSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHM 496
Cdd:cd15896 318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 497 FVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPL---GILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPrpdK 573
Cdd:cd15896 398 FILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKP---K 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 574 KRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEpPKSGVKEK----RKKAA 649
Cdd:cd15896 474 KLKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLD-KVSGMSEMpgafKTRKG 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 650 SFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRY 729
Cdd:cd15896 553 MFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1622840248 730 RILNPSAIPDDtFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd15896 633 EILTPNAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
98-773 |
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: 691.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITG 177
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 178 ESGAGKTVNTKRVIQYFAIVAalgdgpgkkAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 257
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVA---------SSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 258 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSmnPYD-YHFCSQGVITVDNMNDGEELIATD 336
Cdd:cd14919 152 NGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE--PYNkYRFLSNGHVTIPGQQDKDMFQETM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 337 HAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTK 416
Cdd:cd14919 230 EAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 417 GQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQH 495
Cdd:cd14919 310 AQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 496 MFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPL---GILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPrpd 572
Cdd:cd14919 390 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKP--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 573 KKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYEN---------YAGSCSTEPPksGVKE 643
Cdd:cd14919 466 KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriigldqVAGMSETALP--GAFK 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 644 KRKkaASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYT 723
Cdd:cd14919 544 TRK--GMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQ 621
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1622840248 724 DFRQRYRILNPSAIPDDtFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14919 622 EFRQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
98-773 |
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: 684.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITG 177
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 178 ESGAGKTVNTKRVIQYFAIVAALGDG---PGkkaqflatkTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIH 254
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGrkePG---------VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 255 FGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMNPYdYHFCSQGVITVDNmNDGEELIA 334
Cdd:cd14930 152 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 335 TDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYV 414
Cdd:cd14930 230 TLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 415 TKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDtKLPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFF 492
Cdd:cd14930 310 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 493 NQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPL---GILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQP 569
Cdd:cd14930 389 NHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 570 RpdkKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKS---GVKEKRK 646
Cdd:cd14930 468 R---HLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSlgdGPPGGRP 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 647 KAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFR 726
Cdd:cd14930 545 RRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFR 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1622840248 727 QRYRILNPSAIPDDtFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14930 625 QRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
98-773 |
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: 671.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITG 177
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 178 ESGAGKTVNTKRVIQYFAIVAalgdgpGKKAqflatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 257
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAIS------GQHS---------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 258 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMnPYDYHFCSQG-VITVDNMNDGEELIATD 336
Cdd:cd01381 146 NGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGD-ASDYYYLTQGnCLTCEGRDDAAEFADIR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 337 HAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQRE--EQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYV 414
Cdd:cd01381 225 SAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 415 TKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFF---IGVLDIAGFEIFEFNSFEQLCINFTNEKLQQF 491
Cdd:cd01381 305 VSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 492 FNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLI-EKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSpNFQQPr 570
Cdd:cd01381 385 FVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNK-NYLKP- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 571 pdkKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSteppksgvkEKRKKAas 650
Cdd:cd01381 462 ---KSDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGS---------ETRKKS-- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 651 fQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYR 730
Cdd:cd01381 528 -PTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYR 606
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1622840248 731 ILNPSaIPDDTFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd01381 607 VLVPG-IPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
99-773 |
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: 658.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 99 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITGE 178
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 179 SGAGKTVNTKRVIQYFAIVAalGDGPGKkaqflatktGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 258
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVS--GGSESE---------VERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 259 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIATDHA 338
Cdd:cd01378 151 GEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 339 MDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADgTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEY---VT 415
Cdd:cd01378 231 MKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 416 KGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQ-FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQ 494
Cdd:cd01378 310 VPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 495 hmFVL--EQEEYKREGIDWVFIDFgLDLQPCIDLIE-KPLGILSILEEECMFP-KASDASFRAKLydNHAGKSPNFQQPR 570
Cdd:cd01378 390 --LTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL--NQLFSNHPHFECP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 571 PDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYEnyagscstEPPKSGVKeKRKKAAS 650
Cdd:cd01378 465 SGHFELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFP--------EGVDLDSK-KRPPTAG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 651 FQTvsqlhKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYR 730
Cdd:cd01378 536 TKF-----KNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYK 610
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1622840248 731 ILNPSAIPDDTfMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd01378 611 LLSPKTWPAWD-GTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
99-773 |
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: 643.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 99 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITGE 178
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 179 SGAGKTVNTKRVIQYFAIVaalgdgpgkkaqflaTKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 258
Cdd:cd14883 82 SGAGKTETTKLILQYLCAV---------------TNNHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDAS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 259 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKK--PELQDMLLLSmNPYDYHFCSQ-GVITVDNMNDGEELIAT 335
Cdd:cd14883 147 GHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKEKLKLG-EPEDYHYLNQsGCIRIDNINDKKDFDHL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 336 DHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAE-ADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYV 414
Cdd:cd14883 226 RLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 415 TKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQ 494
Cdd:cd14883 306 EIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 495 HMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEK-PLGILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPrpdK 573
Cdd:cd14883 386 YVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKP---D 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 574 KRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATL--YENYAGSCSTEPPKSGVKEKRKKAASF 651
Cdd:cd14883 461 RRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELftYPDLLALTGLSISLGGDTTSRGTSKGK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 652 QTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRI 731
Cdd:cd14883 541 PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLC 620
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1622840248 732 LNPSAIPDDTfMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14883 621 LDPRARSADH-KETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
99-773 |
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: 630.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 99 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYkGKRRSEaPPHIYAVADNAYNDMLRNRDNQSMLITGE 178
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY-RQKLLD-SPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 179 SGAGKTVNTKRVIQYfaiVAALGDGpgkkaqflatktGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 258
Cdd:cd01383 80 SGAGKTETAKIAMQY---LAALGGG------------SSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 259 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMnPYDYHFCSQ-GVITVDNMNDGEELIATDH 337
Cdd:cd01383 145 GKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQsNCLTIDGVDDAKKFHELKE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 338 AMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKG 417
Cdd:cd01383 224 ALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 418 QSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDT-KLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHM 496
Cdd:cd01383 304 LTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 497 FVLEQEEYKREGIDWVFIDFgLDLQPCIDLIE-KPLGILSILEEECMFPKASDASFRAKLyDNHAGKSPNFqqprpdKKR 575
Cdd:cd01383 384 FKLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 576 KYQAhFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSgvkeKRKKAASF-QTV 654
Cdd:cd01383 456 RGGA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASKMLDASRKALPLT----KASGSDSQkQSV 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 655 SQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNP 734
Cdd:cd01383 531 ATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLP 610
|
650 660 670
....*....|....*....|....*....|....*....
gi 1622840248 735 SAIPDDTfmDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd01383 611 EDVSASQ--DPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
98-773 |
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: 596.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLIT 176
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 177 GESGAGKTVNTKRVIQYFAIVAALGDGPGKkaqflatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 256
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGRAVTEGR-----------SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 257 PSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSmNPYDYHFCSQ-GVITVDNMNDGEELIAT 335
Cdd:cd01384 150 DAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLK-DPKQFHYLNQsKCFELDGVDDAEEYRAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 336 DHAMDILGFSVDEKCACYKIVGALLHFGNMKFKqkqreEQAEADGTESADK--------AAYLMGVSSGDLLKGLLHpRV 407
Cdd:cd01384 229 RRAMDVVGISEEEQDAIFRVVAAILHLGNIEFS-----KGEEDDSSVPKDEksefhlkaAAELLMCDEKALEDALCK-RV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 408 RVG-NEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNE 486
Cdd:cd01384 303 IVTpDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 487 KLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIE-KPLGILSILEEECMFPKASDASFRAKLYDNHAGKspn 565
Cdd:cd01384 383 KLQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDH--- 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 566 fqqPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDplneTVVP----IFQKSQNRLLATLYenyagscstePPKSGv 641
Cdd:cd01384 459 ---KRFSKPKLSRTDFTIDHYAGDVTYQTDLFLDKNKD----YVVAehqaLLNASKCPFVAGLF----------PPLPR- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 642 kEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLL 721
Cdd:cd01384 521 -EGTSSSSKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKP 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1622840248 722 YTDFRQRYRILNPSAipDDTFMDSRKATEKLLGSLDLDhaQYQFGHTKVFFK 773
Cdd:cd01384 600 FEEFLDRFGLLAPEV--LKGSDDEKAACKKILEKAGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
98-773 |
0e+00 |
|
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: 569.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLIT 176
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 177 GESGAGKTVNTKRVIQYfaivaaLGDGPGKKAqflatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 256
Cdd:cd01382 81 GESGAGKTESTKYILRY------LTESWGSGA--------GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 257 PSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLsmnpydyhfcsqgVITVDNMNDgeeLIATD 336
Cdd:cd01382 147 EKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLK-------------DPLLDDVGD---FIRMD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 337 HAMDILGFSVDEKCACYKIVGALLHFGNMKFkqkqrEEQAE---------ADGTESADKAAYLMGVSSGDLLKGLLHpRV 407
Cdd:cd01382 211 KAMKKIGLSDEEKLDIFRVVAAVLHLGNIEF-----EENGSdsgggcnvkPKSEQSLEYAAELLGLDQDELRVSLTT-RV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 408 RVGNEYVTKGQS------VEQVVFAVGALAKATYDRLFRWLVSRINQTldtkLPRQ---FFIGVLDIAGFEIFEFNSFEQ 478
Cdd:cd01382 285 MQTTRGGAKGTVikvplkVEEANNARDALAKAIYSKLFDHIVNRINQC----IPFEtssYFIGVLDIAGFEYFEVNSFEQ 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 479 LCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIE-KPLGILSILEEECMFPKASDASFRAKLYD 557
Cdd:cd01382 361 FCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 558 NHAgKSPNFQQPRPDKKRKYQA-----HFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYEnyagsc 632
Cdd:cd01382 440 KHK-NHFRLSIPRKSKLKIHRNlrddeGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFE------ 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 633 STEPPKSGVKEKRKKaASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRIC 712
Cdd:cd01382 513 SSTNNNKDSKQKAGK-LSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLM 591
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622840248 713 RQGFPNRLLYTDFRQRYRILNPSAIPDdtfMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd01382 592 QGGFPSRTSFHDLYNMYKKYLPPKLAR---LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
98-773 |
1.33e-179 |
|
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: 559.78 E-value: 1.33e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLR----NRDNQS 172
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 173 MLITGESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLAT----KTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFG 248
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASeaieQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 249 KFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSmNPYDYHFCSQGVITVDNMND 328
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQ-TPVEYFYLRGECSSIPSCDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 329 GEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGT-ESADKAAYLMGVSSGDLLKGLLHPRV 407
Cdd:cd14890 240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 408 RVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEK 487
Cdd:cd14890 320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 488 LQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIE-KPLGILSILE--EECMFPKASDAS--FRAKLYDNHAGK 562
Cdd:cd14890 400 LQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFItlDDCWRFKGEEANkkFVSQLHASFGRK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 563 S------------PNFQQPRPDKKRkyqaHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLlatlyenyag 630
Cdd:cd14890 479 SgsggtrrgssqhPHFVHPKFDADK----QFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSI---------- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 631 scsteppksgvkekRKKAASFQTVSQLHkenlnKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIR 710
Cdd:cd14890 545 --------------REVSVGAQFRTQLQ-----ELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQ 605
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622840248 711 ICRQGFPNRLLYTDFRQRYRILNPSAIPDDTFMdsrkatEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14890 606 IRQQGFALREEHDSFFYDFQVLLPTAENIEQLV------AVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
98-773 |
1.90e-178 |
|
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: 555.93 E-value: 1.90e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITG 177
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 178 ESGAGKTVNTKRVIQYFAIVAAlgdgpgkkaqflatKTGGtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 257
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAG--------------STNG-VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 258 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMnpyDYHFCSQ-GVITVDNMNDGEELIATD 336
Cdd:cd14872 146 RGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSA---AYGYLSLsGCIEVEGVDDVADFEEVV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 337 HAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESAD---KAAYLMGVSSGDLLKGLLHPRVRVgney 413
Cdd:cd14872 223 LAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDvlkEVATLLGVDAATLEEALTSRLMEI---- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 414 vtKGQ-------SVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTN 485
Cdd:cd14872 299 --KGCdptriplTPAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 486 EKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEK-PLGILSILEEECMFPKASDASFRAKLYDNHAGKSp 564
Cdd:cd14872 377 EKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 565 NFQqprPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYenyagscstePPKSGvKEK 644
Cdd:cd14872 455 TFV---YAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF----------PPSEG-DQK 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 645 RKKAasfqTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTD 724
Cdd:cd14872 521 TSKV----TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHER 596
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1622840248 725 FRQRYRILnPSAIPDDTFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14872 597 FLKRYRFL-VKTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
98-773 |
5.03e-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: 541.67 E-value: 5.03e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLIT 176
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 177 GESGAGKTVNTKRVIQYFAIVAA-LGDGPGKKaqflatktggtledqIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 255
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGgLNDSTIKK---------------IIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 256 GPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSmNPYDYHFcSQGVITVDNMNDGEELIAT 335
Cdd:cd14903 146 DKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSA-NECAYTG-ANKTIKIEGMSDRKHFART 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 336 DHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAE--ADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEY 413
Cdd:cd14903 224 KEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 414 VTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFN 493
Cdd:cd14903 304 YTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 494 QHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSPNFQQPRPDK 573
Cdd:cd14903 384 QDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 574 krkyqAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRK--KAASF 651
Cdd:cd14903 463 -----TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRrgGALTT 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 652 QTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRI 731
Cdd:cd14903 538 TTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1622840248 732 LNPSAipDDTFMDSRKATEKLLGSLDLDH-AQYQFGHTKVFFK 773
Cdd:cd14903 618 FLPEG--RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
98-773 |
1.67e-172 |
|
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: 540.82 E-value: 1.67e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRRSeAPPHIYAVADNAYNDMLRNRDNQSMLIT 176
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPSIS-KSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 177 GESGAGKTVNTKRVIQYFAIVAALgdgpgkkaqflATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF- 255
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSE-----------DIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFs 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 256 --------GPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSG-----------------------KKPELQDML 304
Cdd:cd14888 149 klkskrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAareakntglsyeendeklakgadAKPISIDMS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 305 L-LSMNPYDYHFCSqGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQA---EADG 380
Cdd:cd14888 229 SfEPHLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASC 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 381 TESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFF 459
Cdd:cd14888 308 TDDLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 460 IGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLI-EKPLGILSILE 538
Cdd:cd14888 388 CGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLD 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 539 EECMFPKASDASFRAKLYDNHAGKSpnfqqpRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQN 618
Cdd:cd14888 467 EECFVPGGKDQGLCNKLCQKHKGHK------RFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKN 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 619 RLLATLYENYAGSCSTEPPksgvkEKRKkaasFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLH 698
Cdd:cd14888 541 PFISNLFSAYLRRGTDGNT-----KKKK----FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNE 611
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622840248 699 QLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPsaipddtfmdsrkatekllGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14888 612 QLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN-------------------GEGKKQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
99-773 |
2.30e-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: 536.47 E-value: 2.30e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 99 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITGE 178
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 179 SGAGKTVNTKRVIQYFAivaalgdgpgkkaqFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 258
Cdd:cd01379 82 SGAGKTESANLLVQQLT--------------VLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTST 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 259 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQ-DMLLLSMNPYDYHFCSQGVITVDNMNDG---EELIA 334
Cdd:cd01379 148 GAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDIVNNSgnrEKFEE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 335 TDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQ----AEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVG 410
Cdd:cd01379 228 IEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVTR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 411 NEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL--DTKLP-RQFFIGVLDIAGFEIFEFNSFEQLCINFTNEK 487
Cdd:cd01379 308 GETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASdEPLSIGILDIFGFENFQKNSFEQLCINIANEQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 488 LQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCID-LIEKPLGILSILEEECMFPKASDASFRAKLYDNHagKSPNF 566
Cdd:cd01379 388 IQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--KSKYY 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 567 QQPRPDkkrkyQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLAtlyenyagscsteppksgvkekrk 646
Cdd:cd01379 465 WRPKSN-----ALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR------------------------ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 647 kaasfQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFR 726
Cdd:cd01379 516 -----QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFL 590
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1622840248 727 QRYRILNPSAipDDTFMDSRKATEKLLGSLDLDHaqYQFGHTKVFFK 773
Cdd:cd01379 591 KRYYFLAFKW--NEEVVANRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
98-771 |
3.65e-168 |
|
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: 528.59 E-value: 3.65e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAY------KGKRRSEAPPHIYAVADNAYNDMLRNRD-- 169
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 170 --NQSMLITGESGAGKTVNTKRVIQYFAIVAAlgdgpgKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRF 247
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSS------ATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 248 GKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKP-ELQDMLLLSMNPYDYHFCSQGVITVDNM 326
Cdd:cd14901 155 GKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSdELHALGLTHVEEYKYLNSSQCYDRRDGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 327 NDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAY-LMGVSSGDLLKGLLHP 405
Cdd:cd14901 235 DDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAACdLLGLDMDVLEKTLCTR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 406 RVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLP--RQFFIGVLDIAGFEIFEFNSFEQLCINF 483
Cdd:cd14901 315 EIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 484 TNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgldlqP----CIDLIE-KPLGILSILEEECMFPKASDASFRAKLYDN 558
Cdd:cd14901 395 ANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 559 HAGKSP----NFQQPRpdkkrkyqAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATlyenyagscst 634
Cdd:cd14901 470 LAKHASfsvsKLQQGK--------RQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS----------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 635 eppksgvkekrkkaasfqTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQ 714
Cdd:cd14901 531 ------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRS 592
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622840248 715 GFPNRLLYTDFRQRYRILNPSaIPDDTFMdSRKATEKLLGSLDL------DHAQYQFGHTKVF 771
Cdd:cd14901 593 GYPVRFPHDAFVHTYSCLAPD-GASDTWK-VNELAERLMSQLQHselnieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
98-773 |
1.16e-167 |
|
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: 527.06 E-value: 1.16e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLIT 176
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 177 GESGAGKTVNTKRVIQYFAIVA--ALGDGPGKKAQflatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIH 254
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISqqSLELSLKEKTS--------CVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 255 FGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSmNPYDYHFCSQ-GVITVDNMNDGEELI 333
Cdd:cd14873 153 ICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENYHYLNQsGCVEDKTISDQESFR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 334 ATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFkqkqreeqAEADGTESADK-----AAYLMGVSSGDLLKGLLHPRVR 408
Cdd:cd14873 232 EVITAMEVMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKtalgrSAELLGLDPTQLTDALTQRSMF 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 409 VGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKlpRQF-FIGVLDIAGFEIFEFNSFEQLCINFTNEK 487
Cdd:cd14873 304 LRGEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGK--EDFkSIGILDIFGFENFEVNHFEQFNINYANEK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 488 LQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHAgkspnfQ 567
Cdd:cd14873 382 LQEYFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHA------N 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 568 QPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKk 647
Cdd:cd14873 455 NHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRP- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 648 aasfqTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQ 727
Cdd:cd14873 534 -----TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYK 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1622840248 728 RYRILNPSAIPDDtfmDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14873 609 RYKVLMRNLALPE---DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
98-773 |
9.66e-167 |
|
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: 524.70 E-value: 9.66e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITG 177
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 178 ESGAGKTVNTKRVIQYFAIVAalgdgpgKKAQFLATktggtleDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgP 257
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN-------QRRNNLVT-------EQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-E 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 258 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLsMNPYDYHFCSQG-VITVDNMNDGEELIATD 336
Cdd:cd01387 146 GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGL-QEAEKYFYLNQGgNCEIAGKSDADDFRRLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 337 HAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQRE---EQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEY 413
Cdd:cd01387 225 AAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRER 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 414 VTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFN 493
Cdd:cd01387 305 IFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 494 QHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLI-EKPLGILSILEEECMFPKASDASFRAKLYDNHAgKSPNFQQPRPD 572
Cdd:cd01387 385 KHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHHA-LNELYSKPRMP 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 573 kkrkyQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKKAASFQ 652
Cdd:cd01387 463 -----LPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPRLGKGRFVTMKPRTP 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 653 TVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRIL 732
Cdd:cd01387 538 TVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1622840248 733 NPSAIPDDTFMDSRKATEKLLGSLDLDhAQYQFGHTKVFFK 773
Cdd:cd01387 618 VALKLPRPAPGDMCVSLLSRLCTVTPK-DMYRLGATKVFLR 657
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
98-773 |
9.00e-163 |
|
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: 515.39 E-value: 9.00e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITG 177
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 178 ESGAGKTVNTKRVIQYFAivaalgdgpgkkaqFLATKTGGT-LEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 256
Cdd:cd01385 81 ESGSGKTESTNFLLHHLT--------------ALSQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 257 PSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGkKPELQDMLLLSMNPYDYHFCSQ-GVITVDNMNDGEELIAT 335
Cdd:cd01385 147 ENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAG-ASEEERKELHLKQPEDYHYLNQsDCYTLEGEDEKYEFERL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 336 DHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQK--QREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEY 413
Cdd:cd01385 226 KQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGET 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 414 VTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL----DTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQ 489
Cdd:cd01385 306 LILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 490 QFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIE-KPLGILSILEEECMFPKASDASFRAKlYDNHAGKSPNFQQ 568
Cdd:cd01385 386 YYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 569 PrpdkKRKYQAhFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATL--------------------YENY 628
Cdd:cd01385 464 P----QVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELigidpvavfrwavlraffraMAAF 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 629 AGSCS-----TEPP---------KSGVKEKRKKAASfqTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAF 694
Cdd:cd01385 539 REAGRrraqrTAGHsltlhdrttKSLLHLHKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDE 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 695 LVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIpddtfmDSRKATEK-LLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd01385 617 LVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGL------ISSKEDIKdFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
98-773 |
6.83e-160 |
|
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: 506.22 E-value: 6.83e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTasvVAAYKGKRRSEA-----PPHIYAVADNAYNDMLRNR--- 168
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPlLYD---VPGFDSQRKEEAtasspPPHVFSIAERAYRAMKGVGkgq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 169 -DNQSMLITGESGAGKTVNTKRVIQYFAIVAALGDGPgkKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRF 247
Cdd:cd14892 78 gTPQSIVVSGESGAGKTEASKYIMKYLATASKLAKGA--STSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 248 GKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKpELQDMLLLSMNPYDYHFCSQG-VITVDNM 326
Cdd:cd14892 156 GKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD-ANENAALELTPAESFLFLNQGnCVEVDGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 327 NDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQ--KQREEQAEADGTESADKAAYLMGVSSGDLLKGLLh 404
Cdd:cd14892 235 DDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaDDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLV- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 405 PRVRVGneyvTKGQSVE------QVVFAVGALAKATYDRLFRWLVSRIN-----QTL-----DTKLPRQFFIGVLDIAGF 468
Cdd:cd14892 314 TQTTST----ARGSVLEikltarEAKNALDALCKYLYGELFDWLISRINachkqQTSgvtggAASPTFSPFIGILDIFGF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 469 EIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEK-PLGILSILEEECMFP-KA 546
Cdd:cd14892 390 EIMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKkPLGLLPLLEEQMLLKrKT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 547 SDASFRAKLYDNHAGKSPNFQQPRPDKKrkyqaHFEVVHYAGVVPYSIVGWLEKNKDPLnetvvpifqksQNRLLATLye 626
Cdd:cd14892 469 TDKQLLTIYHQTHLDKHPHYAKPRFECD-----EFVLRHYAGDVTYDVHGFLAKNNDNL-----------HDDLRDLL-- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 627 nyagscsteppksgvkEKRKKaasFQTvsqlhkeNLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVL 706
Cdd:cd14892 531 ----------------RSSSK---FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVL 584
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622840248 707 EGIRICRQGFPNRLLYTDFRQRYRIL-------NPSAIPDDTFMDSRKATEKLLGSLDLDhaQYQFGHTKVFFK 773
Cdd:cd14892 585 EVVRIRREGFPIRRQFEEFYEKFWPLarnkagvAASPDACDATTARKKCEEIVARALERE--NFQLGRTKVFLR 656
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
98-773 |
4.54e-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: 486.50 E-value: 4.54e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKR-RSEAPPHIYAVADNAYNDMLRNRDNQSMLIT 176
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 177 GESGAGKTVNTKRVIQYFAivaalgdgpgkkaqFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 256
Cdd:cd14897 81 GESGAGKTESTKYMIKHLM--------------KLSPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 257 PSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSmNPYDYHFCSQGVITVDNMNDGEELiatD 336
Cdd:cd14897 147 ENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLE-DPDCHRILRDDNRNRPVFNDSEEL---E 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 337 H----------AMDILGFSVDEKCACYKIVGALLHFGNMKFkqkqrEEQAEADGTESADK-----AAYLMGVSSGDLLKG 401
Cdd:cd14897 223 YyrqmfhdltnIMKLIGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 402 LLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDtklPRQFF--------IGVLDIAGFEIFEF 473
Cdd:cd14897 298 LISNVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLW---PDKDFqimtrgpsIGILDMSGFENFKI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 474 NSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLI-EKPLGILSILEEECMFPKASDASFR 552
Cdd:cd14897 375 NSFDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLV 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 553 AKLyDNHAGKSPNFQQPRPDkkrkyQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYagsc 632
Cdd:cd14897 454 QKL-NKYCGESPRYVASPGN-----RVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSY---- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 633 steppksgvkekrkkaasfqtvsqlHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRIC 712
Cdd:cd14897 524 -------------------------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIR 578
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622840248 713 RQGFPNRLLYTDFRQRYRILNPSaiPDDTFMDSRKATEKLLGSLDLDhaQYQFGHTKVFFK 773
Cdd:cd14897 579 RDGYPIRIKYEDFVKRYKEICDF--SNKVRSDDLGKCQKILKTAGIK--GYQFGKTKVFLK 635
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
98-773 |
1.05e-145 |
|
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: 467.59 E-value: 1.05e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGK--------RRSEAPPHIYAVADNAYNDMLRNR 168
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 169 DNQSMLITGESGAGKTVNTKRVIQYFAIVAA--------LGDGPGKKAQFLATKTggtLEDQIIEANPAMEAFGNAKTLR 240
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevLTLTSSIRATSKSTKS---IEQKILSCNPILEAFGNAKTVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 241 NDNSSRFGKFIRIHFG-PSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMNPYDYHFCS-- 317
Cdd:cd14907 158 NDNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSGDRYDYlk 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 318 -QGVITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQ--REEQAEADGTESADKAAYLMGVS 394
Cdd:cd14907 238 kSNCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGID 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 395 SGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL------DTKLPRQFF--IGVLDIA 466
Cdd:cd14907 318 EEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekDQQLFQNKYlsIGLLDIF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 467 GFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVF--IDFgLDLQPCIDLIEK-PLGILSILEEECMF 543
Cdd:cd14907 398 GFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 544 PKASDASFRAKLYDNHAGKSpNFQQPRPDKKRKyqahFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLAT 623
Cdd:cd14907 477 ATGTDEKLLNKIKKQHKNNS-KLIFPNKINKDT----FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISS 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 624 LYENYAGSCSTEPPKSGVKEKRKKaasfqTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCN 703
Cdd:cd14907 552 IFSGEDGSQQQNQSKQKKSQKKDK-----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYL 626
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 704 GVLEGIRICRQGFPNRLLYTDFRQRYRILNpsaipddtfmdsrkatekllgsldldhAQYQFGHTKVFFK 773
Cdd:cd14907 627 GVLESIRVRKQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
98-773 |
1.37e-144 |
|
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: 463.75 E-value: 1.37e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYA----RwmIYTYSGLFCVTINPYKWLPvytASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRD---N 170
Cdd:cd14891 1 AGILHNLEERSKldnqR--PYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 171 QSMLITGESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKT----GGTLEDQIIEANPAMEAFGNAKTLRNDNSSR 246
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKrklsVTSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 247 FGKFIRIHFGPSG-KLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSmNPYDYHFCSQ-GVITVD 324
Cdd:cd14891 156 FGKFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLL-SPEDFIYLNQsGCVSDD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 325 NMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKA----AYLMGVSSGDLLK 400
Cdd:cd14891 235 NIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESDKEAlataAELLGVDEEALEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 401 GLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTK---LPrqfFIGVLDIAGFEIFE-FNSF 476
Cdd:cd14891 315 VITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDpdpLP---YIGVLDIFGFESFEtKNDF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 477 EQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLI-EKPLGILSILEEECMFPKASDASFRAKL 555
Cdd:cd14891 392 EQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 556 YDNHAgKSPNFQQPRPDKKRKyqaHFEVVHYAGVVPYSIVGWLEKNKDplnetvvpIFQKSQNRLLATlyenyagscste 635
Cdd:cd14891 471 HKTHK-RHPCFPRPHPKDMRE---MFIVKHYAGTVSYTIGSFIDKNND--------IIPEDFEDLLAS------------ 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 636 ppksgvkekrkkAASFQTVSQlhkenlnKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQG 715
Cdd:cd14891 527 ------------SAKFSDQMQ-------ELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVG 587
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622840248 716 FPNRLLYTDFRQRYRILNPSAI------PDDTFmdsrkaTEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14891 588 LPTRVTYAELVDVYKPVLPPSVtrlfaeNDRTL------TQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
100-773 |
5.70e-142 |
|
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: 457.06 E-value: 5.70e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 100 VLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDML----RNRDNQSMLI 175
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 176 TGESGAGKTVNTKRVIQyfaivaalgdgpgkkaQFLATKTGGT-LEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIH 254
Cdd:cd14889 83 SGESGAGKTESTKLLLR----------------QIMELCRGNSqLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 255 FgPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLsMNPYDYHFCSQGVITVDNMND-GEELI 333
Cdd:cd14889 147 F-RNGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGL-LDPGKYRYLNNGAGCKREVQYwKKKYD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 334 ATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREE-QAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNE 412
Cdd:cd14889 225 EVCNAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 413 YVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLdtkLPRQFF------IGVLDIAGFEIFEFNSFEQLCINFTNE 486
Cdd:cd14889 305 QIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL---APKDDSsvelreIGILDIFGFENFAVNRFEQACINLANE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 487 KLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDL-IEKPLGILSILEEECMFPKASDASFRAKLyDNHAGKSPN 565
Cdd:cd14889 382 QLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSY 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 566 FQqprpdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSG---VK 642
Cdd:cd14889 460 YG-----KSRSKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKlpqAG 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 643 EKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLY 722
Cdd:cd14889 535 SDNFNSTRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSF 614
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1622840248 723 TDFRQRYRIL-NPSAIPDDtfmdsRKATEKLLGSLDLdhAQYQFGHTKVFFK 773
Cdd:cd14889 615 AEFAERYKILlCEPALPGT-----KQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
99-732 |
6.71e-141 |
|
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: 452.84 E-value: 6.71e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 99 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAY-----------KGKRRSEAPPHIYAVADNAYNDMLR 166
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 167 NRD----NQSMLITGESGAGKTVNTKRVIQYFAIVAAlgdgPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRND 242
Cdd:cd14900 82 GLNgvmsDQSILVSGESGSGKTESTKFLMEYLAQAGD----NNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRND 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 243 NSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMlllsmnpydyhfcsqgvit 322
Cdd:cd14900 158 NSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKR------------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 323 vDNMNDgeeliaTDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTE-------SADKAAYLMGVSS 395
Cdd:cd14900 219 -DMYRR------VMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDlapssiwSRDAAATLLSVDA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 396 GDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL-----DTKLPRQFFIGVLDIAGFEI 470
Cdd:cd14900 292 TKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 471 FEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLI-EKPLGILSILEEECMFPKASDA 549
Cdd:cd14900 372 FPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIsQRPTGILSLIDEECVMPKGSDT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 550 SFRAKLYdNHAGKSPNFQQPRPDKKRkyqAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQksqnrllatlyenYA 629
Cdd:cd14900 451 TLASKLY-RACGSHPRFSASRIQRAR---GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFV-------------YG 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 630 GScsteppksgvkekrkkaasfqtvsqlHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGI 709
Cdd:cd14900 514 LQ--------------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAV 567
|
650 660
....*....|....*....|...
gi 1622840248 710 RICRQGFPNRLLYTDFRQRYRIL 732
Cdd:cd14900 568 RVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
98-773 |
5.96e-138 |
|
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: 445.54 E-value: 5.96e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLIT 176
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 177 GESGAGKTVNTKRVIQYFAIVAAlgdgpGKKAQFLAtktggtledQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 256
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG-----GRKDKTIA---------KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 257 PSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSG-KKPELQDMLLLSMNPYDYHFCSQGVITVDNMNDGEELIAT 335
Cdd:cd14904 147 GRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFAST 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 336 DHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGtESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVT 415
Cdd:cd14904 227 QKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNG-SQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 416 KGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQF-FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQ 494
Cdd:cd14904 306 VPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 495 HMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKLYDNHA--GKSPNFQQPRPD 572
Cdd:cd14904 386 DVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQtkKDNESIDFPKVK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 573 KkrkyqAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKKAASFQ 652
Cdd:cd14904 465 R-----TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSETKEGKSGKGTKAPKSLGSQ 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 653 tvsqlHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRIL 732
Cdd:cd14904 540 -----FKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIM 614
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1622840248 733 NPSAIPDDtfmDSRKATEKLLGSLDLDHA-QYQFGHTKVFFK 773
Cdd:cd14904 615 FPPSMHSK---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
853-1930 |
3.36e-135 |
|
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: 451.55 E-value: 3.36e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 853 EEELAALRAELRGLRGALAAAEAKRQELEETHVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSER 932
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 933 LEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQ 1012
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1013 ALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADATQDKQQLEEKLKKKDS 1092
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1093 ELSQLSLRVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGSR 1172
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1173 KREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASA 1252
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1253 EKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSHLLEEKECLISQLSRGKALAAQSLEELRRQLEEESKA 1332
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1333 KSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAiQRTEELEEAKKKLALRLQEAEEGVE 1412
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1413 AANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRLQ 1492
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1493 HSHEEALEALETLKRENKNLQEEISDLTDQLSLSGKSIQELEKAKKALEGEKSEIQAALEEAEGALELEETKTLRIQLEL 1572
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1573 SQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRL 1652
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1653 MQAQLKEEQAGRDEEQRLAAELREQAQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLN 1732
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1733 QKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAAL 1812
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1813 RGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEA 1892
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 1622840248 1893 EQQANTNLAKYRKAQHELDDAEERADMAETQANKLRAR 1930
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
98-735 |
1.17e-134 |
|
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: 438.56 E-value: 1.17e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYK--------GKRRSEAPPHIYAVADNAYNDMLRN- 167
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKPe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 168 RDNQSMLITGESGAGKTVNTKRVIQYFAIVA---ALGDGPGKKAQFLATktggtledQIIEANPAMEAFGNAKTLRNDNS 244
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGrdqSSTEQEGSDAVEIGK--------RILQTNPILESFGNAQTIRNDNS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 245 SRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLS-MNPYDYH---FCSQGV 320
Cdd:cd14902 153 SRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQkGGKYELLnsyGPSFAR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 321 ITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESA---DKAAYLMGVSSGD 397
Cdd:cd14902 233 KRAVADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 398 LLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFF---------IGVLDIAGF 468
Cdd:cd14902 313 LETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSIsdedeelatIGILDIFGF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 469 EIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIE-KPLGILSILEEECMFPKAS 547
Cdd:cd14902 393 ESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 548 DASFRAKLYDNHAGkspnfqqprpdkkrkyQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATL--Y 625
Cdd:cd14902 472 NQALSTKFYRYHGG----------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIgaD 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 626 ENYAGSCSTEPPKSGVKEKRKKAASfqtVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGV 705
Cdd:cd14902 536 ENRDSPGADNGAAGRRRYSMLRAPS---VSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGV 612
|
650 660 670
....*....|....*....|....*....|
gi 1622840248 706 LEGIRICRQGFPNRLLYTDFRQRYRILNPS 735
Cdd:cd14902 613 LEAVRIARHGYSVRLAHASFIELFSGFKCF 642
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
98-773 |
1.95e-134 |
|
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: 436.65 E-value: 1.95e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYK--GKRRS---EAP----PHIYAVADNAYNDMLRN- 167
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 168 RDNQSMLITGESGAGKTVNTKRVIQYfaiVAALGDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRF 247
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLY---LTTLGNGEEGAPNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 248 GKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSG------KKPELQDMLLLSMN-PYDYHFCSQG- 319
Cdd:cd14908 158 GKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGgdeeehEKYEFHDGITGGLQlPNEFHYTGQGg 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 320 VITVDNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAY---LMGVSSG 396
Cdd:cd14908 238 APDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARvakLLGVDVD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 397 DLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQF--FIGVLDIAGFEIFEFN 474
Cdd:cd14908 318 KLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrsSVGVLDIFGFECFAHN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 475 SFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIE-KPLGILSILEEECMFP-KASDASFR 552
Cdd:cd14908 398 SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 553 AKLYDNHAgksPNFQQPRPDKKR-------KYQAHFEVVHYAGVVPYSI-VGWLEKNKDPLNETVVPIFQKSQNrllatl 624
Cdd:cd14908 477 SRLYETYL---PEKNQTHSENTRfeatsiqKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFESGQQ------ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 625 yenyagscsteppksgvkekrkkaasfqtvsqlHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNG 704
Cdd:cd14908 548 ---------------------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGG 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 705 VLEGIRICRQGFPNRLLYTDFRQRYRILNPSaIPDDT---FMDSRKATEKLLGSLDLDHAQY-----------------Q 764
Cdd:cd14908 595 VLEAVRVARSGYPVRLPHKDFFKRYRMLLPL-IPEVVlswSMERLDPQKLCVKKMCKDLVKGvlspamvsmknipedtmQ 673
|
....*....
gi 1622840248 765 FGHTKVFFK 773
Cdd:cd14908 674 LGKSKVFMR 682
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
88-826 |
2.63e-133 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 438.31 E-value: 2.63e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 88 DMAMMTHLNEASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEA-PPHIYAVADNAYNDMLR 166
Cdd:PTZ00014 100 DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDKlPPHVFTTARRALENLHG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 167 NRDNQSMLITGESGAGKTVNTKRVIQYFAivaalgdgPGKKAQflatkTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSR 246
Cdd:PTZ00014 180 VKKSQTIIVSGESGAGKTEATKQIMRYFA--------SSKSGN-----MDLKIQNAIMAANPVLEAFGNAKTIRNNNSSR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 247 FGKFIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDML-LLSMNpyDYHFCSQGVITVDN 325
Cdd:PTZ00014 247 FGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYkLKSLE--EYKYINPKCLDVPG 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 326 MNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEA-----DGTESADKAAYLMGVSSGDLLK 400
Cdd:PTZ00014 325 IDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDAaaisdESLEVFNEACELLFLDYESLKK 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 401 GLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLC 480
Cdd:PTZ00014 405 ELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLF 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 481 INFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLI-EKPLGILSILEEECMFPKASDASFRAKLYDNH 559
Cdd:PTZ00014 485 INITNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLcGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNL 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 560 AgKSPNFQQPRPDKKRKyqahFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYEnyagscsteppks 639
Cdd:PTZ00014 564 K-NNPKYKPAKVDSNKN----FVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFE------------- 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 640 GVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNR 719
Cdd:PTZ00014 626 GVEVEKGKLAKGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYR 705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 720 LLYTDFRQRYRILNPSAIPDDTfMDSRKATEKLLGSLDLDHAQYQFGHTKVFFKAGLLGVLEELRDQRLAKVLTLLQARS 799
Cdd:PTZ00014 706 RTFAEFLSQFKYLDLAVSNDSS-LDPKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAAWEPLVSVLE 784
|
730 740
....*....|....*....|....*...
gi 1622840248 800 rGRLMRLEYQRLLGGR-DALFTIQWNIR 826
Cdd:PTZ00014 785 -ALILKIKKKRKVRKNiKSLVRIQAHLR 811
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
99-773 |
2.38e-125 |
|
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: 412.04 E-value: 2.38e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 99 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTasvVAAYKGKRR--SEAPPHIYAVADNAYNDMLR-------NR 168
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEMPgwTALPPHVFSIAEGAYRSLRRrlhepgaSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 169 DNQSMLITGESGAGKTVNTKRVIQYFAIVAAlgdgpGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFG 248
Cdd:cd14895 79 KNQTILVSGESGAGKTETTKFIMNYLAESSK-----HTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 249 KFIRIHFGP-----SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLL-SMNPYDYHFCSQGVIT 322
Cdd:cd14895 154 KFVRMFFEGheldtSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLeLLSAQEFQYISGGQCY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 323 V--DNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESA---------------- 384
Cdd:cd14895 234 QrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqq 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 385 --DKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINqtldTKLP-RQF--- 458
Cdd:cd14895 314 hlDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVN----SASPqRQFaln 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 459 -----------FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDlQPCIDLI 527
Cdd:cd14895 390 pnkaankdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEML 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 528 E-KPLGILSILEEECMFPKASDASFRAKLYDNHAGKSpNFQQPRPDKKrkyQAHFEVVHYAGVVPYSIVGWLEKNKDPLN 606
Cdd:cd14895 469 EqRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHS-NFSASRTDQA---DVAFQIHHYAGAVRYQAEGFCEKNKDQPN 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 607 ETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKKA--ASFQTVSQLhKENLNKLMTNLRATQPHFVRCIVPNE 684
Cdd:cd14895 545 AELFSVLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSvlSSVGIGSQF-KQQLASLLDVVQQTQTHYIRCIKPND 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 685 NKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTfmdsrkATEKLLGSLDLDHAqyQ 764
Cdd:cd14895 624 ESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDA------TASALIETLKVDHA--E 695
|
....*....
gi 1622840248 765 FGHTKVFFK 773
Cdd:cd14895 696 LGKTRVFLR 704
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
98-773 |
4.41e-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: 409.17 E-value: 4.41e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITG 177
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 178 ESGAGKTVNTKRVIQYFAIvaalgdgpgkkaqfLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgP 257
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSS--------------LYQDQTEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL-Q 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 258 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSmNPYDYHFCSQG-VITVDNMNDGEELIATD 336
Cdd:cd14896 146 HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQ-GPETYYYLNQGgACRLQGKEDAQDFEGLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 337 HAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESAD--KAAYLMGVSSgDLLKGLLHPRVRVGN-EY 413
Cdd:cd14896 225 KALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEihTAARLLQVPP-ERLEGAVTHRVTETPyGR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 414 VTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFF--IGVLDIAGFEIFEFNSFEQLCINFTNEKLQQF 491
Cdd:cd14896 304 VSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 492 FNQHMFVLEQEEYKREGIDWVFIDfGLDLQPCIDLI-EKPLGILSILEEECMFPKASDASFRAKLYDNHaGKSPNFQQPR 570
Cdd:cd14896 384 SSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQ 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 571 ---PDkkrkyqahFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENyagscstEPPKSGVKEKRKK 647
Cdd:cd14896 462 lplPV--------FTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQE-------AEPQYGLGQGKPT 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 648 AAS-FQtvsqlhkENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFR 726
Cdd:cd14896 527 LASrFQ-------QSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFL 599
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1622840248 727 QRYRILNPSAIPDdtFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14896 600 ARFGALGSERQEA--LSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
98-773 |
2.73e-123 |
|
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: 403.98 E-value: 2.73e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKG-KRRSEAPPHIYAVADNAYNDMLRNRDNQSMLIT 176
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 177 GESGAGKTVNTKRVIQYFAivaalgdgpgkkaqflATKTG---GTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 253
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA----------------SAKSGnmdLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 254 HFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDML-LLSMNPYDY--HFCSQgVITVDNMNDGE 330
Cdd:cd14876 145 DVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYhLLGLKEYKFlnPKCLD-VPGIDDVADFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 331 ELIATDHAMdilGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADK-----AAYLMGVSSGDLLKGLLHP 405
Cdd:cd14876 224 EVLESLKSM---GLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVDDAAAISNESLevfkeACSLLFLDPEALKRELTVK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 406 RVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTN 485
Cdd:cd14876 301 VTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 486 EKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCID-LIEKPLGILSILEEECMFPKASDASFRAKLYDNHAGkSP 564
Cdd:cd14876 381 EMLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKS-NG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 565 NFQQPRPDKKRKyqahFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYEnyagscsteppksGVKEK 644
Cdd:cd14876 459 KFKPAKVDSNIN----FIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFE-------------GVVVE 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 645 RKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTD 724
Cdd:cd14876 522 KGKIAKGSLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEE 601
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1622840248 725 FRQRYRILNPSAIPDDTfMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14876 602 FLYQFKFLDLGIANDKS-LDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
98-730 |
7.32e-117 |
|
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: 388.30 E-value: 7.32e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYK-------GKRRSEA---PPHIYAVADNAYNDMLR 166
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhnsqfGDRVTSTdprEPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 167 NRDNQSMLITGESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLA---TKTGGTLEDQIIEANPAMEAFGNAKTLRNDN 243
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISppaSPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 244 SSRFGKFIRIHF-GPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGK----KPELQDMLLLSMNPYDYHFCSQ 318
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 319 GVITV--DNMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQ--KQREEQAEADGTESA---------- 384
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 385 DKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL-------------- 450
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 451 -DTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIE- 528
Cdd:cd14899 401 vDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEh 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 529 KPLGILSILEEECMFPKASDASFRAKLYDNHAGKS--PNFQQPrPDKKRKYQahFEVVHYAGVVPYSIVGWLEKNKDPLN 606
Cdd:cd14899 480 RPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNshPHFRSA-PLIQRTTQ--FVVAHYAGCVTYTIDGFLAKNKDSFC 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 607 ETVVPIFQKSQNRLLATL-----YENYAGSCSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIV 681
Cdd:cd14899 557 ESAAQLLAGSSNPLIQALaagsnDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIK 636
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1622840248 682 PNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYR 730
Cdd:cd14899 637 PNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
98-735 |
2.06e-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: 378.17 E-value: 2.06e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRR-SEAPPHIYAVADNAYNDMLRNRDNQSMLI 175
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 176 TGESGAGKTVNTKRVIQYfaIVAALGDGPGKKAQflATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 255
Cdd:cd14906 81 SGESGSGKTEASKTILQY--LINTSSSNQQQNNN--NNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 256 -GPSGKLASADIDSYLLEKSRvIFQLPGER--SYHVYYQILSGKKPELQDMLLLSMNPYDYHF--CSQGVITV------- 323
Cdd:cd14906 157 rSSDGKIDGASIETYLLEKSR-ISHRPDNInlSYHIFYYLVYGASKDERSKWGLNNDPSKYRYldARDDVISSfksqssn 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 324 --DNMNDGEELIAT----DHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQ---REEQAEADGTESADKAAYLMGVS 394
Cdd:cd14906 236 knSNHNNKTESIESfqllKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 395 SGDLLKGLLHPRVRVGNE--YVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQ-----------FFIG 461
Cdd:cd14906 316 ESVFKQALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNdlaggsnkknnLFIG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 462 VLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIE-KPLGILSILEEE 540
Cdd:cd14906 396 VLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 541 CMFPKASDASFRAKlYDNHAGKSPNFQQPRPDKkrkyqAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRL 620
Cdd:cd14906 475 CIMPKGSEQSLLEK-YNKQYHNTNQYYQRTLAK-----GTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFL 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 621 LATLYENYagscSTEPPKSgvkekRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQL 700
Cdd:cd14906 549 KKSLFQQQ----ITSTTNT-----TKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQL 619
|
650 660 670
....*....|....*....|....*....|....*
gi 1622840248 701 RCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPS 735
Cdd:cd14906 620 RNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
98-771 |
4.18e-113 |
|
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: 375.34 E-value: 4.18e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRRSEA-PPHIYAVADNAYNDMLRNRD--NQSM 173
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQKlKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 174 LITGESGAGKTVNTKRVIQYFAIVAAlgdgpgKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 253
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAA------SPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 254 HFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKK---------PELQDMLLLSmNPydyhfcsqgvitvD 324
Cdd:cd14880 155 QLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASaderlqwhlPEGAAFSWLP-NP-------------E 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 325 NMNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQA---EADGTESADKAAYLMGVSSGDLLKG 401
Cdd:cd14880 221 RNLEEDCFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLET 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 402 LlhpRVRVgneyVTKGQsvEQVVFAV-----------GALAKATYDRLFRWLVSRINQTLDTKLPR-QFFIGVLDIAGFE 469
Cdd:cd14880 301 L---QIRT----IRAGK--QQQVFKKpcsraecdtrrDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 470 IFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIE-KPLGILSILEEECMFPKASD 548
Cdd:cd14880 372 SFPENSLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgSPISICSLINEECRLNRPSS 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 549 ASFRAKLYDNHAGKSPNFQQPRPDKKrkyqAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENY 628
Cdd:cd14880 451 AAQLQTRIESALAGNPCLGHNKLSRE----PSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPAN 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 629 AGSCSTEPPKSgvkekRKKAASFQTVSQLhKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEG 708
Cdd:cd14880 527 PEEKTQEEPSG-----QSRAPVLTVVSKF-KASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVET 600
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622840248 709 IRICRQGFPNRLLYTDFRQRYRILNPSAIPDDTFMDSRKATEKLLGSLdldhaqyQFGHTKVF 771
Cdd:cd14880 601 IHISAAGFPIRVSHQNFVERYKLLRRLRPHTSSGPHSPYPAKGLSEPV-------HCGRTKVF 656
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
98-773 |
2.27e-111 |
|
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: 369.99 E-value: 2.27e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRRS-----EAPPHIYAVADNAYNDMLRNRDNQ 171
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 172 SMLITGESGAGKTVNTKRVIQYFAIVAALGDGPGKKAqflatktggtledqIIEANPAMEAFGNAKTLRNDNSSRFGKFI 251
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSSTDVQSL--------------ILGSNPLLESFGNAKTLRNNNSSRFGKFI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 252 RIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDML-LLSMNPYDYHFCSQgVITVDNMNDGE 330
Cdd:cd14886 147 KLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLgFKSLESYNFLNASK-CYDAPGIDDQK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 331 ELIATDHAMDILgFSVDEKCACYKIVGALLHFGNMKFKQKQR---EEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRV 407
Cdd:cd14886 226 EFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 408 RVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEK 487
Cdd:cd14886 305 VINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANER 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 488 LQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEKP-LGILSILEEECMFPKASDASFRAKLydNHAGKSPNF 566
Cdd:cd14886 385 LQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC--KSKIKNNSF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 567 QqprPDKKRkyQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYagscstePPKSGVKEKRK 646
Cdd:cd14886 462 I---PGKGS--QCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDI-------PNEDGNMKGKF 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 647 KAASFQTvsqlhkeNLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFR 726
Cdd:cd14886 530 LGSTFQL-------SIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFF 602
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1622840248 727 QRYRILNP-SAIPDDTFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14886 603 HRNKILIShNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
98-773 |
8.05e-110 |
|
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: 367.02 E-value: 8.05e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITG 177
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 178 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKaqflatktggtleDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 257
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSV-------------EKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 258 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMNPYDYHFcsqGVITVDNMNDGEELIA--- 334
Cdd:cd01386 148 AGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSF---GIVPLQKPEDKQKAAAafs 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 335 -TDHAMDILGFSVDEKCACYKIVGALLHFGN---MKFKQKQREEQAEadgTESADKAAYLMGVSSGDLLK---------G 401
Cdd:cd01386 225 kLQAAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFAR---PEWAQRAAYLLGCTLEELSSaifkhhlsgG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 402 LLHPRVRVGNEYVTKGQSVEQVVFAVGAL---AKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFN---- 474
Cdd:cd01386 302 PQQSTTSSGQESPARSSSGGPKLTGVEALegfAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqr 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 475 --SFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDwvfIDFGLD---LQPCIDLIEKPL---------------GIL 534
Cdd:cd01386 382 gaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVE---VDFDLPelsPGALVALIDQAPqqalvrsdlrdedrrGLL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 535 SILEEECMFPKASDASFRAKLYdNHAGKSPNFQQPRPDKKRKYQAHFEVVHYAGV--VPYSIVGWLEKNK-DPLNETVVP 611
Cdd:cd01386 459 WLLDEEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQ 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 612 IFQKSQNRLlatlyenyagscsteppkSGVKekrKKAASFQTvsqlhKENLNKLMTNLRATQPHFVRCIVPNENKTPGV- 690
Cdd:cd01386 538 LLQESQKET------------------AAVK---RKSPCLQI-----KFQVDALIDTLRRTGLHFVHCLLPQHNAGKDEr 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 691 -----------MDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPS----AIPDDTFMDSRKATEKLLGS 755
Cdd:cd01386 592 stsspaagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPltkkLGLNSEVADERKAVEELLEE 671
|
730
....*....|....*...
gi 1622840248 756 LDLDHAQYQFGHTKVFFK 773
Cdd:cd01386 672 LDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
98-773 |
1.27e-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: 362.59 E-value: 1.27e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMI-YTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEA-PPHIYAVADNAYNDM-LRNRDNQSML 174
Cdd:cd14875 1 ATLLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 175 ITGESGAGKTVNTKRVIQYFaivaalgdgpGKKAQFLATKTGG-TLEDQIIE----ANPAMEAFGNAKTLRNDNSSRFGK 249
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYL----------GQLSYMHSSNTSQrSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 250 FIRIHFGP-SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMNPYDYHfCSQGVIT-----V 323
Cdd:cd14875 151 YIKLYFDPtSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYK-CLNGGNTfvrrgV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 324 DN--MNDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESAdKAAYLMGVSSGDLLKG 401
Cdd:cd14875 230 DGktLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFL-TACRLLQLDPAKLREC 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 402 LLhprVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKL--PRQFFIGVLDIAGFEIFEFNSFEQL 479
Cdd:cd14875 309 FL---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNSFEQL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 480 CINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIE-KPLGILSILEEECMFPKASDASFRAKLYDN 558
Cdd:cd14875 386 CINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQ 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 559 HAGKSPNFQQPrpdkKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYenyagscSTEPpk 638
Cdd:cd14875 465 WANKSPYFVLP----KSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLL-------STEK-- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 639 sgVKEKRKkaasfQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPN 718
Cdd:cd14875 532 --GLARRK-----QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPV 604
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 719 RLLYTDF-RQRYRILNPSAIPDDTFMDSRKATEKLLGS----LDLDHAQYQFGHTKVFFK 773
Cdd:cd14875 605 RRPIEQFcRYFYLIMPRSTASLFKQEKYSEAAKDFLAYyqrlYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
98-773 |
7.37e-100 |
|
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: 337.17 E-value: 7.37e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAY---KGKRRSEAPPHIYAVADNAYNDMLRNRDNQSML 174
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 175 ITGESGAGKTVNTKRVIQYFAivaalgdgpgkkaqFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIH 254
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLT--------------CRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 255 FGPSGK-LASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSmNPYDYHFCSQG----VITVDNMNDG 329
Cdd:cd14878 147 FCERKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLN-NLCAHRYLNQTmredVSTAERSLNR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 330 EELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRV 409
Cdd:cd14878 226 EKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 410 GNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL----DTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTN 485
Cdd:cd14878 306 KGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 486 EKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLI-EKPLGILSILEEECMFPKASDASFRAKLY------DN 558
Cdd:cd14878 386 EKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDFFfQKPSGFLSLLDEESQMIWSVEPNLPKKLQsllessNT 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 559 HAGKSPNFQQPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENyagscsteppk 638
Cdd:cd14878 466 NAVYSPMKDGNGNVALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQS----------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 639 sgvkekrkKAASfqTVSQLHKeNLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPN 718
Cdd:cd14878 535 --------KLVT--IASQLRK-SLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPV 603
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622840248 719 RLLYTDFRQRYRILNPSAIpddtfMDSRKATEKLLGSLDLDHAQ---YQFGHTKVFFK 773
Cdd:cd14878 604 RLSFSDFLSRYKPLADTLL-----GEKKKQSAEERCRLVLQQCKlqgWQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
98-773 |
1.19e-97 |
|
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: 330.05 E-value: 1.19e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYtasvVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITG 177
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 178 ESGAGKTVNTKRVIQYFaivaalgdgpgkkaqFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 257
Cdd:cd14937 77 ESGSGKTEASKLVIKYY---------------LSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 258 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDML-LLSMNPYDYHFCSQGVI-TVDNMNDGEELIAT 335
Cdd:cd14937 142 YQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYkIRSENEYKYIVNKNVVIpEIDDAKDFGNLMIS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 336 DHAMDIlgfsVDEKCACYKIVGALLHFGNMKFKQ-----KQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVG 410
Cdd:cd14937 222 FDKMNM----HDMKDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 411 NEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQ 490
Cdd:cd14937 298 NQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 491 FFNQHMFVLEQEEYKREGIDWVFIDFGLDlQPCIDLIEKPLGILSILEEECMFPKASDASFrAKLYDNHAGKSPNFQQpr 570
Cdd:cd14937 378 IYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESI-VSVYTNKFSKHEKYAS-- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 571 pdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTeppksgvkeKRKKAAS 650
Cdd:cd14937 454 --TKKDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESL---------GRKNLIT 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 651 FQtvsqlHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRIcRQGFPNRLLYTDFRQRYR 730
Cdd:cd14937 523 FK-----YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFE 596
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1622840248 731 ILNPSAIPDDTFMDSRKATEKLLGSLDLDhaQYQFGHTKVFFK 773
Cdd:cd14937 597 YLDYSTSKDSSLTDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
99-736 |
2.61e-95 |
|
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: 321.08 E-value: 2.61e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 99 SVLHNLRQRYARWMIYTYSGLFCVTINPYKwlPVYTASVVAAYKgKRRSEAPPHIYAVADNAYNDMLRNrDNQSMLITGE 178
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVH-GNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 179 SGAGKTVNTKRVIQYFaivaalgdgpgkkaqFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgpS 258
Cdd:cd14898 78 SGSGKTENAKLVIKYL---------------VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--D 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 259 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLlsmnpyDYHFCSQGVITVDNMNdgEELIATDHA 338
Cdd:cd14898 141 GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI------DTSSTAGNKESIVQLS--EKYKMTCSA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 339 MDILG---FSVDEKCACykivgALLHFGNMKFKQkqrEEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVT 415
Cdd:cd14898 213 MKSLGianFKSIEDCLL-----GILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 416 KGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQffIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQH 495
Cdd:cd14898 285 VFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKK 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 496 MFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEKPLGILSILEEECMFPKASDASFRAKL--YDNHAGKSpnfqqprpdk 573
Cdd:cd14898 363 MFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIkkYLNGFINT---------- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 574 krKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNetVVPIfqksQNRLLATlyenyagscsteppksgvKEKRKKAASFqt 653
Cdd:cd14898 432 --KARDKIKVSHYAGDVEYDLRDFLDKNREKGQ--LLIF----KNLLIND------------------EGSKEDLVKY-- 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 654 vsqlHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILN 733
Cdd:cd14898 484 ----FKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILG 559
|
...
gi 1622840248 734 PSA 736
Cdd:cd14898 560 ITL 562
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
98-773 |
2.68e-85 |
|
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: 296.56 E-value: 2.68e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYA--------RWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRD 169
Cdd:cd14887 1 PNLLENLYQRYNkayinkenRNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 170 NQSMLITGESGAGKTVNTKRVIQYFAIVAALGDGPGKKaqflatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGK 249
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQ----------GLEARLLQSGPVLEAFGNAHTVLNANSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 250 FIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKK-PELQDMLLLSMNPYDYhfcsqgvitvdnmnD 328
Cdd:cd14887 151 MLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVaAATQKSSAGEGDPEST--------------D 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 329 GEELIAtdhAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADG---------------------------- 380
Cdd:cd14887 217 LRRITA---AMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKltsvsvgceetaadrshssevkclssgl 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 381 --TESADK----AAYLMGVSSGD-----LLKGLLHPRVRVGNEYVTkgqsVEQVVFAVGALAKATYDRLFRWLVSRINQT 449
Cdd:cd14887 294 kvTEASRKhlktVARLLGLPPGVegeemLRLALVSRSVRETRSFFD----LDGAAAARDAACKNLYSRAFDAVVARINAG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 450 L-------------DTKLPRQF-FIGVLDIAGFEIFE---FNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGidwV 512
Cdd:cd14887 370 LqrsakpsesdsdeDTPSTTGTqTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEG---V 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 513 FID-----FGLDLQPCIDLIEKP------------------------LGILSILEEE-CMFPKASDASFRAKLYDNHAGK 562
Cdd:cd14887 447 FQNqdcsaFPFSFPLASTLTSSPsstspfsptpsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNK 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 563 ----SPNFQQPRPDKKRKyQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVvpifqksqnrllatlyENYAGSCSTEPPK 638
Cdd:cd14887 527 niinSAKYKNITPALSRE-NLEFTVSHFACDVTYDARDFCRANREATSDEL----------------ERLFLACSTYTRL 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 639 SGVKEKRKKAA---SFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQG 715
Cdd:cd14887 590 VGSKKNSGVRAissRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADG 669
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622840248 716 FPNRLLYTDFRQRYRILNPSAIPDdtFMDSRKATEKLLGSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14887 670 FPCRLPYVELWRRYETKLPMALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
95-772 |
1.15e-84 |
|
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: 292.53 E-value: 1.15e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 95 LNEASVLHNLRQRYARWMIYTY---SGLfcVTINPYKWLPVYTASVVAAYK-------GKRRSEAPPHIYAVADNAYNDM 164
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 165 LRNRDNQSMLITGESGAGKTVNTKRVIQyfaivaalgdgpgkkaQFL----ATKTGGTLEDQIIEANPAMEAFGNAKTLR 240
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLR----------------QLLrlssHSKKGTKLSSQISAAEFVLDSFGNAKTLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 241 NDNSSRFGKFIRIHFGPSGKLASADIDSYLLEKSRVIfQLP-GERSYHVYYQILSGKKPELQDMLLLSmNPYDY-----H 314
Cdd:cd14879 143 NPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVA-SVPtGERNFHVFYYLLAGASPEERQHLGLD-DPSDYallasY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 315 FCSQGVITVDNmNDGEELiatDH---AMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQ--REEQAEADGTESADKAAY 389
Cdd:cd14879 221 GCHPLPLGPGS-DDAEGF---QElktALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 390 LMGVSSGDLLKGLLHPRVRVGNEYVTkgqsveqvVF--AVGA------LAKATYDRLFRWLVSRINQTL-DTKLPRQFFI 460
Cdd:cd14879 297 FLGVSPEDLETSLTYKTKLVRKELCT--------VFldPEGAaaqrdeLARTLYSLLFAWVVETINQKLcAPEDDFATFI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 461 GVLDIAGFEIF---EFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLI-EKPLGILSI 536
Cdd:cd14879 369 SLLDFPGFQNRsstGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGI 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 537 LEEEC-MFPKASDASFRAKLYDNHAGKSPnFQQPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVpifqk 615
Cdd:cd14879 448 LDDQTrRMPKKTDEQMLEALRKRFGNHSS-FIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFV----- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 616 sqnrllaTLyenyagscsteppksgvkekrkkaasFQTVSQLhKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFL 695
Cdd:cd14879 522 -------NL--------------------------LRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRR 567
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622840248 696 VLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYrilnpsaIPDDTFMDSRKATEKLLGSLDLDHAQYQFGHTKVFF 772
Cdd:cd14879 568 VKAQIRSLGLPELAARLRVEYVVSLEHAEFCERY-------KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
98-721 |
1.00e-81 |
|
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: 284.88 E-value: 1.00e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRRSEA-------PPHIYAVADNAYNDMLRNRD 169
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 170 NQSMLITGESGAGKTVNTKRVIQYFAIVaalgdgpgkKAQFLATKtggtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGK 249
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI---------QTDSQMTE----RIDKLIYINNILESMSNATTIKNNNSSRCGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 250 FIRIHF---------GPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSMNPYDYHFCSQGV 320
Cdd:cd14884 148 INLLIFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 321 ------------ITVDNMNDGEELIATD--------HAMDILGFSVDEKCACYKIVGALLHFGNMKFKQkqreeqaeadg 380
Cdd:cd14884 228 shqkrsvkgtlrLGSDSLDPSEEEKAKDeknfvallHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA----------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 381 tesadkAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQT----------L 450
Cdd:cd14884 297 ------AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNvlkckekdesD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 451 DTKLPR--QFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIE 528
Cdd:cd14884 371 NEDIYSinEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIA 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 529 KPLGIL-SILEEECMFPKASDASFRAKLYDNH----------AGKSPNFQQPRPDKKRKYQAH-FEVVHYAGVVPYSIVG 596
Cdd:cd14884 450 KIFRRLdDITKLKNQGQKKTDDHFFRYLLNNErqqqlegkvsYGFVLNHDADGTAKKQNIKKNiFFIRHYAGLVTYRINN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 597 WLEKNKDPLNETVVPIFQKSQNRllaTLYENYAGscsteppksgvkekrKKAASFQTVSQLHKENLNKLMTNLRATQPHF 676
Cdd:cd14884 530 WIDKNSDKIETSIETLISCSSNR---FLREANNG---------------GNKGNFLSVSKKYIKELDNLFTQLQSTDMYY 591
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1622840248 677 VRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLL 721
Cdd:cd14884 592 IRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
98-737 |
6.37e-75 |
|
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: 263.27 E-value: 6.37e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 98 ASVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYkgkrrseappHIYAVADNAYNDMLRNRDNQSMLI-T 176
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNAESIVfG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 177 GESGAGKTVNTKRVIQYfaivaaLGDGPGKKaqfLATKTGGTLEDQIieanpamEAFGNAKTLRNDNSSRFGKFIRIHFG 256
Cdd:cd14874 71 GESGSGKSYNAFQVFKY------LTSQPKSK---VTTKHSSAIESVF-------KSFGCAKTLKNDEATRFGCSIDLLYK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 257 PSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSmNPYDYHFCSQGVITVDNMNDGEELIATD 336
Cdd:cd14874 135 RNVLTGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIK-GLQKFFYINQGNSTENIQSDVNHFKHLE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 337 HAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQR---EEQAEADGTESADK-AAYLMGVSSGDLLKGLLhPRVRVGNE 412
Cdd:cd14874 214 DALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNpnvEQDVVEIGNMSEVKwVAFLLEVDFDQLVNFLL-PKSEDGTT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 413 YvtkgqSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLpRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFF 492
Cdd:cd14874 293 I-----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPL-HTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 493 NQHMFVLEQEEYKREGIDwvfIDF----GLDLQPCIDLI-EKPLGILSILEEECMFPKASDASFRAKLYDNHAGKSpNFQ 567
Cdd:cd14874 367 VKHSFHDQLVDYAKDGIS---VDYkvpnSIENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRS-SYG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 568 QPRpdkkRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEppksgvkekrkk 647
Cdd:cd14874 443 KAR----NKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDM------------ 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 648 aasFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQ 727
Cdd:cd14874 507 ---IVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFAR 583
|
650
....*....|
gi 1622840248 728 RYRILNPSAI 737
Cdd:cd14874 584 QYRCLLPGDI 593
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
171-753 |
5.29e-73 |
|
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: 257.73 E-value: 5.29e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 171 QSMLITGESGAGKTVNTKRVI-QYFAIVaalGDGPGKKA-QFLATktggtledqiieANPAMEAFGNAKTLRNDNSSRFG 248
Cdd:cd14881 69 QAIILSGTSGSGKTYASMLLLrQLFDVA---GGGPETDAfKHLAA------------AFTVLRSLGSAKTATNSESSRIG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 249 KFIRIHFgPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLS-MNPYDYHFCSQGVITVDNMN 327
Cdd:cd14881 134 HFIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgYSPANLRYLSHGDTRQNEAE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 328 DGEELIATDHAMDILGFS-VDekcaCYKIVGALLHFGNMKFKQKQREEQAEADGTEsADKAAYLMGVSSGDLLKGLlhpR 406
Cdd:cd14881 213 DAARFQAWKACLGILGIPfLD----VVRVLAAVLLLGNVQFIDGGGLEVDVKGETE-LKSVAALLGVSGAALFRGL---T 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 407 VRVGNeyvTKGQSVEQVV------FAVGALAKATYDRLFRWLVSRINQ------TLDTKlPRQFFIGVLDIAGFEIFEFN 474
Cdd:cd14881 285 TRTHN---ARGQLVKSVCdanmsnMTRDALAKALYCRTVATIVRRANSlkrlgsTLGTH-ATDGFIGILDMFGFEDPKPS 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 475 SFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDW-VFIDFgLDLQPCIDLIEK-PLGILSILEEECMfPKASDASFR 552
Cdd:cd14881 361 QLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCeVEVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYV 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 553 AKLYDNHAGkSPNFQQPRPDKKRKyqahFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSqnrllatlyenyagSC 632
Cdd:cd14881 439 AKIKVQHRQ-NPRLFEAKPQDDRM----FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQ--------------NC 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 633 STeppksgvkekrkkaaSFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRIC 712
Cdd:cd14881 500 NF---------------GFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLM 564
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1622840248 713 RQGFPNRLLYTDFRQRYRILNPSAiPDDTFMDSRKATEKLL 753
Cdd:cd14881 565 AGGYPHRMRFKAFNARYRLLAPFR-LLRRVEEKALEDCALI 604
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
101-772 |
2.36e-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: 237.95 E-value: 2.36e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 101 LHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRR----------SEAPPHIYAVADNAYNDMLRNRDN 170
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 171 QSMLITGESGAGKTVNTKRVIQYfaiVAALGDGPGKKAQFL-ATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGK 249
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQY---LCEIGDETEPRPDSEgASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 250 FIRIHFGPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKK--PELQDMLLLSMNPYDYHFCSQGVITVDNMN 327
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQADPLATNFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 328 dgeeLIATDHAMDILGFSV-----DEKCACYKIVGALLHFGNMKF--KQKQREEQAEADGTESADKAAYLMGVSSGDLLK 400
Cdd:cd14893 241 ----LDARDYRDLMSSFSAlrirkNQRVEIVRIVAALLHLGNVDFvpDPEGGKSVGGANSTTVSDAQSCALKDPAQILLA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 401 GLL---HPRV------------RVGNEYVT--KGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPR------- 456
Cdd:cd14893 317 AKLlevEPVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRyeksniv 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 457 --QFFIGVLDIAGFEIFE--FNSFEQLCINFTNEKLQQFFNQHMFV-----LEQEEYKREG--IDWVFIDFGLDLQPCID 525
Cdd:cd14893 397 inSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrlTVNSNVDITSEQEKCLQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 526 LIE-KPLGILSILEEECMFPKASDASFRAKLY---DNHAGKS-PN----FQQPRPDKKRKYQAHFEVVHYAGVVPYSIVG 596
Cdd:cd14893 477 LFEdKPFGIFDLLTENCKVRLPNDEDFVNKLFsgnEAVGGLSrPNmgadTTNEYLAPSKDWRLLFIVQHHCGKVTYNGKG 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 597 WLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKKAASFQTVSQLHKENLN------------- 663
Cdd:cd14893 557 LSSKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqa 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 664 -KLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRilnpsaipddTF 742
Cdd:cd14893 637 dALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK----------NV 706
|
730 740 750
....*....|....*....|....*....|....
gi 1622840248 743 MDSRKATEKLLGSLD----LDHAQYQFGHTKVFF 772
Cdd:cd14893 707 CGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
99-773 |
3.83e-65 |
|
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: 234.63 E-value: 3.83e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 99 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITGE 178
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 179 SGAGKTVNTKRVIQYFAIvaaLGDGPGKKAQflatktggtledQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 258
Cdd:cd14882 82 SYSGKTTNARLLIKHLCY---LGDGNRGATG------------RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGST 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 259 GKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPE--LQDMLLLSMNPYDYHFCSQGV-------ITVDNMNDG 329
Cdd:cd14882 147 GKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQnrLKEYNLKAGRNYRYLRIPPEVppsklkyRRDDPEGNV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 330 EELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREeqAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRV 409
Cdd:cd14882 227 ERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCLIK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 410 GNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLdtKLPRQFF-----IGVLDIAGFEIFEFNSFEQLCINFT 484
Cdd:cd14882 305 GGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKM--SFPRAVFgdkysISIHDMFGFECFHRNRLEQLMVNTL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 485 NEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCID-LIEKPLGILSILEEecmfpkASDASFRAKLYDN--HAG 561
Cdd:cd14882 383 NEQMQYHYNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDqLMTKPDGLFYIIDD------ASRSCQDQNYIMDriKEK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 562 KSPNFqqprpdkKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENyagscsteppkSGV 641
Cdd:cd14882 456 HSQFV-------KKHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-----------SQV 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 642 KEKRKKAASFQTVSQlhkENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLL 721
Cdd:cd14882 518 RNMRTLAATFRATSL---ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIP 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1622840248 722 YTDFRQRYRILnpsAIPDDTFMDSRKATEKLLgSLDLDHAQYQFGHTKVFFK 773
Cdd:cd14882 595 FQEFLRRYQFL---AFDFDETVEMTKDNCRLL-LIRLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
99-725 |
1.36e-60 |
|
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: 222.28 E-value: 1.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 99 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLP-VYTASVVAAYKGKRrsEAPPHIYAVADNAYNDMLRNRDNQSMLITG 177
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRR--GLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 178 ESGAGKTVNTKRVIQYFAIVAAlgdgpgKKAQFLatktggtlEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 257
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTDL------SRSKYL--------RDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 258 SGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSmNPYDYHFCSQ-GVITVDNMNDGEELIATD 336
Cdd:cd14905 146 YGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLG-DINSYHYLNQgGSISVESIDDNRVFDRLK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 337 HAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQreEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTK 416
Cdd:cd14905 225 MSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKN--GKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVEN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 417 GQSveqvvfavgaLAKATYDRLFRWLVSRINQTLDtklPRQF--FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQ 494
Cdd:cd14905 303 RDS----------LARSLYSALFHWIIDFLNSKLK---PTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 495 HMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKplgILSILEEECMFPKASDASFRAKLYD----NHA-GKSPNfqqp 569
Cdd:cd14905 370 TVLKQEQREYQTERIPWMTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKLQNflsrHHLfGKKPN---- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 570 rpdkkrkyqaHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLL----------ATLYE--------NYAG- 630
Cdd:cd14905 443 ----------KFGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLfsrdgvfninATVAElnqmfdakNTAKk 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 631 ----------SCSTEPPKSGVKEKRKK----------------AASFQTVSqlhkeNLNKLMTNlRATQPHFVRCIVPNE 684
Cdd:cd14905 513 splsivkvllSCGSNNPNNVNNPNNNSgggggggnsgggsgsgGSTYTTYS-----STNKAINN-SNCDFHFIRCIKPNS 586
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1622840248 685 NKTPGVMDAFLVLHQLRCNGVLEGIRICRQGFP----NRLLYTDF 725
Cdd:cd14905 587 KKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
120-253 |
8.73e-56 |
|
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: 191.79 E-value: 8.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 120 FCVTINPYKWLPVYTASVV-AAYKGKRRSEAPPHIYAVADNAYNDMLRNRDNQSMLITGESGAGKTVNTKRVIQYFAIVA 198
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622840248 199 ALGDGPGK-KAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 253
Cdd:cd01363 81 FNGINKGEtEGWVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-771 |
6.07e-47 |
|
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: 181.57 E-value: 6.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 99 SVLHNLRQRYARWMIYTYSGLFCVTINPYKWLPVYTASVVAAYKGKRRSE-APPHIYAVADNAYNDMLRNRDNQSMLITG 177
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 178 ESGAGKTVNTKRVIQYFA---------IVAALGDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFG 248
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAyqvkgsrrlPTNLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 249 KFIRIHFgPSGKLASADIDSYLLEKSRVIFQLPGERSYHVYYQILSGKKPELQDMLLLSmNPYDYHFCSQGVITVDNMND 328
Cdd:cd14938 162 KFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLK-NIENYSMLNNEKGFEKFSDY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 329 GEELIATDHAMDILGFSVDEKCACYKIVGALLHFGN-------------MKFKQKQRE----------EQAEADGTESAD 385
Cdd:cd14938 240 SGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDENV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 386 KAAYLmgvsSGDLLKGLLHPRVR------VGNEYV-TKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL-DTKLPRQ 457
Cdd:cd14938 320 KNLLL----ACKLLSFDIETFVKyfttnyIFNDSIlIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCtQLQNINI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 458 F--FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCID-LIEKPLGIL 534
Cdd:cd14938 396 NtnYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNlLVGPTEGSL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 535 -SILEEECMfPKASDASFRAKLYDNHAGKSPNFqqPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIF 613
Cdd:cd14938 476 fSLLENVST-KTIFDKSNLHSSIIRKFSRNSKY--IKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 614 QKSQNRLLATLYENY----AGSCSTEPPKSGVKE-----KRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNE 684
Cdd:cd14938 553 KQSENEYMRQFCMFYnydnSGNIVEEKRRYSIQSalklfKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNE 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 685 NKTP-GVMDAFLVLHQLRCNGVLEGIRICRQGFPNRLLYTDFRQRYRILNPsaipddtfmDSRKATEKLLGSLDLDHAQY 763
Cdd:cd14938 633 SKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEW 703
|
....*...
gi 1622840248 764 QFGHTKVF 771
Cdd:cd14938 704 MIGNNMIF 711
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
846-1401 |
4.32e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 114.26 E-value: 4.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 846 LLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGK 925
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 926 VKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKA 1005
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1006 LQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADATQDKQQLEE 1085
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1086 KLKKKDSELSQLSLRVEDEqllgAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASA 1165
Cdd:COG1196 471 EAALLEAALAELLEELAEA----AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAA 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1166 GQREGSRKREAELGRLRRELEEAALRhEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETL 1245
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKAAKAG-RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1246 TRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSHLLEEKECLISQLSRGKALAAQSLEELRRQ 1325
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622840248 1326 LEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQwrSKYEADAIQRteELEEAKKKLA 1401
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP--EPPDLEELER--ELERLEREIE 777
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
854-1414 |
4.37e-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: 4.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 854 EELAALRAELRGLRgaLAAAEAKRQELEETHVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERL 933
Cdd:COG1196 220 EELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 934 EDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQA 1013
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1014 LGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADATQDKQQLEEKLKKKDSE 1093
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1094 LSQLSLRVEDEQLLGAQLQKKIKELQAraeeleeeleaeraararvekQRAEAARELEELSERLEEAGGASAGQREgsRK 1173
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLE---------------------ELAEAAARLLLLLEAEADYEGFLEGVKA--AL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1174 REAELGRLRRELEEAALRHEATVAALRrkQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAE 1253
Cdd:COG1196 515 LLAGLRGLAGAVAVLIGVEAAYEAALE--AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1254 KLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSHLLEEKECLISQLSRGKALAAQSLEELRRQLEEESKAK 1333
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1334 SALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEA 1413
Cdd:COG1196 673 ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA 752
|
.
gi 1622840248 1414 A 1414
Cdd:COG1196 753 L 753
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1186-1937 |
7.81e-23 |
|
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: 107.06 E-value: 7.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1186 EEAALRHEATVAALRRKQAEgAAELGEQVDSLQRVRQKLEK---EKSELR--------MEVDDLAANVETLTRAKASAEK 1254
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDI-LNELERQLKSLERQAEKAERykeLKAELRelelallvLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1255 LCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSHLLEEKEcliSQLSRGKALAAQSLEELRRQLEEESKAKS 1334
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE---QQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1335 ALAHAVQALrhdcDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEAdaiqRTEELEEAKKKLALRLQEAE---EGV 1411
Cdd:TIGR02168 331 KLDELAEEL----AELEEKLEELKEELESLEAELEELEAELEELESRLEE----LEEQLETLRSKVAQLELQIAslnNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1412 EAANAKCSSLEKAKLRLQTESEDVTLELERATSAA-----AALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLGT 1486
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaelEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1487 ELFRLQ---HSHEEALEALETLKRENKNLQEEISDLTDQLSLSGKSIQELEKAKKALE-----------GEKSEIQAALE 1552
Cdd:TIGR02168 483 ELAQLQarlDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEaalggrlqavvVENLNAAKKAI 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1553 EAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLD--------AETRArnEALRLKKK 1624
Cdd:TIGR02168 563 AFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvVDDLD--NALELAKK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1625 M-------------------------EGDLNDLELQ--LGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELREQ 1677
Cdd:TIGR02168 641 LrpgyrivtldgdlvrpggvitggsaKTNSSILERRreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1678 AQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERRE 1757
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1758 AEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGgKKQVQKLEAKVRELEAELDAEQ 1837
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL-AAEIEELEELIEELESELEALL 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1838 KKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYR-KAQHELDDAEER 1916
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEAL 959
|
810 820
....*....|....*....|....*..
gi 1622840248 1917 ADMAETQANKLRARTR------DALGP 1937
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKrlenkiKELGP 986
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1182-1835 |
2.07e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.40 E-value: 2.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1182 RRE-LEEAA--LRHEAtvaalRRKQAEG---------------AAELGEQVDSLQRVRQKLEKEKsELRMEVDDLAANVE 1243
Cdd:COG1196 157 RRAiIEEAAgiSKYKE-----RKEEAERkleateenlerlediLGELERQLEPLERQAEKAERYR-ELKEELKELEAELL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1244 TLTRakasaeklcRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSHLLEEKECLISQLSrgkalaaqsleelr 1323
Cdd:COG1196 231 LLKL---------RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-------------- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1324 rqlEEESKAKSALAHAVQALRHDCDLLREQHEEeaeaqaelqrlLSKANAEVAQWRSKyEADAIQRTEELEEAKKKLALR 1403
Cdd:COG1196 288 ---AEEYELLAELARLEQDIARLEERRRELEER-----------LEELEEELAELEEE-LEELEEELEELEEELEEAEEE 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1404 LQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARG 1483
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1484 LGTELFRLQHSHEEALEALETLKRENKNLQEEISDLTDQLSLSGKSIQELEKAKKALEGEKSEIQAALEEAEGALELEET 1563
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1564 KTLRIQLELSQVKAEVDRKLAEKDEECANLRrnhqRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQA 1643
Cdd:COG1196 513 ALLLAGLRGLAGAVAVLIGVEAAYEAALEAA----LAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAAL 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1644 TEAQAATRLMQAQLKEEQAGRDEEQRLAAELREQAQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLL 1723
Cdd:COG1196 589 AAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1724 HSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQAR 1803
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
650 660 670
....*....|....*....|....*....|..
gi 1622840248 1804 LEEAEQAALRGGKkqVQKLEAKVRELEAELDA 1835
Cdd:COG1196 749 EEEALEELPEPPD--LEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
937-1902 |
7.24e-22 |
|
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: 103.98 E-value: 7.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 937 EEVNADLAarrrKLEDECTELKKDIDDLELTLAKAEK--EKQATENKVKN--LTEEMAALDESVARLTKEKKALQEAHQQ 1012
Cdd:TIGR02168 182 ERTRENLD----RLEDILNELERQLKSLERQAEKAERykELKAELRELELalLVLRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1013 ALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLrmdteraKRKLEGDLKLTQESVADATQDKQQLEEKLKKKDS 1092
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE-------ISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1093 ELSQLSLRVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAAreleelserleeagGASAGQREGSR 1172
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR--------------SKVAQLELQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1173 KREAELGRLRRELEEAALRHEatvaalrrKQAEGAAELGEQVDSLQRvrQKLEKEKSELRMEVDDLAANVETLTRAKASA 1252
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRE--------RLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEEALEEL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1253 EKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSHLLEEKE-------CLISQLS----RGKAL-AAQSLE 1320
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSglsgilgVLSELISvdegYEAAIeAALGGR 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1321 ELRRQLEEESKAKSALAHAVQALRHDCDLLreqheeeaEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKL 1400
Cdd:TIGR02168 547 LQAVVVENLNAAKKAIAFLKQNELGRVTFL--------PLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1401 ALRLQeaeeGVEAANAKCSSLEKAKlRLQTESEDVTLELERATSAAAAldkkqrhleraleerrrqeeemqreleaAQRE 1480
Cdd:TIGR02168 619 SYLLG----GVLVVDDLDNALELAK-KLRPGYRIVTLDGDLVRPGGVI----------------------------TGGS 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1481 ARGLGTELFRlqhsheealealetlKRENKNLQEEISDLTDQlslsgksIQELEKAKKALEGEKSEIQAALEEAEGALEL 1560
Cdd:TIGR02168 666 AKTNSSILER---------------RREIEELEEKIEELEEK-------IAELEKALAELRKELEELEEELEQLRKELEE 723
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1561 EETKTLRIQLELSQVKAEVdrklaekdEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLElqlghat 1640
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEV--------EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE------- 788
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1641 RQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELREQAQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERL 1720
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1721 NLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVREL 1800
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1801 QARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQS 1880
Cdd:TIGR02168 949 YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
970 980
....*....|....*....|..
gi 1622840248 1881 KVKSykrQFEEAEQQANTNLAK 1902
Cdd:TIGR02168 1029 EARE---RFKDTFDQVNENFQR 1047
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1166-1918 |
7.67e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 100.60 E-value: 7.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1166 GQREGSRKREAELGRLRReLEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKE-KSELRMEVDDLAANVET 1244
Cdd:PTZ00121 1054 GNHEGKAEAKAHVGQDEG-LKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEArKAEEAKKKAEDARKAEE 1132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1245 LTRAKAS--AEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSHLLEEKECLISQLSRG--KALAAQSLE 1320
Cdd:PTZ00121 1133 ARKAEDArkAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKaeAARKAEEER 1212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1321 ELRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKyeADAIQRTEELEEAK-KK 1399
Cdd:PTZ00121 1213 KAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK--AEEARKADELKKAEeKK 1290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1400 LALRLQEAEEGVEAANAKCSSLEKAKlrlqteSEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQR 1479
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKK------ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1480 EARGLGTELFRLQHSHEEALEALETLKR--ENKNLQEEISDLTDQLSLSGKSIQELEKAKKALEgeksEIQAALEEAEGA 1557
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE----EKKKADEAKKKA 1440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1558 LELEETKTLRIQLELSQvKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAEtRARNEALRLKKKMEGDLNDLELQLG 1637
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAK-KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEAKKA 1518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1638 HATRQATEAQAAtrlmQAQLKEEQAGRDEEQRLAAELREQAQALERRAallaaeleelraaleqgersRRLAEQELLEAT 1717
Cdd:PTZ00121 1519 EEAKKADEAKKA----EEAKKADEAKKAEEKKKADELKKAEELKKAEE--------------------KKKAEEAKKAEE 1574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1718 ERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAitdaammaEELKKEQDTSAHLERMKKTLEQTV 1797
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA--------EELKKAEEEKKKVEQLKKKEAEEK 1646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1798 RELQARLEEAEQAALRGG--KKQVQKLEAKVRELEAElDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLV 1875
Cdd:PTZ00121 1647 KKAEELKKAEEENKIKAAeeAKKAEEDKKKAEEAKKA-EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE 1725
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1622840248 1876 DKLQSKVKSYKRQFEEAEQQAN---TNLAKYRKAQHELDDAEERAD 1918
Cdd:PTZ00121 1726 EENKIKAEEAKKEAEEDKKKAEeakKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1391-1937 |
8.12e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.01 E-value: 8.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1391 EELEEAKKKL-ALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKqrhleraleerrrqeee 1469
Cdd:COG1196 220 EELKELEAELlLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE----------------- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1470 mqreLEAAQREARGLGTELFRLQHSHEEALEALETLKRENKNLQEEISDLTDQLSLSGKSIQELEKAKKALEGEKSEIQA 1549
Cdd:COG1196 283 ----LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1550 ALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEKdEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDL 1629
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA-AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1630 NDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELREQAQALERRAALLAAELEELRAALEQGERSRRLA 1709
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1710 EQEL------------------LEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAM 1771
Cdd:COG1196 518 GLRGlagavavligveaayeaaLEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1772 MA--------------------EELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKK--QVQKLEAKVREL 1829
Cdd:COG1196 598 GAavdlvasdlreadaryyvlgDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTggSRRELLAALLEA 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1830 EAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAkyrKAQHE 1909
Cdd:COG1196 678 EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE---EEALE 754
|
570 580
....*....|....*....|....*...
gi 1622840248 1910 LDDAEERADMAETQANKLRARtRDALGP 1937
Cdd:COG1196 755 ELPEPPDLEELERELERLERE-IEALGP 781
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
842-1750 |
1.96e-19 |
|
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: 95.89 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 842 KMKPLLRSAQAEEELAALRAELRGLRGALAA-----AEAKRQELEETHVSVTQEKNDLALQLQAEQDNLADAEERCHLLI 916
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAELRELELALLVlrleeLREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 917 KSKVQLEGKVKELSERLEDEEEVNADLAARRRKLED-------ECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEM 989
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLERqleeleaQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 990 AALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRmdTERAKRKLEGDLKLT 1069
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI--EELLKKLEEAELKEL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1070 QESVADATQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQLQKKIKELQAraeeleeeleaeraararvekqraeaare 1149
Cdd:TIGR02168 439 QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA----------------------------- 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1150 leelserleeaggasagqregsrkREAELGRLRRELEEAAlrheATVAALRRKQAEGAAELGeQVDSLQRVRQKLEKEKS 1229
Cdd:TIGR02168 490 ------------------------RLDSLERLQENLEGFS----EGVKALLKNQSGLSGILG-VLSELISVDEGYEAAIE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1230 E-LRMEVDDLAanVETLTRAKASAEKLcrtYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSHLLEekecLISQL 1308
Cdd:TIGR02168 541 AaLGGRLQAVV--VENLNAAKKAIAFL---KQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKD----LVKFD 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1309 SRGKALAAqsleelrrqleeeskakSALAHAV------QALRhdcdlLREQHEEEAEAQAELQRLLSKANAeVAQWRSKY 1382
Cdd:TIGR02168 612 PKLRKALS-----------------YLLGGVLvvddldNALE-----LAKKLRPGYRIVTLDGDLVRPGGV-ITGGSAKT 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1383 EADAIQRTEELEEAKKKLAlrlqEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEE 1462
Cdd:TIGR02168 669 NSSILERRREIEELEEKIE----ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1463 RRRQEEEMQRELEAAQREARGLGTELfrlqhshEEALEALETLKRENKNLQEEISDLTDQLSLSGKSIQELEKAKKALEG 1542
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERL-------EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1543 EKSEIQAALEEAEGALELEETKTLRIQLELSQVKAEVDrKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLK 1622
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE-SLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1623 KKMEGDLNDLELQLGHATRQATEAQaaTRLMQAQLKEEQAgRDEEQRLAAELREQAQALERRAALLAAELEELRAALEqg 1702
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELR--EKLAQLELRLEGL-EVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR-- 971
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622840248 1703 ERSRRL-------------AEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEE 1750
Cdd:TIGR02168 972 RRLKRLenkikelgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
223-713 |
1.11e-18 |
|
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: 92.88 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 223 IIEANPAMEAFGNAKTLRNDNSSRFGKF--IRIHFGPSG---KLASADIDSYLLEKSRVIFQL------PGERSYHVYYQ 291
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 292 ILSGKKPELQDMLLLSMNPYDYHFCSQ------------GVITVDNM--NDGEELIATDHAMDILGFSVDEKCACYKIVG 357
Cdd:cd14894 329 MVAGVNAFPFMRLLAKELHLDGIDCSAltylgrsdhklaGFVSKEDTwkKDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 358 ALLHFGNMKFKQKQREEQAEADGT---ESADKAAYLMGVSSGDLLKGLLHPR-VRVGNEYVTKGQSVE--QVVFAVGALA 431
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsVSLQSTSETFEVTLEkgQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 432 KATYDRLFRWLVSRINQTL----------------DTKLPRQF-FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQ 494
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEATkmsalstdgnkhqmdsNASAPEAVsLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYAREEQ 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 495 ----------HMFVLEQEEykregiDWVFIdfgldlqpcidlIEKPLGILSILEEECMFPKASDAS----------FRAK 554
Cdd:cd14894 569 viavayssrpHLTARDSEK------DVLFI------------YEHPLGVFASLEELTILHQSENMNaqqeekrnklFVRN 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 555 LYDNHAGKSPNFQQPRPDKKRKYQAHFEVV-----HYAGVVPYSIVGWLEKNKDPL-NETVVPIFQKSQNRLLATLYENY 628
Cdd:cd14894 631 IYDRNSSRLPEPPRVLSNAKRHTPVLLNVLpfvipHTRGNVIYDANDFVKKNSDFVyANLLVGLKTSNSSHFCRMLNESS 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 629 AGSCSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDAFLVLHQLRCNGVLEG 708
Cdd:cd14894 711 QLGWSPNTNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQ 790
|
....*
gi 1622840248 709 IRICR 713
Cdd:cd14894 791 MEICR 795
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1174-1929 |
1.11e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.20 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1174 REAELGRLrrelEEAALRHEATVAALRRKQAEGAAElGEQVDSLQRVRQKLEKEKSELRMEVDDlAANVETLTRAKAS-- 1251
Cdd:PTZ00121 1104 KKTETGKA----EEARKAEEAKKKAEDARKAEEARK-AEDARKAEEARKAEDAKRVEIARKAED-ARKAEEARKAEDAkk 1177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1252 AEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSHLLEEKECLISQLSRGKALAAQSLEELRRQLEEESK 1331
Cdd:PTZ00121 1178 AEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKF 1257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1332 AKSALAH-AVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEEL----EEAKKKLALRLQE 1406
Cdd:PTZ00121 1258 EEARMAHfARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAkkkaEEAKKKADAAKKK 1337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1407 AEEGVEAANAKCSSLEKAKLRLQT---ESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARG 1483
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAaeeKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK 1417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1484 LGTElfRLQHSHEEALEALETLKR-ENKNLQEEISDLTDQLSLSGKSIQELEKAKKALEGEKseiqaaleeaeGALELEE 1562
Cdd:PTZ00121 1418 KKAD--EAKKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK-----------KAEEAKK 1484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1563 TKTLRIQLELSQVKAEVDRKLAEKDEECANLRRNHqraveslqasldaETRARNEALRLKKKMEGDlndlELQLGHATRQ 1642
Cdd:PTZ00121 1485 ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE-------------EAKKADEAKKAEEAKKAD----EAKKAEEKKK 1547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1643 ATEAQAATRLMQAQ--LKEEQAGRDEEQ-----RLAAELREQAQALERRAALLAAELEELRAALEQGERSRRLAEQELLE 1715
Cdd:PTZ00121 1548 ADELKKAEELKKAEekKKAEEAKKAEEDknmalRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1716 ATERLNLLHSQNTGLLNQKKKLE-------------ADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDT 1782
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEelkkaeeenkikaAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1783 SAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKgvrKHERRVKELAYQAE 1862
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKA---EEIRKEKEAVIEEE 1784
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622840248 1863 EDRKNLARMQDlVDKlqsKVKSYKRQFEEAEQQANTNlAKYRKAQHELDDAE--ERADMAETQANKLRA 1929
Cdd:PTZ00121 1785 LDEEDEKRRME-VDK---KIKDIFDNFANIIEGGKEG-NLVINDSKEMEDSAikEVADSKNMQLEEADA 1848
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1632-1937 |
1.37e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.53 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1632 LELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELREQAQALERRAALLAAELEELRAALEQGERSRRLAEQ 1711
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1712 ELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKK 1791
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1792 TLEQTVRELQARLEEAEQAALRgGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARM 1871
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAE-LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622840248 1872 QDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDALGP 1937
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
924-1809 |
2.16e-15 |
|
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: 82.42 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 924 GKVKELSERLEDEEEVNADLAARRRKLEDEcTELKKDIDDLELTLAKAE-----KEKQATENKVKNLTEEMAALDESVAR 998
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 999 LTKEKKALQEAHQQALGDLQAEEDRVSALTKAK-LRLEQQVEDLECSLEQekklrmdterakrkLEGDLKLTQESVADAT 1077
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqLRVKEKIGELEAEIAS--------------LERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1078 QDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERL 1157
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1158 EEAGGASAGQREGSRKREAELGRLRRELEEAalrhEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDD 1237
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGI----EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1238 LaanvetltrakasaeklcRTYEDQLSeakikveELQRQLADASTQRGRLQTESGELSHLLEEKEC-------LISQLSR 1310
Cdd:TIGR02169 478 Y------------------DRVEKELS-------KLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1311 GK---ALA---AQSLEELRRQLEEESKAKSA--LAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKY 1382
Cdd:TIGR02169 533 VGeryATAievAAGNRLNNVVVEDDAVAKEAieLLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKY 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1383 EAD---AIQRT---EELEEAKK--------KLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAA 1448
Cdd:TIGR02169 613 EPAfkyVFGDTlvvEDIEAARRlmgkyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSS 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1449 LDKKQRHleraleeRRRQEEEMQRELEAAQREARGLGTELFRLQHSHEEALEALETLKRENKNLQEEISDLTDQLSLSGK 1528
Cdd:TIGR02169 693 LQSELRR-------IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1529 SIQELEKAKKALEGEKSEIQAALEEAEGALeleetktlrIQLELSQVKAEVDRKLAEKDEECANLRRNHQRavESLQASL 1608
Cdd:TIGR02169 766 RIEELEEDLHKLEEALNDLEARLSHSRIPE---------IQAELSKLEEEVSRIEARLREIEQKLNRLTLE--KEYLEKE 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1609 DAETRARNEALRLKKKMEGD-LNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEeqrLAAELREQaqalerraal 1687
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKeIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE---LEAQLREL---------- 901
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1688 laaeleelraaleqgERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAA-----QERREAEEKA 1762
Cdd:TIGR02169 902 ---------------ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELsledvQAELQRVEEE 966
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 1622840248 1763 KKAITDAAMMA-EELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQ 1809
Cdd:TIGR02169 967 IRALEPVNMLAiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1100-1914 |
2.64e-15 |
|
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: 82.15 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1100 RVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEaarelEELSERLEEAGGASAGQREGSRKREAE-- 1177
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQE-----QLQAETELCAEAEEMRARLAARKQELEei 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1178 LGRLRRELEEAALRHEAtVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLtrakasaeklcr 1257
Cdd:pfam01576 77 LHELESRLEEEEERSQQ-LQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLL------------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1258 tyEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSHLLEEKECLISQLsrgkalaaqsleelRRQLEEESKAKSALA 1337
Cdd:pfam01576 144 --EDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDL--------------EERLKKEEKGRQELE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1338 HAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELeEAKKKLALRLQEAEEGVEAANAK 1417
Cdd:pfam01576 208 KAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNAL-KKIRELEAQISELQEDLESERAA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1418 CSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFrlqhshEE 1497
Cdd:pfam01576 287 RNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQAL------EE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1498 ALEALETLKRENKN-------LQEEISDLTDQLSLSGKSIQELEKAKKALEGEKSEIQAALEEAEGALELEETKTLRIQL 1570
Cdd:pfam01576 361 LTEQLEQAKRNKANlekakqaLESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1571 ELSQVKA---EVDRKLAEKDEECANLRRNHQRAVESLQasldAETRARNEALRLKKKMEGDLNDLELQLGH--ATRQATE 1645
Cdd:pfam01576 441 ELESVSSllnEAEGKNIKLSKDVSSLESQLQDTQELLQ----EETRQKLNLSTRLRQLEDERNSLQEQLEEeeEAKRNVE 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1646 AQAATrlMQAQLKEEQAGRDEEQRLAAELREQAQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHS 1725
Cdd:pfam01576 517 RQLST--LQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQ 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1726 QNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDT----------------------- 1782
Cdd:pfam01576 595 LVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAkeelertnkqlraemedlvsskd 674
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1783 ----SAH-LERMKKTLEQTVRELQARLEE-------AEQAALR---------------------GGKKQVQKLEAKVREL 1829
Cdd:pfam01576 675 dvgkNVHeLERSKRALEQQVEEMKTQLEEledelqaTEDAKLRlevnmqalkaqferdlqardeQGEEKRRQLVKQVREL 754
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1830 EAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHE 1909
Cdd:pfam01576 755 EAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKK 834
|
....*
gi 1622840248 1910 LDDAE 1914
Cdd:pfam01576 835 LKNLE 839
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1375-1941 |
2.86e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.50 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1375 VAQWRSKYEADAIQRTEELEEAKKKLALRlqEAEEGVEAANA-KCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQ 1453
Cdd:PTZ00121 1154 VEIARKAEDARKAEEARKAEDAKKAEAAR--KAEEVRKAEELrKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKK 1231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1454 RHLERALEERRRQEEEMQRELEAAQ-REARGLGTELFRLQHSHEEALEALETLKRENKNLQEEISDlTDQLSLSGKSIQE 1532
Cdd:PTZ00121 1232 AEEAKKDAEEAKKAEEERNNEEIRKfEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKK-AEEKKKADEAKKK 1310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1533 LEKAKKALEGEKSEIQAALEEAEGALELEETKTlriQLELSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAET 1612
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKK---AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA 1387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1613 RARNEALRLKKKMEGDLNDLElQLGHATRQATEAQAATRLMQAQLKEEQAGRD-EEQRLAAELREQAQALERRAALLAAE 1691
Cdd:PTZ00121 1388 EEKKKADEAKKKAEEDKKKAD-ELKKAAAAKKKADEAKKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAKKAEEAKKKA 1466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1692 LEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKleADLAQlSGEVEEAAQERREAEEKAKkaiTDAAM 1771
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK--ADEAK-KAEEAKKADEAKKAEEAKK---ADEAK 1540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1772 MAEELKKEQDTSAhLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKgvRKHE 1851
Cdd:PTZ00121 1541 KAEEKKKADELKK-AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK--KAEE 1617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1852 RRVK-ELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEE----AEQQANTNLAKYRKAQhELDDAEERADMAETQANK 1926
Cdd:PTZ00121 1618 AKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkikAAEEAKKAEEDKKKAE-EAKKAEEDEKKAAEALKK 1696
|
570
....*....|....*
gi 1622840248 1927 LRARTRDALGPKHKE 1941
Cdd:PTZ00121 1697 EAEEAKKAEELKKKE 1711
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1576-1941 |
2.72e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.03 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1576 KAEVDRKLAEKDEECANLRRNHQ-RAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQ 1654
Cdd:PTZ00121 1116 KAEEAKKKAEDARKAEEARKAEDaRKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRK 1195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1655 AQ--LKEEQAGRDEEQRLAAELREQAQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLN 1732
Cdd:PTZ00121 1196 AEdaRKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1733 QKKKLE----------ADLAQLSGEVEEAAQERREAEEK-----AKKAITDAAMMAEELKKEQdtsahlERMKKTLEQTV 1797
Cdd:PTZ00121 1276 EARKADelkkaeekkkADEAKKAEEKKKADEAKKKAEEAkkadeAKKKAEEAKKKADAAKKKA------EEAKKAAEAAK 1349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1798 RELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDK 1877
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE 1429
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622840248 1878 LQsKVKSYKRQFEEAEQ--QANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDALGPKHKE 1941
Cdd:PTZ00121 1430 KK-KADEAKKKAEEAKKadEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEE 1494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
921-1284 |
4.62e-14 |
|
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: 78.17 E-value: 4.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 921 QLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLT 1000
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1001 KEKKALqeahqqalgdlqaeEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADATQDK 1080
Cdd:TIGR02168 761 AEIEEL--------------EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1081 QQLEEKLKKKDSELSQLSLRVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEA 1160
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1161 GGASAGQREGSRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAA 1240
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGP 986
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1622840248 1241 -NVETLTRAKASAEK---LCRTYEDqLSEAKIKVEELQRQLADASTQR 1284
Cdd:TIGR02168 987 vNLAAIEEYEELKERydfLTAQKED-LTEAKETLEEAIEEIDREARER 1033
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
852-1548 |
8.96e-14 |
|
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: 77.42 E-value: 8.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 852 AEEELAALRAELRGLRGALAAAEAKRQELEETHVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKV-QLEGKVKELS 930
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIaSLERSIAEKE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 931 ERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAH 1010
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1011 QQA---LGDLQAEEDRvsaLTKAKLRLEQQVEDLECSLEqekklrmDTERAKRKLEGDLKLTQESVADATQDKQQLEEKL 1087
Cdd:TIGR02169 395 EKLkreINELKRELDR---LQEELQRLSEELADLNAAIA-------GIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1088 KKKDSELSQLSL---RVEDEQllgAQLQKKIKELQARAEELEEELEAERAARARVEKQR-------AEAARELEELSERL 1157
Cdd:TIGR02169 465 SKYEQELYDLKEeydRVEKEL---SKLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvAQLGSVGERYATAI 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1158 EEAGGASAG------------------QREGSRKREAELGRLRRELEEAALRHEATV----------------------- 1196
Cdd:TIGR02169 542 EVAAGNRLNnvvveddavakeaiellkRRKAGRATFLPLNKMRDERRDLSILSEDGVigfavdlvefdpkyepafkyvfg 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1197 ---------AALR-----------------------------------RKQAEGAAELGEQVDSLQRVRQKLEKEKSELR 1232
Cdd:TIGR02169 622 dtlvvedieAARRlmgkyrmvtlegelfeksgamtggsraprggilfsRSEPAELQRLRERLEGLKRELSSLQSELRRIE 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1233 MEVDDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSHLLEEKECLISQLSrgK 1312
Cdd:TIGR02169 702 NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE--E 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1313 ALAAQSLEELRrqleeeskaksalaHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEaDAIQRTEE 1392
Cdd:TIGR02169 780 ALNDLEARLSH--------------SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ-ELQEQRID 844
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1393 LEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQR 1472
Cdd:TIGR02169 845 LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1473 ELEAAQREARGLGTELFRLQHSHEEALeALETLKRENKNLQEEISDL-------TDQLSLSGKSIQELEKAKKALEGEKS 1545
Cdd:TIGR02169 925 KLEALEEELSEIEDPKGEDEEIPEEEL-SLEDVQAELQRVEEEIRALepvnmlaIQEYEEVLKRLDELKEKRAKLEEERK 1003
|
...
gi 1622840248 1546 EIQ 1548
Cdd:TIGR02169 1004 AIL 1006
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
917-1806 |
1.35e-13 |
|
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: 76.55 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 917 KSKVQLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESV 996
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 997 ARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLeQQVEDLECSLEQEKKlrmdtERAKRKLEGDLKLTQESVADA 1076
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKL-QEEELKLLAKEEEEL-----KSELLKLERRKVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1077 TQDKQQLEEKLKKKDSELSQLslrvedeqllgaqlqKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSER 1156
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEEL---------------EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1157 LEeagGASAGQREGSRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVD 1236
Cdd:pfam02463 385 RL---SSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1237 DLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELqRQLADASTQRGRLQTESGELSHLLEEKECLISQLSRGKALAA 1316
Cdd:pfam02463 462 KDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER-SQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEN 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1317 QSLEELRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQwrSKYEADAIQRTEELEEA 1396
Cdd:pfam02463 541 YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDP--ILNLAQLDKATLEADED 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1397 KKKLALRLQEAEEGVEAanakcSSLEKAKLRLQTESEDVTLELERA----TSAAAALDKKQRHLERALEERRRQEEEMQR 1472
Cdd:pfam02463 619 DKRAKVVEGILKDTELT-----KLKESAKAKESGLRKGVSLEEGLAekseVKASLSELTKELLEIQELQEKAESELAKEE 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1473 ELEAAQREARGLGTELFRLQHSHEEALEALETLKRENKNLQEEISDLTDQLSLSgKSIQELEKAKKALEGEKSEIQAALE 1552
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDE-EEEEEEKSRLKKEEKEEEKSELSLK 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1553 EAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEEC-ANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLND 1631
Cdd:pfam02463 773 EKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELkEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLA 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1632 LELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELREQAQALERRAALLAAELeelraaleqgERSRRLAEQ 1711
Cdd:pfam02463 853 EEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLE----------EKENEIEER 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1712 ELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERM-- 1789
Cdd:pfam02463 923 IKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLee 1002
|
890
....*....|....*....
gi 1622840248 1790 --KKTLEQTVRELQARLEE 1806
Cdd:pfam02463 1003 ekKKLIRAIIEETCQRLKE 1021
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
30-75 |
6.17e-13 |
|
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: 64.76 E-value: 6.17e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1622840248 30 DGKKRVWVPDEQDAYVEAEVKSEaTGGRVTVETKDQKVLTVREAEL 75
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEE-EGDKVTVETEDGKTVTVKKDDV 45
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1175-1930 |
1.83e-12 |
|
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: 72.79 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1175 EAELGRLRRELEEAALRHEATVAALRrkqaegaaELGEQVDSLQRVRQKLEKEKsELRMEVDDLAANVetLTRAKASAEK 1254
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIID--------EKRQQLERLRREREKAERYQ-ALLKEKREYEGYE--LLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1255 LCRTYEDQLSEAKIKVEELQRQLADastqrgrLQTESGELSHLLEEKECLISQLSRGKALAAQSLeelrrqleeeskaks 1334
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISE-------LEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEK--------------- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1335 alahavqalrhdcdllreqheeeaeaqaelqrlLSKANAEVAQWRSKyEADAIQRTEELEEAKKKLALRLQEAEEGVEAA 1414
Cdd:TIGR02169 296 ---------------------------------IGELEAEIASLERS-IAEKERELEDAEERLAKLEAEIDKLLAEIEEL 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1415 NAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRLQHS 1494
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEE 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1495 HEEALEALETLKRENKNLQEEISDLTDQLSlsgKSIQELEKAKKALEGEKSEIqaaleeaegalELEETKTLRIQLELSQ 1574
Cdd:TIGR02169 422 LADLNAAIAGIEAKINELEEEKEDKALEIK---KQEWKLEQLAADLSKYEQEL-----------YDLKEEYDRVEKELSK 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1575 VKAEVDRKLAEKDE---------------------------ECANLRRNHQRAVES-----LQASLDAETRARNEALRLK 1622
Cdd:TIGR02169 488 LQRELAEAEAQARAseervrggraveevlkasiqgvhgtvaQLGSVGERYATAIEVaagnrLNNVVVEDDAVAKEAIELL 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1623 KKMEG-------------------------------DLNDLELQLGHATRQA-------TEAQAATRLM--------QAQ 1656
Cdd:TIGR02169 568 KRRKAgratflplnkmrderrdlsilsedgvigfavDLVEFDPKYEPAFKYVfgdtlvvEDIEAARRLMgkyrmvtlEGE 647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1657 LKEEQ----AGRDEEQRL---AAELREQAQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTG 1729
Cdd:TIGR02169 648 LFEKSgamtGGSRAPRGGilfSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1730 LLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMkkTLEQTVRELQARLEEAEq 1809
Cdd:TIGR02169 728 LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--LSHSRIPEIQAELSKLE- 804
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1810 aalrggkKQVQKLEAKVRELEAELDAE-------QKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKV 1882
Cdd:TIGR02169 805 -------EEVSRIEARLREIEQKLNRLtlekeylEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 1622840248 1883 KSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRAR 1930
Cdd:TIGR02169 878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
847-1119 |
1.13e-11 |
|
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: 70.48 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 847 LRSAQAEEELAALRAELRGLRGALAAAEAKRQELEEthvsvtqekndlalQLQAEQDNLADAEERCHLLIKSKVQLEGKV 926
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSLQSELRRIEN--------------RLDELSQELSDASRKIGEIEKEIEQLEQEE 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 927 KELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATE-----NKVKNLTEEMAALDESVARLTK 1001
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEarlshSRIPEIQAELSKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1002 EKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADATQDKQ 1081
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
|
250 260 270
....*....|....*....|....*....|....*...
gi 1622840248 1082 QLEEKLKKKDSELSQLSLRVEDEQLLGAQLQKKIKELQ 1119
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1389-1938 |
1.54e-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: 69.82 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1389 RTEELEEAKKKLALRLQEAEEgveaanaKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEE 1468
Cdd:pfam01576 69 RKQELEEILHELESRLEEEEE-------RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDIL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1469 EMQRELEAAQREARGLGTELFRLQHSHEEALEALETLKRENKNLQEEISDLTDQLSLSGKSIQELEKAKKALEGEKSEIQ 1548
Cdd:pfam01576 142 LLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1549 AALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEECANLRRnHQRAVESLQASLDAETRARNEALRLKKKMEGD 1628
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE-LEAQISELQEDLESERAARNKAEKQRRDLGEE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1629 LNDLELQLgHATRQATEAQAATRLMQAQLKEE--QAGRDEEQRLAAELREQAQALERRAALLAAELEELRAALEQGERSR 1706
Cdd:pfam01576 301 LEALKTEL-EDTLDTTAAQQELRSKREQEVTElkKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1707 RLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAIT------------------- 1767
Cdd:pfam01576 380 QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSelesvssllneaegknikl 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1768 --DAAMMAEELKKEQDTSAHLERMKKTLEQTVRE-------LQARLEEaEQAALRGGKKQVQKLEAKVRELEAELDaEQK 1838
Cdd:pfam01576 460 skDVSSLESQLQDTQELLQEETRQKLNLSTRLRQledernsLQEQLEE-EEEAKRNVERQLSTLQAQLSDMKKKLE-EDA 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1839 KHAEALKGVRKHERRVKELAYQAEEDR--------------------------------KNLARMQDLVDKLQSKVKSYK 1886
Cdd:pfam01576 538 GTLEALEEGKKRLQRELEALTQQLEEKaaaydklektknrlqqelddllvdldhqrqlvSNLEKKQKKFDQMLAEEKAIS 617
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622840248 1887 RQFEE----AEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDALGPK 1938
Cdd:pfam01576 618 ARYAEerdrAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSK 673
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
853-1314 |
4.77e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.14 E-value: 4.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 853 EEELAALRAELRGLRGALAAAEAKRQELEETHVSVTQEKNDLALQLQAeqdnladAEERCHLLIKSKVQLEGKVKELSER 932
Cdd:PRK02224 292 EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA-------HNEEAESLREDADDLEERAEELREE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 933 LEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQ 1012
Cdd:PRK02224 365 AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1013 ALGDLQA-----------EEDRVSALTKAklrlEQQVEDLECSLEQekkLRMDTERAKRKLEgdlklTQESVADATQDKQ 1081
Cdd:PRK02224 445 AEALLEAgkcpecgqpveGSPHVETIEED----RERVEELEAELED---LEEEVEEVEERLE-----RAEDLVEAEDRIE 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1082 QLEEKLKKKDSELSQLSLRVEDEQLLGAQLQKKIKELQARAeeleeeleaeraararvEKQRAEAARELEELSERLEEAG 1161
Cdd:PRK02224 513 RLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA-----------------EEKREAAAEAEEEAEEAREEVA 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1162 GASAGQREGSRKREAeLGRLRRELEEAAlRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKlekeKSELRMEVDDlaAN 1241
Cdd:PRK02224 576 ELNSKLAELKERIES-LERIRTLLAAIA-DAEDEIERLREKREALAELNDERRERLAEKRER----KRELEAEFDE--AR 647
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622840248 1242 VETLTRAKASAEklcrTYEDQLSEakiKVEELQRQLADASTQRGRLQTESGELSHLLEEKECLISQLSRGKAL 1314
Cdd:PRK02224 648 IEEAREDKERAE----EYLEQVEE---KLDELREERDDLQAEIGAVENELEELEELRERREALENRVEALEAL 713
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
919-1301 |
7.18e-11 |
|
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: 66.84 E-value: 7.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 919 KVQLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVAR 998
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 999 LTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADATQ 1078
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1079 DKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAAreleelserle 1158
Cdd:pfam07888 193 EFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELS----------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1159 eaggASAGQREGSrkrEAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSEL-RMEVdd 1237
Cdd:pfam07888 262 ----SMAAQRDRT---QAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELqRLEE-- 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622840248 1238 lAANVETLTRAKASAE----KLCRTYedQLSEAKIKVEELQRQLADASTQRGRLQTESGEL---SHLLEEK 1301
Cdd:pfam07888 333 -RLQEERMEREKLEVElgreKDCNRV--QLSESRRELQELKASLRVAQKEKEQLQAEKQELleyIRQLEQR 400
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
872-1310 |
1.66e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.70 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 872 AAEAKRQELEETHVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNADLAARRRKLE 951
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 952 DECTELKKDIDDLEltlAKAEKEKQATENKVKnlTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAK 1031
Cdd:PTZ00121 1391 KKADEAKKKAEEDK---KKADELKKAAAAKKK--ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK 1465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1032 LRLEQQVEDLECSLEQEKKlrmdTERAKRKLEgdlkltqESVADATQDKQQLEEKlkKKDSELSQLSLRVEDEQLLGAQL 1111
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKK----ADEAKKKAE-------EAKKKADEAKKAAEAK--KKADEAKKAEEAKKADEAKKAEE 1532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1112 QKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGSRKREAELGRLRRELEEAALR 1191
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1192 HEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRA----KASAEKLCRTYEDQ--LSE 1265
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKaeedKKKAEEAKKAEEDEkkAAE 1692
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1622840248 1266 AKIKVEELQRQLADASTQRGRLQTESGELSHLLEEKECLISQLSR 1310
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
850-1050 |
2.08e-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: 64.79 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 850 AQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKEL 929
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 930 SERLED------------------EEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAA 991
Cdd:COG4942 103 KEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622840248 992 LDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKK 1050
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1212-1878 |
2.32e-10 |
|
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: 66.15 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1212 EQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRtYEDQLSEAKIKVEELQRQLA---------DAST 1282
Cdd:TIGR00618 212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK-KQQLLKQLRARIEELRAQEAvleetqeriNRAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1283 QRGRLQTESGELSHLLEEKECLISQLSRGKALAAQSLEELRRQLEEESKAKSAlAHAVQALRHDCDLLREQHEEEAEAQA 1362
Cdd:TIGR00618 291 KAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ-RRLLQTLHSQEIHIRDAHEVATSIRE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1363 ELQRLLSKANaEVAQWRSKYEADaiqrtEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEdvtLELERA 1442
Cdd:TIGR00618 370 ISCQQHTLTQ-HIHTLQQQKTTL-----TQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE---LQQRYA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1443 TSAAAALDK-------KQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRLQHSHEEALEALETLKRENKNLQEE 1515
Cdd:TIGR00618 441 ELCAAAITCtaqceklEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDI 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1516 ISDLTDQLSLSG--KSIQELEKAKKALEGEKSEIQAALEEAEGALELEETKTLRIQLELSQVKAEVDrklaekdeecaNL 1593
Cdd:TIGR00618 521 DNPGPLTRRMQRgeQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP-----------NL 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1594 RRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAE 1673
Cdd:TIGR00618 590 QNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRV 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1674 LREQAQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLN-LLHSQNTGLLNQKKKLEAD---LAQLSGEVE 1749
Cdd:TIGR00618 670 LPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDrEFNEIENASSSLGSDLAARedaLNQSLKELM 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1750 EAAQERREAEEKAKKAITDAAMMAEEL-KKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRE 1828
Cdd:TIGR00618 750 HQARTVLKARTEAHFNNNEEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQE 829
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1829 LEAELDAEQKKHAeALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKL 1878
Cdd:TIGR00618 830 EEQFLSRLEEKSA-TLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
844-1673 |
2.96e-10 |
|
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: 65.76 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 844 KPLLRSAQAEEELAALRAELRGLRGALAAA-----EAKRQELEETHVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKS 918
Cdd:pfam02463 200 LKLKEQAKKALEYYQLKEKLELEEEYLLYLdylklNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 919 KVQLEGKVKELSERLEDEEEVNADLAARRRKLEDEctELKKDIDDLELTLAKAEKEKQATENKVKnlteemaALDESVAR 998
Cdd:pfam02463 280 EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE--KLKESEKEKKKAEKELKKEKEEIEELEK-------ELKELEIK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 999 LTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLEcsleqEKKLRMDTERAKRKLEGDLKLTQESVADATQ 1078
Cdd:pfam02463 351 REAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE-----EELELKSEEEKEAQLLLELARQLEDLLKEEK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1079 DKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLE 1158
Cdd:pfam02463 426 KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKA 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1159 EAGGAsagqREGSRKREAELGRLRRELEEAALRHEATVAalrrkqAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDL 1238
Cdd:pfam02463 506 RSGLK----VLLALIKDGVGGRIISAHGRLGDLGVAVEN------YKVAISTAVIVEVSATADEVEERQKLVRALTELPL 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1239 AAN-VETLTRAKASAEKLCRTYE--DQLSEAKIKVEELQRQLADASTQRGRLQTESGELSHLLEEKECLISQLSRGKALA 1315
Cdd:pfam02463 576 GARkLRLLIPKLKLPLKSIAVLEidPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLE 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1316 AQSLEELRRQLEEESKAKSALAHAVQalrhdcDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADaiqrtEELEE 1395
Cdd:pfam02463 656 EGLAEKSEVKASLSELTKELLEIQEL------QEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEA-----EELLA 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1396 AKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELE 1475
Cdd:pfam02463 725 DRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELR 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1476 AAQREaRGLGTELFRLQHSHEEALEALETLKRENKNLQEEISDLTDQLSLSGKSIQELEKAKKALEGEKSEIQAALEEAE 1555
Cdd:pfam02463 805 ALEEE-LKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQK 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1556 GALE-LEETKTLRIQLELSQVKAEVDRKLAEKDEECANLRRNH---QRAVESLQASLDAETRARNEALRLKKKMEGDLND 1631
Cdd:pfam02463 884 LKDElESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEaeiLLKYEEEPEELLLEEADEKEKEENNKEEEEERNK 963
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 1622840248 1632 LELQLghatRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAE 1673
Cdd:pfam02463 964 RLLLA----KEELGKVNLMAIEEFEEKEERYNKDELEKERLE 1001
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1080-1931 |
3.60e-10 |
|
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: 65.38 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1080 KQQLEEKLKKKDSELSQL-SLRVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERle 1158
Cdd:pfam02463 168 KRKKKEALKKLIEETENLaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL-- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1159 eaggasagQREGSRKREAELGRLRRELEEAALRHEatvaalrrKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDL 1238
Cdd:pfam02463 246 --------LRDEQEEIESSKQEIEKEEEKLAQVLK--------ENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1239 AANVETLTRAKASAEKLcrtyEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSHLLEEKECLISQLSRGKALAAQS 1318
Cdd:pfam02463 310 VDDEEKLKESEKEKKKA----EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1319 LEELRRQLEEeskaksALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKK 1398
Cdd:pfam02463 386 LSSAAKLKEE------ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELK 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1399 KLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVtlELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQ 1478
Cdd:pfam02463 460 LLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE--ERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVA 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1479 REARGLGTELFRLQHSHEEALEALETLKRENKNLQEEISDLTDQLSLSGKSIQELEKAKKALEGEKSEIQAALEEAEGAL 1558
Cdd:pfam02463 538 VENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1559 ELEETKTLRIQLELSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGH 1638
Cdd:pfam02463 618 DDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRR 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1639 ATRQATEAQAATRLMQAQLKEEQ---AGRDEEQRLAAELREQAQALERRAALLAAELEELRAALEQGERSRRLAEQELLE 1715
Cdd:pfam02463 698 QLEIKKKEQREKEELKKLKLEAEellADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELA 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1716 ATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKA----ITDAAMMAEELKKEQDTSAHLERMKK 1791
Cdd:pfam02463 778 EEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEekikEEELEELALELKEEQKLEKLAEEELE 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1792 TL--EQTVRELQARLEEAEQAALRGGKKQV-QKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNL 1868
Cdd:pfam02463 858 RLeeEITKEELLQELLLKEEELEEQKLKDElESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEP 937
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622840248 1869 ARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRART 1931
Cdd:pfam02463 938 EELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERL 1000
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
925-1147 |
3.70e-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: 64.01 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 925 KVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKK 1004
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1005 ALQEAHQQALGDLQaeedRVSALTKAKLRLEQQ-VEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADATQDKQQL 1083
Cdd:COG4942 101 AQKEELAELLRALY----RLGRQPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622840248 1084 EEKLKKKDSELSQLSLRVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAA 1147
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1577-1933 |
7.06e-10 |
|
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: 64.32 E-value: 7.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1577 AEVDRKLAEKDEECANLRRNHQRA---VESLQASLDAETRARNEALRLKKkMEGDLNDLELQLGHATRQATEAQAATRLM 1653
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLdliIDEKRQQLERLRREREKAERYQA-LLKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1654 Q-AQLKEEQAGRDEE-QRLAAELREQAQALERRAallaaeleelraaleqgERSRRLAEQELLEATERLNLLHSQntgll 1731
Cdd:TIGR02169 245 QlASLEEELEKLTEEiSELEKRLEEIEQLLEELN-----------------KKIKDLGEEEQLRVKEKIGELEAE----- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1732 nqKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEE--AEQ 1809
Cdd:TIGR02169 303 --IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1810 AALRGGKKQVQ-KLEAKVRELEaELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNL-ARMQDL---VDKLQSKVKS 1884
Cdd:TIGR02169 381 AETRDELKDYReKLEKLKREIN-ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELeEEKEDKaleIKKQEWKLEQ 459
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1622840248 1885 YKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRD 1933
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
847-1290 |
1.20e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 847 LRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSVTQEKNDLALQL-QAEQDNLADAEERCHLLIKSKVQLEGK 925
Cdd:COG4913 281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 926 VKELSERLED----EEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTK 1001
Cdd:COG4913 361 RARLEALLAAlglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1002 EKKALQEAHQQALG-------------DLQAEEDR-----VSALTKAKLRL---EQQVEDLECSLEQEK-KLRMDTERAK 1059
Cdd:COG4913 441 RLLALRDALAEALGldeaelpfvgeliEVRPEEERwrgaiERVLGGFALTLlvpPEHYAAALRWVNRLHlRGRLVYERVR 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1060 RklegdlklTQESVADATQDKQQLEEKLKKKDSELS-----QLSLR-----VEDEQ------------------------ 1105
Cdd:COG4913 521 T--------GLPDPERPRLDPDSLAGKLDFKPHPFRawleaELGRRfdyvcVDSPEelrrhpraitragqvkgngtrhek 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1106 ----------LLG-------AQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGgasagqr 1168
Cdd:COG4913 593 ddrrrirsryVLGfdnraklAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS------- 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1169 egsrkREAELGRLRRELEEAalrhEATVAALRRKQAEgAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRA 1248
Cdd:COG4913 666 -----AEREIAELEAELERL----DASSDDLAALEEQ-LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1622840248 1249 KASAEKLCRTYEDQLSEAKIK-----------VEELQRQLADASTQRGRLQTE 1290
Cdd:COG4913 736 LEAAEDLARLELRALLEERFAaalgdaverelRENLEERIDALRARLNRAEEE 788
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
841-1287 |
2.52e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 841 FKMKPLLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEEthvsvtqekndlalqlqaeqdnladaeerchlLIKSKV 920
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE--------------------------------LKKKLK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 921 QLEGKVKELSERLEDEEEVNAdLAARRRKLEDECTELkkDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLT 1000
Cdd:PRK03918 349 ELEKRLEELEERHELYEEAKA-KKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1001 KEKKALQEAHQQ--ALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRmdteRAKRKLEGDLKLTQESVADATQ 1078
Cdd:PRK03918 426 KAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLR----KELRELEKVLKKESELIKLKEL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1079 DKQ--QLEEKLKKKDSE-----------LSQLSLRVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARARVEKQRAE 1145
Cdd:PRK03918 502 AEQlkELEEKLKKYNLEelekkaeeyekLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1146 AARELEELSERLEEAGGASAGQREGSRKREAELGRLRRELEEAALRHEATVAALRRKQAEgAAELGEQVDSLQRV----- 1220
Cdd:PRK03918 582 LGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKR-LEELRKELEELEKKyseee 660
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1221 RQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRTYEDQL---SEAKIKVEELQRQLADASTQRGRL 1287
Cdd:PRK03918 661 YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELeerEKAKKELEKLEKALERVEELREKV 730
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
850-1058 |
4.05e-09 |
|
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: 62.01 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 850 AQAEEELAALRAELRG-----LRGALAAAEAKRQELEETHVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEG 924
Cdd:TIGR02169 775 HKLEEALNDLEARLSHsripeIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 925 KVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKV-------KNLTEEMAALDESVA 997
Cdd:TIGR02169 855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIekkrkrlSELKAKLEALEEELS 934
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622840248 998 RLTKEKKALQE--AHQQALGDLQAE----EDRVSALTKAKLRLEQQVEDLECSLE--QEKKLRMDTERA 1058
Cdd:TIGR02169 935 EIEDPKGEDEEipEEELSLEDVQAElqrvEEEIRALEPVNMLAIQEYEEVLKRLDelKEKRAKLEEERK 1003
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
852-1041 |
4.57e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 852 AEEELAALRAELRGLRGALAAAEAKRQELEETHVSVTQEKNDLA--LQLQAEQDNLADAEERCHllikskvqlegkvkEL 929
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIA--------------EL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 930 SERLEDEEEVNADLAARRRKLEdectELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKA---- 1005
Cdd:COG4913 674 EAELERLDASSDDLAALEEQLE----ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelra 749
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622840248 1006 -LQEAHQQALGDLQAE------EDRVSALTKAKLRLEQQVEDL 1041
Cdd:COG4913 750 lLEERFAAALGDAVERelrenlEERIDALRARLNRAEEELERA 792
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
854-1048 |
5.89e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 5.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 854 EELAALRAELRGLRGALAAAEAKR---QELEETHVSVTQEKNDLA-LQLQAEQDNLADAEERCHLLIKSKVQLEGKVKEL 929
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIellEPIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 930 SERLEDEEEVNADLAARRRKLEDECTELK-KDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQE 1008
Cdd:COG4913 308 EAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622840248 1009 AHQQALGDLQAEEDRVS-ALTKAKLRLEQQVEDLEcSLEQE 1048
Cdd:COG4913 388 EAAALLEALEEELEALEeALAEAEAALRDLRRELR-ELEAE 427
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
844-1310 |
1.04e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 844 KPLLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSVTQEKNdlalQLQAEQDNLADAEERCHLLIKSKvQLE 923
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELE----ELREELEKLEKLLQLLPLYQELE-ALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 924 GKVKELSERLE---DEEEVNADLAARRRKLEDECTELKKDIDDLEltlakaEKEKQATENKVKNLTEEMAALDESVARLT 1000
Cdd:COG4717 139 AELAELPERLEeleERLEELRELEEELEELEAELAELQEELEELL------EQLSLATEEELQDLAEELEELQQRLAELE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1001 KEKKALQEAHQQalgdlqaeedrvsaltkaklrLEQQVEDLECSLEQEKKlrmdtERAKRKLEGDLKLTQESVADATQDK 1080
Cdd:COG4717 213 EELEEAQEELEE---------------------LEEELEQLENELEAAAL-----EERLKEARLLLLIAAALLALLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1081 QQLEEKLKKKDSELSQLSLRVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEA 1160
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1161 GGAsagqregsRKREAELGRLRRELEEAALRHEATvAALRRKQAEGAAELGEQVDSLQRvRQKLEKEKSELRMEVDDLAA 1240
Cdd:COG4717 347 EEL--------QELLREAEELEEELQLEELEQEIA-ALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLG 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622840248 1241 NVETLTRAKASAEklcrtYEDQLSEAKIKVEELQRQLADASTQRGRLQTE------SGELSHLLEEKECLISQLSR 1310
Cdd:COG4717 417 ELEELLEALDEEE-----LEEELEELEEELEELEEELEELREELAELEAEleqleeDGELAELLQELEELKAELRE 487
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
850-1307 |
1.78e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 850 AQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSVTQekndLALQLQAEQDNLADAEERchlliksKVQLEGKVKEL 929
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE----LEKELESLEGSKRKLEEK-------IRELEERIEEL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 930 SERLEDEEEVNADLaARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEa 1009
Cdd:PRK03918 272 KKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1010 hqqALGDLQAEEDRVSALTKAKL---RLEQQVEDLEC-SLEQEKKLRMDTERAKRKLEGDLKLTQESVADATQDKQQLE- 1084
Cdd:PRK03918 350 ---LEKRLEELEERHELYEEAKAkkeELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKk 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1085 --EKLKKKDSE--LSQLSLRVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEA 1160
Cdd:PRK03918 427 aiEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1161 GGASAGQREGSRKREAElGRLRRELEEAALRHEATVAALrRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLA- 1239
Cdd:PRK03918 507 ELEEKLKKYNLEELEKK-AEEYEKLKEKLIKLKGEIKSL-KKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGf 584
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622840248 1240 ANVETLTRAKASAEKLCRTY------EDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSHLLEEKECLISQ 1307
Cdd:PRK03918 585 ESVEELEERLKELEPFYNEYlelkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
850-1295 |
2.06e-08 |
|
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: 59.80 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 850 AQAEEELAALRAELRGLRGALAAAEAKRQELeethvsvTQEKNDLALQLQAEQDNLADaEERCHLLIKSKV-QLEGKVKE 928
Cdd:pfam01576 429 AELAEKLSKLQSELESVSSLLNEAEGKNIKL-------SKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLrQLEDERNS 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 929 LSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQE 1008
Cdd:pfam01576 501 LQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQ 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1009 AHQQALGDLQAEEDRVSALTKAKLRLEQQVEDlecslEQEKKLRMDTERAKRKLEGDLKLTQE-SVADATQDKQQLEEKL 1087
Cdd:pfam01576 581 ELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAE-----EKAISARYAEERDRAEAEAREKETRAlSLARALEEALEAKEEL 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1088 KKKDSelsqlSLRVEDEQLLGAQ--LQKKIKELQARAEELEEELEAERAARARVEK--QRAEAARELEELSERLEEAG-- 1161
Cdd:pfam01576 656 ERTNK-----QLRAEMEDLVSSKddVGKNVHELERSKRALEQQVEEMKTQLEELEDelQATEDAKLRLEVNMQALKAQfe 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1162 -GASAGQREGSRKREAELGRLRR-ELEEAALRHEATVAALRRKQAEG-AAELGEQVDSLQRVRQKLEKEKSELRMEVDDL 1238
Cdd:pfam01576 731 rDLQARDEQGEEKRRQLVKQVRElEAELEDERKQRAQAVAAKKKLELdLKELEAQIDAANKGREEAVKQLKKLQAQMKDL 810
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622840248 1239 AANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELS 1295
Cdd:pfam01576 811 QRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELA 867
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1438-1930 |
2.27e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1438 ELERATSAAAAL----DKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRLQHSHEEALEALETLKRENKNLQ 1513
Cdd:COG4913 243 ALEDAREQIELLepirELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1514 EEISDLTDQL-SLSGKSIQELEKAKKALEGEKSEIQaaleeaegaleleetktlRIQLELSQVKAEVDRKLAEKDEECAN 1592
Cdd:COG4913 323 EELDELEAQIrGNGGDRLEQLEREIERLERELEERE------------------RRRARLEALLAALGLPLPASAEEFAA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1593 LRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQAT----EAQAATRLMQAQLKEEQA------ 1662
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSnipaRLLALRDALAEALGLDEAelpfvg 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1663 ------GRDEEQRLAAE--LREQA--------------------QALERRAALLAAELEELRAALEQGERS--------- 1705
Cdd:COG4913 465 elievrPEEERWRGAIErvLGGFAltllvppehyaaalrwvnrlHLRGRLVYERVRTGLPDPERPRLDPDSlagkldfkp 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1706 ---RRLAEQEL--------------LEATER---LNLLHSQNTGL--LNQKKKLEAD----------LAQLSGEVEEAAQ 1753
Cdd:COG4913 545 hpfRAWLEAELgrrfdyvcvdspeeLRRHPRaitRAGQVKGNGTRheKDDRRRIRSRyvlgfdnrakLAALEAELAELEE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1754 ERREAEEKAKKAitdaammAEELKKEQDTSAHLERMKKTL--EQTVRELQARLEEAEQ--AALRGGKKQVQKLEAKVREL 1829
Cdd:COG4913 625 ELAEAEERLEAL-------EAELDALQERREALQRLAEYSwdEIDVASAEREIAELEAelERLDASSDDLAALEEQLEEL 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1830 EAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQskVKSYKRQFEEAEQQANTNLAKyRKAQHE 1909
Cdd:COG4913 698 EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL--RALLEERFAAALGDAVERELR-ENLEER 774
|
570 580
....*....|....*....|.
gi 1622840248 1910 LDDAEERADMAETQANKLRAR 1930
Cdd:COG4913 775 IDALRARLNRAEEELERAMRA 795
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
892-1118 |
3.74e-08 |
|
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: 58.49 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 892 NDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKA 971
Cdd:TIGR04523 310 KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 972 EKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKL 1051
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622840248 1052 RMDTERAKRKLEGDLKLTQESVADATQD-------KQQLEEKLKKKDSELSQLSLRVEDEQLLGAQLQKKIKEL 1118
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKELKSKEKElkklneeKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1591-1814 |
3.81e-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: 57.85 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1591 ANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQL----KEEQAGRDE 1666
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1667 EQRLAAELREQAQALERRAALLAAELEELRAALEQGERSRRL------AEQELLEA-TERLNLLHSQNTGLLNQKKKLEA 1739
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYlkylapARREQAEElRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622840248 1740 DLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRG 1814
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1709-1936 |
3.97e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1709 AEQELLEATERLNLLhsqntgllnqkkkleADLAQLSGEVEEAAQERREAEE-----KAKKAITDAAMMAEELKKEQDTS 1783
Cdd:COG4913 240 AHEALEDAREQIELL---------------EPIRELAERYAAARERLAELEYlraalRLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1784 AHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQkleakvrELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEE 1863
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGNGGDRLE-------QLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622840248 1864 DRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELddAEERADMAETQAN------KLRARTRDALG 1936
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL--EAEIASLERRKSNiparllALRDALAEALG 454
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1167-1802 |
5.98e-08 |
|
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: 58.21 E-value: 5.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1167 QREGSRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLT 1246
Cdd:pfam15921 251 KSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1247 RAKASAEklcRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSHLLEEkecLISQL-SRGKALAAQSLEELRRQ 1325
Cdd:pfam15921 331 SELREAK---RMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQK---LLADLhKREKELSLEKEQNKRLW 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1326 LEEESKAKSalahavqalrhdCDLLREQHEEEAEAQAELQRLLSKANAEvAQWRSKYEADAIQRTEELEEAKKKLALRLQ 1405
Cdd:pfam15921 405 DRDTGNSIT------------IDHLRRELDDRNMEVQRLEALLKAMKSE-CQGQMERQMAAIQGKNESLEKVSSLTAQLE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1406 EAEEG----VEAANAKCSSLEKAKlRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQREA 1481
Cdd:pfam15921 472 STKEMlrkvVEELTAKKMTLESSE-RTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEC 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1482 RGLgtelfRLQHSHEEALEALetlkrenknLQEEISDLTDQLSLSGKSIQELEKAKKALEGEKSEiqaaleeaegalele 1561
Cdd:pfam15921 551 EAL-----KLQMAEKDKVIEI---------LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIND--------------- 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1562 etKTLRIQlELSQVKAEVDRKLAEKDEECANLRRNHQRAV----ESLQASLDAEtRARNEALRLKKKMEGDLNDL----E 1633
Cdd:pfam15921 602 --RRLELQ-EFKILKDKKDAKIRELEARVSDLELEKVKLVnagsERLRAVKDIK-QERDQLLNEVKTSRNELNSLsedyE 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1634 LQLGHATRQATEAQAATRLMQAQLKEEQAgRDEEQRLAAELREQAQALERRAALLAAELEELRAALEQGERSR-RLAEQE 1712
Cdd:pfam15921 678 VLKRNFRNKSEEMETTTNKLKMQLKSAQS-ELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKiQFLEEA 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1713 LLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEE-AAQERREAEEKAK------KAITDAAMMAEELKKEQDTSAH 1785
Cdd:pfam15921 757 MTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVlRSQERRLKEKVANmevaldKASLQFAECQDIIQRQEQESVR 836
|
650
....*....|....*..
gi 1622840248 1786 LeRMKKTLEqtVRELQA 1802
Cdd:pfam15921 837 L-KLQHTLD--VKELQG 850
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1379-1930 |
6.41e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 6.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1379 RSKYEADAIQRTEELEEakkklalRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRhler 1458
Cdd:PRK03918 177 RIERLEKFIKRTENIEE-------LIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEK---- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1459 aleerrrqeeemqrELEAAQREARGLGTELFRLQHSHEEALEALETLKRENKNLqEEISDLTDQLSLSGKSIQELEKAKK 1538
Cdd:PRK03918 246 --------------ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1539 ALEGEKSEIQAALEEAEGALELEETKTLRIQlELSQVKAEVDRKLA--EKDEECANLRRNHQRAVESLQASLDAET---- 1612
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEelEERHELYEEAKAKKEELERLKKRLTGLTpekl 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1613 -RARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAA-TRLMQAQLKEEQAGR----DEEQRLAAELREQAQALERRAA 1686
Cdd:PRK03918 390 eKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAiEELKKAKGKCPVCGRelteEHRKELLEEYTAELKRIEKELK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1687 LLAAELEelraaleqgERSRRLAEQE-LLEATERLNLLHSqntgLLNQKKKLEADLAQLSGE-VEEAAQERREAEEKAKK 1764
Cdd:PRK03918 470 EIEEKER---------KLRKELRELEkVLKKESELIKLKE----LAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIK 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1765 AITDAAMMAEELKKEQDtsahLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEaELDAEQKKHAEAL 1844
Cdd:PRK03918 537 LKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAE 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1845 KGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNL-----AKYRKAQHELDDAEERADM 1919
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEylelsRELAGLRAELEELEKRREE 691
|
570
....*....|.
gi 1622840248 1920 AETQANKLRAR 1930
Cdd:PRK03918 692 IKKTLEKLKEE 702
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
926-1602 |
6.74e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 6.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 926 VKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVknlTEEMAALDEsvARLTKEKKA 1005
Cdd:PTZ00121 1229 VKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK---AEEKKKADE--AKKAEEKKK 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1006 LQEAHQQALGDLQAEEDRVSA------LTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADATQD 1079
Cdd:PTZ00121 1304 ADEAKKKAEEAKKADEAKKKAeeakkkADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA 1383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1080 KQQLEEKlkKKDSELSQlslRVEDEQllgaqlqKKIKELQARAEeleeeleaeraararvEKQRAEAAreleelserlee 1159
Cdd:PTZ00121 1384 KKKAEEK--KKADEAKK---KAEEDK-------KKADELKKAAA----------------AKKKADEA------------ 1423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1160 aggasagQREGSRKREAElgRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKselrmEVDDLA 1239
Cdd:PTZ00121 1424 -------KKKAEEKKKAD--EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK-----KADEAK 1489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1240 ANVEtltRAKASAEKLCRTyedqlSEAKIKVEELQRQLADASTQRGRLQTESGELSHLLEEKEclisqLSRGKALAAQSL 1319
Cdd:PTZ00121 1490 KKAE---EAKKKADEAKKA-----AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE-----KKKADELKKAEE 1556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1320 EELRRQLEEESKAKSALAHAVQALRHdCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKK 1399
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRK-AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1400 LALRLQEAEEgveaanakcsslekaklrlQTESEDVTLELERATSAAAALDKKQRHLERAleerrrqEEEMQRELEAAQR 1479
Cdd:PTZ00121 1636 EQLKKKEAEE-------------------KKKAEELKKAEEENKIKAAEEAKKAEEDKKK-------AEEAKKAEEDEKK 1689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1480 EARGLGTE------LFRLQHSHEEALEALETLKRENKNLQEEISDLTDQLSLSGKSIQELEKAkkalEGEKSEIQAALEE 1553
Cdd:PTZ00121 1690 AAEALKKEaeeakkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD----EEEKKKIAHLKKE 1765
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1622840248 1554 AEGALELEETKTLRIQLElsQVKAEVDRKLAEKDEECANLRRNHQRAVE 1602
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAVIEE--ELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1703-1926 |
1.18e-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: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1703 ERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDT 1782
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1783 SAHLER-MKKTLEQTVRELQARLEEAEQAALRGG--KKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAY 1859
Cdd:COG4942 106 LAELLRaLYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622840248 1860 QAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANK 1926
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
842-1254 |
1.50e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 842 KMKPLLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEEthvsvtqekndLALQLQAEQDNLADAEERC-HLLIKSKV 920
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE-----------LEEELEELEAELAELQEELeELLEQLSL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 921 QLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTE-EMAALDESVARL 999
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAaALLALLGLGGSL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1000 TKEKKALQEAHQQALGDLQAEedrVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADATQD 1079
Cdd:COG4717 269 LSLILTIAGVLFLVLGLLALL---FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1080 KQQLEEKLKKKDSELSQLSLrvedeqllgAQLQKKIKELqaRAEELEEELEAERAARARVEKQRAEAARELEELSERLEE 1159
Cdd:COG4717 346 IEELQELLREAEELEEELQL---------EELEQEIAAL--LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEEL 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1160 AGGASAGQREGSRKR-EAELGRLRRELEEAALRHEatvaALRRKQAEGAAELG--EQVDSLQRVRQKLEKEKSELRMEVD 1236
Cdd:COG4717 415 LGELEELLEALDEEElEEELEELEEELEELEEELE----ELREELAELEAELEqlEEDGELAELLQELEELKAELRELAE 490
|
410 420
....*....|....*....|.
gi 1622840248 1237 DLAAN---VETLTRAKASAEK 1254
Cdd:COG4717 491 EWAALklaLELLEEAREEYRE 511
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
842-1026 |
2.29e-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: 53.78 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 842 KMKPLLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSVTQEKNDLALQLQAEQDNLADAEERchllikskvq 921
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 922 lEGKVKELSERLEDEEEVNAdlaarrrkledecteLKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTK 1001
Cdd:COG1579 75 -IKKYEEQLGNVRNNKEYEA---------------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138
|
170 180
....*....|....*....|....*
gi 1622840248 1002 EKKALQEAHQQALGDLQAEEDRVSA 1026
Cdd:COG1579 139 ELEEKKAELDEELAELEAELEELEA 163
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
922-1519 |
2.34e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 922 LEGKVKELSERLEDEEEVNADLAARRRKLED----------ECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAA 991
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEvleeheerreELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 992 LDESVARLTKE---KKALQEAHQQALGDLQAEEDRV-SALTKAKLRLEQQVEDLECSLEQEKKLRmdtERAKRKLEGDLK 1067
Cdd:PRK02224 291 LEEERDDLLAEaglDDADAEAVEARREELEDRDEELrDRLEECRVAAQAHNEEAESLREDADDLE---ERAEELREEAAE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1068 LTQEsVADATQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAA 1147
Cdd:PRK02224 368 LESE-LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1148 RELEELSERLEEAGGASAGQREGSRKREAELGRLRRELEEAALRHEATVAALRRkqAEGAAELGEQVDSLQRVRQKLEKE 1227
Cdd:PRK02224 447 ALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER--AEDLVEAEDRIERLEERREDLEEL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1228 KSELRMEVDDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTEsgelshlleekeclISQ 1307
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKER--------------IES 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1308 LSRGKALAAqsleelrrqleeeskaksalahAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAI 1387
Cdd:PRK02224 591 LERIRTLLA----------------------AIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARI 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1388 qrteelEEAKKKLalrlQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERatsaaaaldkkqrhleraleerrrqe 1467
Cdd:PRK02224 649 ------EEAREDK----ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE-------------------------- 692
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1622840248 1468 eemqreLEAAQREARGLgtelfrlqhshEEALEALETLKRENKNLQEEISDL 1519
Cdd:PRK02224 693 ------LEELRERREAL-----------ENRVEALEALYDEAEELESMYGDL 727
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
853-1117 |
2.35e-07 |
|
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: 55.67 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 853 EEELAALRAELRGLRGALAAAEAKRQELEETHVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSER 932
Cdd:pfam07888 79 ESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKER 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 933 -------LEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVAR---LTKE 1002
Cdd:pfam07888 159 akkagaqRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEneaLLEE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1003 KKALQE---AHQQA-------LGDLQAEEDRVSA-LTKAKLRLEQ---QVEDLECSLEQEK--------KLRMDTERAKR 1060
Cdd:pfam07888 239 LRSLQErlnASERKveglgeeLSSMAAQRDRTQAeLHQARLQAAQltlQLADASLALREGRarwaqereTLQQSAEADKD 318
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622840248 1061 KLE---GDLKLTQESVADATQDKQQLEEKL-KKKDSELSQLSLRVEDEQLLGAQLQKKIKE 1117
Cdd:pfam07888 319 RIEklsAELQRLEERLQEERMEREKLEVELgREKDCNRVQLSESRRELQELKASLRVAQKE 379
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1697-1898 |
3.62e-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: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1697 AALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAE-- 1774
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRqp 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1775 --ELKKEQDTSAHLERMKKTLEQTVRELQARLEEAeQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHER 1852
Cdd:COG4942 121 plALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL-RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQK 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622840248 1853 RVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANT 1898
Cdd:COG4942 200 LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1368-1928 |
5.57e-07 |
|
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: 54.73 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1368 LSKANAEVAQWRSKYEADAIQRTEELEEAKKKLalrlqEAEEgveaanakcssleKAKLRLQTESEDVTLELERATSAAA 1447
Cdd:pfam05483 83 LYKEAEKIKKWKVSIEAELKQKENKLQENRKII-----EAQR-------------KAIQELQFENEKVSLKLEEEIQENK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1448 ALDKKQ---RHLERALEERRRQEEEMQRELEAAQREARGLGTEL--------------------------FRLQHSHEEA 1498
Cdd:pfam05483 145 DLIKENnatRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLnnniekmilafeelrvqaenarlemhFKLKEDHEKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1499 LEALETLKRENKNLQEEISDLTDQLSLSGKSIQEL-----EKAKKALE-GEKSEIQAALEEAEGALELEETKTLR----- 1567
Cdd:pfam05483 225 QHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLtflleESRDKANQlEEKTKLQDENLKELIEKKDHLTKELEdikms 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1568 IQLELSQVKA-EVDRKLAEK-------DEECANLRRNHQRAVESLQAS-LDAETRARNEALRL-KKKMEGDLNDLELQLG 1637
Cdd:pfam05483 305 LQRSMSTQKAlEEDLQIATKticqlteEKEAQMEELNKAKAAHSFVVTeFEATTCSLEELLRTeQQRLEKNEDQLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1638 HATRQATEAQAATRL----------MQAQLKEEQAGRDEE---QRLAAELREQAQALERRAALLAAELEELRAALEQGER 1704
Cdd:pfam05483 385 ELQKKSSELEEMTKFknnkeveleeLKKILAEDEKLLDEKkqfEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKT 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1705 SRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSA 1784
Cdd:pfam05483 465 SEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEM 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1785 HL----ERMKKTLEQTVRELQARLEEAEQAAlRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQ 1860
Cdd:pfam05483 545 NLrdelESVREEFIQKGDEVKCKLDKSEENA-RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK 623
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622840248 1861 AEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLR 1928
Cdd:pfam05483 624 GSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQ 691
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
853-1318 |
7.04e-07 |
|
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: 54.74 E-value: 7.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 853 EEELAALRAELRGLRGALAAAEAKR--QELEETHVSVT---QEKNDLALQLQAEQDNLADAEErchlliKSKVQLEGKVK 927
Cdd:pfam15921 244 EDQLEALKSESQNKIELLLQQHQDRieQLISEHEVEITgltEKASSARSQANSIQSQLEIIQE------QARNQNSMYMR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 928 ELSERLEDEEEVNADLAARRRKLEDECTELKKD--IDDLELTLAKAEKEKQATENkvKNLTEEMAALdesVARLTKEKKA 1005
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQLQKL---LADLHKREKE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1006 LQEAHQQ--------------------ALGDLQAEEDRVSALTKA-----KLRLEQQVEDLEC---SLEQEKKLRMDTER 1057
Cdd:pfam15921 393 LSLEKEQnkrlwdrdtgnsitidhlrrELDDRNMEVQRLEALLKAmksecQGQMERQMAAIQGkneSLEKVSSLTAQLES 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1058 AK---RKLEGDL---KLTQES----VADATQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQLQKKIKELQARAEELEE 1127
Cdd:pfam15921 473 TKemlRKVVEELtakKMTLESsertVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEA 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1128 ELEAERAARARVEKQRAEAARELEELSERLEEAGgasAGQREGSrKREAELGRLRRELEEAALRHEATVAALRRKQAEGA 1207
Cdd:pfam15921 553 LKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAG---AMQVEKA-QLEKEINDRRLELQEFKILKDKKDAKIRELEARVS 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1208 AELGEQVDSLQRVRQKLEKEKsELRMEVDDLAANVET----LTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQ 1283
Cdd:pfam15921 629 DLELEKVKLVNAGSERLRAVK-DIKQERDQLLNEVKTsrneLNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSE 707
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1622840248 1284 ----RGRLQTESGELSHLLEEKECLISQLS--RGKALAAQS 1318
Cdd:pfam15921 708 leqtRNTLKSMEGSDGHAMKVAMGMQKQITakRGQIDALQS 748
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1474-1917 |
7.61e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 7.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1474 LEAAQREARGLGTELFRLQHSHEEALEALETLKRENKNLQEEISDLTDQLSLSGKSIQELEKAKKALEGEKSEIQAALEE 1553
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1554 aegaleleetktlriqLELSQVKAEVDRKLAEKDEECANLR------RNHQRAVESLQASLDAETRARNEALR-LKKKME 1626
Cdd:COG4717 128 ----------------LPLYQELEALEAELAELPERLEELEerleelRELEEELEELEAELAELQEELEELLEqLSLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1627 GDLNDLELQLGHATRQATEAQAATRLMQAQLK--EEQAGRDEEQRLAAELREQAQALE---------------------- 1682
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEelEEELEQLENELEAAALEERLKEARlllliaaallallglggsllsl 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1683 -------------------RRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQ 1743
Cdd:COG4717 272 iltiagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1744 LSGEVEEAAQERR-EAEEKAKKAITDAAMMA--EELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQvq 1820
Cdd:COG4717 352 LLREAEELEEELQlEELEQEIAALLAEAGVEdeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE-- 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1821 kLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELayqaEEDrknlarmqDLVDKLQSKVKSYKRQFEEAEQQAntnl 1900
Cdd:COG4717 430 -LEEELEELEEELEELEEELEELREELAELEAELEQL----EED--------GELAELLQELEELKAELRELAEEW---- 492
|
490
....*....|....*..
gi 1622840248 1901 AKYRKAQHELDDAEERA 1917
Cdd:COG4717 493 AALKLALELLEEAREEY 509
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1490-1936 |
8.48e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1490 RLQHSHEEALEALETL--KRENKNLQEEISDLTDQLSLSGKSIQELEKAKKALEGEKSEIQAALEEAEGAleleetktlr 1567
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQieEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER---------- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1568 iQLELSQVKAEVDrKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLghATRQATEAQ 1647
Cdd:PRK02224 250 -REELETLEAEIE-DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARR--EELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1648 AATRLMQ----AQLKEEQAGRDEEQrlAAELREQAQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLL 1723
Cdd:PRK02224 326 LRDRLEEcrvaAQAHNEEAESLRED--ADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1724 HSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAitdAAMMAE----ELKKEQDTSAHLERMKKTLEQtVRE 1799
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA---EALLEAgkcpECGQPVEGSPHVETIEEDRER-VEE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1800 LQARLEEAEQaalrggkkQVQKLEAKVRELEAELDAEqkKHAEALKGVRKH-ERRVKELAYQAEEDRKNLARMQDLVDKL 1878
Cdd:PRK02224 480 LEAELEDLEE--------EVEEVEERLERAEDLVEAE--DRIERLEERREDlEELIAERRETIEEKRERAEELRERAAEL 549
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622840248 1879 QSKVKSYKRQFEEAEQQANT---NLAKYRKAQHELDDAEERADMAETQANkLRARTRDALG 1936
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEareEVAELNSKLAELKERIESLERIRTLLA-AIADAEDEIE 609
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1654-1892 |
8.52e-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: 53.61 E-value: 8.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1654 QAQLKEEQAGRDEEQRLAAELREQAQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQ 1733
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1734 KKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKeqdTSAHLERMKKTLEQTVRELQARLEEAEQAalr 1813
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKY---LAPARREQAEELRADLAELAALRAELEAE--- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622840248 1814 ggKKQVQKLEAKVRELEAELDAEQKKHAEALKgvrKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEA 1892
Cdd:COG4942 173 --RAELEALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1389-1892 |
1.03e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1389 RTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRhleraleerrrqee 1468
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE-------------- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1469 eMQRELEAAQREARGLgtelfrlqhshEEALEALETLKRENKNLQEEISDLTDQLSLSGKSIQELEKAKkALEGEKSEIQ 1548
Cdd:PRK03918 312 -IEKRLSRLEEEINGI-----------EERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAK-AKKEELERLK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1549 AALEEAEGALELEETKtlriqlELSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETR--------ARNEALR 1620
Cdd:PRK03918 379 KRLTGLTPEKLEKELE------ELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelTEEHRKE 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1621 LKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQrLAAELREQAQALERRAALLAAELEELRAALE 1700
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE-LAEQLKELEEKLKKYNLEELEKKAEEYEKLK 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1701 qgERSRRLAEQ--ELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGE--------VEEAAQERREAEE------KAKK 1764
Cdd:PRK03918 532 --EKLIKLKGEikSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEleelgfesVEELEERLKELEPfyneylELKD 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1765 AITDAAMMAEELKKEQDT----SAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKH 1840
Cdd:PRK03918 610 AEKELEREEKELKKLEEEldkaFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRR 689
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1622840248 1841 AEALKGVRKHERRVKELAyQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEA 1892
Cdd:PRK03918 690 EEIKKTLEKLKEELEERE-KAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
926-1541 |
1.16e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 926 VKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNL---TEEMAALDESVARLTKE 1002
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELeelKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1003 KKALQEahqqalgDLQAEEDRVSALTKAKLRLEQQVEDLEcSLEQEKKLRMDTERAKRKLEGDLKLTQESVADATQDKQQ 1082
Cdd:PRK03918 254 KRKLEE-------KIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1083 LEEKLKK---KDSELSQLSLRVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARARvEKQRAEAARELEELSERLEE 1159
Cdd:PRK03918 326 IEERIKEleeKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL-TPEKLEKELEELEKAKEEIE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1160 AGGASAGQREGS-RKREAELGRLRRELEEA-----ALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRm 1233
Cdd:PRK03918 405 EEISKITARIGElKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR- 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1234 EVDDLAANVETLTRAKASAEKLcRTYEDQLSeaKIKVEELQRQLADASTQRGRLQTESGELSHLLEEkeclisqLSRGKA 1313
Cdd:PRK03918 484 ELEKVLKKESELIKLKELAEQL-KELEEKLK--KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE-------LEKLEE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1314 LaaqsleelrrqleeeSKAKSALAHAVQALRhdcdllreqheeeaeaqaelqRLLSKANAEVAQWRSKYEADAIQRTEEL 1393
Cdd:PRK03918 554 L---------------KKKLAELEKKLDELE---------------------EELAELLKELEELGFESVEELEERLKEL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1394 EEAKKKLaLRLQEAEEGVEaanAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRhleraleerrrqeeemqre 1473
Cdd:PRK03918 598 EPFYNEY-LELKDAEKELE---REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK------------------- 654
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622840248 1474 lEAAQREARGLGTELFRLQHSHEEALEALETLKRENKNLQEEISDLTDQLSLSGKSIQELEKAKKALE 1541
Cdd:PRK03918 655 -KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
854-1248 |
1.24e-06 |
|
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: 53.80 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 854 EELAALRAELRGLRGALAAAEAKRQELEETHVSVTQEKNDLALQLQAEQDNLAdaeerchlLIKSKVQLEGK-------V 926
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLN--------LVQTALRQQEKieryqedL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 927 KELSERLEDEEEVNADLAARRrkledectelkkdiddleltlAKAEKEKQATENKVKNLTEEMA----ALDESVARLTKE 1002
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQL---------------------AEAEARLEAAEEEVDSLKSQLAdyqqALDVQQTRAIQY 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1003 KKALQ---EAHQQ-ALGDLQAE--EDRVSALtkaKLRLEQQVEDLecsLEQEKKLRmDTERAKRKLEGDLKLTQESV--- 1073
Cdd:COG3096 416 QQAVQaleKARALcGLPDLTPEnaEDYLAAF---RAKEQQATEEV---LELEQKLS-VADAARRQFEKAYELVCKIAgev 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1074 --ADATQDKQQL-------------EEKLKKKDSELSQLSLRVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARAR 1138
Cdd:COG3096 489 erSQAWQTARELlrryrsqqalaqrLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1139 VEKQRAEAAReleelserleeaggasagQREGSRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQ 1218
Cdd:COG3096 569 LEEQAAEAVE------------------QRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTA 630
|
410 420 430
....*....|....*....|....*....|
gi 1622840248 1219 RVRQKLEKEKsELRMEVDDLAANVETLTRA 1248
Cdd:COG3096 631 AMQQLLERER-EATVERDELAARKQALESQ 659
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1495-1935 |
1.70e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1495 HEEALEALETLKRENKNLqEEISDLTDQLSLSGKSIQELEKAKKALEGEKSEIQAALEEAEGALELEETKtlRIQLELSQ 1574
Cdd:COG4913 237 LERAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELA--RLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1575 VKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQ 1654
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1655 AQLKEEQAGRDEEQRLAAELREQAQALERRAALLAAELEELRAALEQGERSRR--LAEQ------------ELLE----- 1715
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRdaLAEAlgldeaelpfvgELIEvrpee 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1716 -----ATERlnLLHSQNTGLL--------------NQKKKLEADLAQLSGEVEEAAQERREAE----------------- 1759
Cdd:COG4913 474 erwrgAIER--VLGGFALTLLvppehyaaalrwvnRLHLRGRLVYERVRTGLPDPERPRLDPDslagkldfkphpfrawl 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1760 -------------------EKAKKAITDAAMM-----AEELKKEQDTSAHL------ERMKKTLEQTVRELQARLEEAEQ 1809
Cdd:COG4913 552 eaelgrrfdyvcvdspeelRRHPRAITRAGQVkgngtRHEKDDRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEE 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1810 aalrggkkQVQKLEAKVRELEAELDAEQK--KHAEALKGVRKHERRVKELayqaEEDRKNLARMQDLVDKLQSKVKSYKR 1887
Cdd:COG4913 632 --------RLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAEL----EAELERLDASSDDLAALEEQLEELEA 699
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1622840248 1888 QFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDAL 1935
Cdd:COG4913 700 ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
655-682 |
2.13e-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: 49.65 E-value: 2.13e-06
10 20
....*....|....*....|....*...
gi 1622840248 655 SQLHKENLNKLMTNLRATQPHFVRCIVP 682
Cdd:cd01363 143 FEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
1747-1858 |
2.21e-06 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 51.91 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1747 EVEEAAQERREAEEKAKKAITDAAMMAEELkkeqdtsahlERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEaKV 1826
Cdd:pfam07767 206 EAEKKRLKEEEKLERVLEKIAESAATAEAR----------EEKRKTKAQRNKEKRRKEEEREAKEEKALKKKLAQLE-RL 274
|
90 100 110
....*....|....*....|....*....|..
gi 1622840248 1827 RELEAELDAEQKKHAEALKGVRKHERRVKELA 1858
Cdd:pfam07767 275 KEIAKEIAEKEKEREEKAEARKREKRKKKKEE 306
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
848-1659 |
2.73e-06 |
|
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: 52.66 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 848 RSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVS----VTQEKNDLALQLQAEQDNLADAEERCHLLIkskvQLE 923
Cdd:TIGR00618 98 RSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLkldyKTFTRVVLLPQGEFAQFLKAKSKEKKELLM----NLF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 924 GKvkELSERLEDEEEVNADLAARRRKLEDECTELKKDidDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEK 1003
Cdd:TIGR00618 174 PL--DQYTQLALMEFAKKKSLHGKAELLTLRSQLLTL--CTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1004 KALQEAH--QQALGDLQAEEDRVSALTKaklRLEQQVEdlecsleqekklRMDTERAKRKLEGDLKLTQESVADATQDKQ 1081
Cdd:TIGR00618 250 EAQEEQLkkQQLLKQLRARIEELRAQEA---VLEETQE------------RINRARKAAPLAAHIKAVTQIEQQAQRIHT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1082 QLEEKLKKKDSELSQLSLRVEDEQLLGAQlQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEag 1161
Cdd:TIGR00618 315 ELQSKMRSRAKLLMKRAAHVKQQSSIEEQ-RRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTL-- 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1162 gasagqREGSRKREAELGRLRRELEEAALRHeatvAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAAN 1241
Cdd:TIGR00618 392 ------TQKLQSLCKELDILQREQATIDTRT----SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1242 VETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTES-----GELSHLLEEKECLISQLSRGKALAA 1316
Cdd:TIGR00618 462 QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIhpnpaRQDIDNPGPLTRRMQRGEQTYAQLE 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1317 QSLEELRRQLEEESKAKSALAHAVQALRHDCDLLreqheeeaeaqaELQRLLSKANAEVAQwrsKYEADAIQRTEELEEA 1396
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIL------------TQCDNRSKEDIPNLQ---NITVRLQDLTEKLSEA 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1397 KKKLALRLQEAEEGVEAANAKcssLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERA-LEERRRQEEEMQRELE 1475
Cdd:TIGR00618 607 EDMLACEQHALLRKLQPEQDL---QDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSiRVLPKELLASRQLALQ 683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1476 AAQREARGLGTELFRLQHSHEEALEALETLKRENKNLQE-------EISDLTDQLSLSGKSIQELEKAKKALEGEKSEIQ 1548
Cdd:TIGR00618 684 KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEienasssLGSDLAAREDALNQSLKELMHQARTVLKARTEAH 763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1549 AALEEAEGALELEETKTLRIQLELS---QVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKM 1625
Cdd:TIGR00618 764 FNNNEEVTAALQTGAELSHLAAEIQffnRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSAT 843
|
810 820 830
....*....|....*....|....*....|....
gi 1622840248 1626 EGDLNDLELQLGHATRQATEAQAATRLMQAQLKE 1659
Cdd:TIGR00618 844 LGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1388-1898 |
2.82e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1388 QRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQE 1467
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1468 EEMQRELEAAQREARGLGTELFRLQHSHEEALEALETLKRENKNLQEEISDLTDQLSLSGKSIQELEKA--KKALEGEKS 1545
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgDAPVDLGNA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1546 EIQAALEEAEGALELEETKTLRIQL-ELSQVKAEVDRKLAE-KDEECAnlrrnhQRAVESLQASLDAETRARNEALRLK- 1622
Cdd:PRK02224 411 EDFLEELREERDELREREAELEATLrTARERVEEAEALLEAgKCPECG------QPVEGSPHVETIEEDRERVEELEAEl 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1623 KKMEGDLNDLELQLGHATR-QATEAQAATRLMQA----QLKEEQAGRDEEQRL-AAELREQAQALERRAALLAAELEELr 1696
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDlVEAEDRIERLEERRedleELIAERRETIEEKRErAEELRERAAELEAEAEEKREAAAEA- 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1697 aaleqgersrRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSgEVEEAAQERREAEEKakkaitdaamMAEEL 1776
Cdd:PRK02224 564 ----------EEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIA-DAEDEIERLREKREA----------LAELN 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1777 KKEQDTSAHLERMKKTLEQTVRElqARLEEAEQAALRgGKKQVQKLEAKVRELEAELDAEQKkhaeALKGVrkhERRVKE 1856
Cdd:PRK02224 623 DERRERLAEKRERKRELEAEFDE--ARIEEAREDKER-AEEYLEQVEEKLDELREERDDLQA----EIGAV---ENELEE 692
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1622840248 1857 LayqaEEDRKNLARMQDLVDKLQSkvksykrQFEEAEQQANT 1898
Cdd:PRK02224 693 L----EELRERREALENRVEALEA-------LYDEAEELESM 723
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
895-1545 |
3.13e-06 |
|
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: 52.53 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 895 ALQLQAEQDNLADAEERCHLLIKSKVQLEgkvKELSERLEDEEEVNADLAARRRKLEDECTELKkdiddleltlAKAEKE 974
Cdd:pfam12128 243 FTKLQQEFNTLESAELRLSHLHFGYKSDE---TLIASRQEERQETSAELNQLLRTLDDQWKEKR----------DELNGE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 975 KQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQAL----GDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKK 1050
Cdd:pfam12128 310 LSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLpswqSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNN 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1051 L---RMDTERAKRKLEGDLKLTQESvadatQDKQQLEEKLKkkdSELSQLSLRVEDEQLLGAQLQKKIKELQARAEELEE 1127
Cdd:pfam12128 390 RdiaGIKDKLAKIREARDRQLAVAE-----DDLQALESELR---EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1128 ELEAERAARARVEKQRAE---AARELEELSERLEEAGGASAGQREGSRKREAELGRLRRELEEAALRHEA---TVAALRR 1201
Cdd:pfam12128 462 LLLQLENFDERIERAREEqeaANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPqagTLLHFLR 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1202 KQAEGAAE-LGEQVDSLQRVRQKLEKEKSEL----------------RMEVDDLAANVETLTRAKASAEKLCRT------ 1258
Cdd:pfam12128 542 KEAPDWEQsIGKVISPELLHRTDLDPEVWDGsvggelnlygvkldlkRIDVPEWAASEEELRERLDKAEEALQSarekqa 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1259 -YEDQLSEAKIKVEELQRQLADASTQrgrLQTESGELSHLLEEKECLisQLSRGKALAAQSLEELRRQLEEESKAKSALA 1337
Cdd:pfam12128 622 aAEEQLVQANGELEKASREETFARTA---LKNARLDLRRLFDEKQSE--KDKKNKALAERKDSANERLNSLEAQLKQLDK 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1338 HAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKlalrlQEAEEGVEaanak 1417
Cdd:pfam12128 697 KHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKR-----DLASLGVD----- 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1418 csslEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARGlgtELFRLQHSHEE 1497
Cdd:pfam12128 767 ----PDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQ---QLARLIADTKL 839
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1622840248 1498 ALEALETLKRENKNLQEEISDLTDQLSLSGKSIQELEKAKKALEGEKS 1545
Cdd:pfam12128 840 RRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGS 887
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
976-1232 |
3.50e-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: 51.69 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 976 QATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLEcslEQEKKLRMDT 1055
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE---AELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1056 ERAKRKLEGDLKLTQESVADATQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQLQKKIKELQAraeeleeeleaeraA 1135
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA--------------D 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1136 RARVEKQRAEAAReleelserleeaggasagQREGSRKREAELGRLRRELEEAALRHEATVAALRRKQAEGA---AELGE 1212
Cdd:COG4942 159 LAELAALRAELEA------------------ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAaelAELQQ 220
|
250 260
....*....|....*....|
gi 1622840248 1213 QVDSLQRVRQKLEKEKSELR 1232
Cdd:COG4942 221 EAEELEALIARLEAEAAAAA 240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1732-1933 |
4.03e-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: 51.30 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1732 NQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQ-- 1809
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAel 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1810 AALRGG-KKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQ 1888
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622840248 1889 FEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRD 1933
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1653-1933 |
4.83e-06 |
|
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: 51.71 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1653 MQAQLKEEQAGRDEEQRLAAELRE----QAQALERRAALLAAELEELRAALEQGERSRRLA------EQELLEATERLNL 1722
Cdd:pfam01576 7 MQAKEEELQKVKERQQKAESELKElekkHQQLCEEKNALQEQLQAETELCAEAEEMRARLAarkqelEEILHELESRLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1723 LHSQNTGLLNQKKKLEADLAQLSG--EVEEAAQERREAEekakKAITDAAM--MAEELKKEQDTSAHLERMKKTLEQTVR 1798
Cdd:pfam01576 87 EEERSQQLQNEKKKMQQHIQDLEEqlDEEEAARQKLQLE----KVTTEAKIkkLEEDILLLEDQNSKLSKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1799 ELQARLEEAEQAAlRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKL 1878
Cdd:pfam01576 163 EFTSNLAEEEEKA-KSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1622840248 1879 QSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRD 1933
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRD 296
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
868-1101 |
5.51e-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: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 868 GALAAAEAKRQELEETHVSVTQEKNDLAlQLQAEQDNLADAEERchlLIKSKVQLEGKVKELSERLEDEEEVNADLAARR 947
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELA-ALKKEEKALLKQLAA---LERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 948 RKLEDECTELKKDIDDLeltLAKAEKEKQATENKVKNLTEEMAALDESVA---RLTKEKKALQEAHQQALGDLQAEEDRV 1024
Cdd:COG4942 93 AELRAELEAQKEELAEL---LRALYRLGRQPPLALLLSPEDFLDAVRRLQylkYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622840248 1025 SALTKAKLRLEQQVEDLECSLEQEKKLRmdtERAKRKLEGDLKLTQESVADATQDKQQLEEKLKKKDSELSQLSLRV 1101
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1748-1887 |
5.69e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.40 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1748 VEEAAQERREAE--EKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQaalrggkkQVQKLEAK 1825
Cdd:COG2433 378 IEEALEELIEKElpEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDE--------RIERLERE 449
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622840248 1826 VRELEAELDAEQKKHAEalkgVRKHERRVKELayqaeedRKNLARMQDLVDKLQSKVKSYKR 1887
Cdd:COG2433 450 LSEARSEERREIRKDRE----ISRLDREIERL-------ERELEEERERIEELKRKLERLKE 500
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
846-1103 |
5.82e-06 |
|
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: 51.71 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 846 LLRSAQAEEELAALRAELRGLRGALAAAE-AKRQeleethvsVTQEKNDLalqlqaeQDNLADAEERCHLLIKSKVQLEG 924
Cdd:pfam01576 825 LAQSKESEKKLKNLEAELLQLQEDLAASErARRQ--------AQQERDEL-------ADEIASGASGKSALQDEKRRLEA 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 925 KVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVArlTKEKK 1004
Cdd:pfam01576 890 RIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK--SKFKS 967
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1005 ALQEahqqalgdlqaeedrvsaltkaklrLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADATQDKQQLE 1084
Cdd:pfam01576 968 SIAA-------------------------LEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYK 1022
|
250
....*....|....*....
gi 1622840248 1085 EKLKKKDSELSQLSLRVED 1103
Cdd:pfam01576 1023 DQAEKGNSRMKQLKRQLEE 1041
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
941-1177 |
6.72e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 941 ADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAE 1020
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1021 EDRVS---ALTKAK--LRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADATQDKQQLEEKLKKKDSELS 1095
Cdd:COG3883 99 GGSVSyldVLLGSEsfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1096 QLSLRVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGSRKRE 1175
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAA 258
|
..
gi 1622840248 1176 AE 1177
Cdd:COG3883 259 AG 260
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1366-1916 |
8.19e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 8.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1366 RLLSKANAEVAQWRSkyeADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKL--------RLQTESEDVTL 1437
Cdd:COG4913 276 YLRAALRLWFAQRRL---ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggdrleQLEREIERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1438 ELERATSAAAALDKKQRHLERALEERRRQEEEMQREleaAQREARGLGTELFRLQHSHEEALEALETLKRENKNLQEEIs 1517
Cdd:COG4913 353 ELEERERRRARLEALLAALGLPLPASAEEFAALRAE---AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI- 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1518 dltDQLSLSGKSI-QELEKAKKALEGEkseiqaaleeaegalELEETKTLRIQLELSQVKAE-------VDRKL------ 1583
Cdd:COG4913 429 ---ASLERRKSNIpARLLALRDALAEA---------------LGLDEAELPFVGELIEVRPEeerwrgaIERVLggfalt 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1584 ---AEKDEECAN--LRRNHQRA---VESLQASLDAETRARNEALRLKKKMEGDLND----LELQLGH-------ATRQA- 1643
Cdd:COG4913 491 llvPPEHYAAALrwVNRLHLRGrlvYERVRTGLPDPERPRLDPDSLAGKLDFKPHPfrawLEAELGRrfdyvcvDSPEEl 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1644 -TEAQAATRlmQAQLKEEQA----------------GRDEEQRLAAeLREQAQalerraallaaeleelraaleQGERSR 1706
Cdd:COG4913 571 rRHPRAITR--AGQVKGNGTrhekddrrrirsryvlGFDNRAKLAA-LEAELA---------------------ELEEEL 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1707 RLAEQELLEATERLNLLHSQNTGLLNQKKKLEA--DLAQLSGEVEEAAQERREAeEKAKKAITDAAMMAEELKKEQDTsa 1784
Cdd:COG4913 627 AEAEERLEALEAELDALQERREALQRLAEYSWDeiDVASAEREIAELEAELERL-DASSDDLAALEEQLEELEAELEE-- 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1785 hLERMKKTLEQTVRELQARLEEAEQaalrggkkQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEED 1864
Cdd:COG4913 704 -LEEELDELKGEIGRLEKELEQAEE--------ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEER 774
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1622840248 1865 RKNL-ARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEER 1916
Cdd:COG4913 775 IDALrARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEED 827
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1181-1888 |
8.35e-06 |
|
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: 51.27 E-value: 8.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1181 LRRELEEAALRHEAtVAALRRKQAEGAAELGEQvdsLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLC---- 1256
Cdd:pfam15921 115 LQTKLQEMQMERDA-MADIRRRESQSQEDLRNQ---LQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLqeir 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1257 ------------RTYE-DQLSEAKIK-----VEELQRQL-ADASTQRGRLQTESGELSHLLEEK----ECLISQ-LSRGK 1312
Cdd:pfam15921 191 silvdfeeasgkKIYEhDSMSTMHFRslgsaISKILRELdTEISYLKGRIFPVEDQLEALKSESqnkiELLLQQhQDRIE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1313 ALAAQSLEELRRQLEEESKAKSAlAHAVQALrhdcdlLREQHEEEAEAQAELQRLLSKANAEVAQWRSkyeadaiqrteE 1392
Cdd:pfam15921 271 QLISEHEVEITGLTEKASSARSQ-ANSIQSQ------LEIIQEQARNQNSMYMRQLSDLESTVSQLRS-----------E 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1393 LEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQR 1472
Cdd:pfam15921 333 LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSI 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1473 ELEAAQREARGLGTELFRLqhshEEALEALET-----LKRENKNLQ------EEISDLTDQLSLSG----KSIQELEKAK 1537
Cdd:pfam15921 413 TIDHLRRELDDRNMEVQRL----EALLKAMKSecqgqMERQMAAIQgkneslEKVSSLTAQLESTKemlrKVVEELTAKK 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1538 KALEGEKSEIQAALEEAEGALELEETKtlriQLELSQVKAEVDRKLAE----KDEEcanlrrNHQRAVESLQASLDAETR 1613
Cdd:pfam15921 489 MTLESSERTVSDLTASLQEKERAIEAT----NAEITKLRSRVDLKLQElqhlKNEG------DHLRNVQTECEALKLQMA 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1614 ARNEALRLKKKMEGDLNDLelqLGHATRQAteaqAATRLMQAQLKEEQAGRDEEQRLAAELREQAQALERRAALLAAELE 1693
Cdd:pfam15921 559 EKDKVIEILRQQIENMTQL---VGQHGRTA----GAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1694 ELRAALEQGERSRRLAEQELLEATERLnllhsqntglLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMA 1773
Cdd:pfam15921 632 LEKVKLVNAGSERLRAVKDIKQERDQL----------LNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQL 701
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1774 E----ELKKEQDTSAHLER-----------MKKTLEQT---VRELQARLEEAEQAaLRGGKKQVQKLEAKVRELEAELDA 1835
Cdd:pfam15921 702 KsaqsELEQTRNTLKSMEGsdghamkvamgMQKQITAKrgqIDALQSKIQFLEEA-MTNANKEKHFLKEEKNKLSQELST 780
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1836 ---EQKKHAEALKGVRKHERRVKELAYQAEE--DRKNL--ARMQDLVDKLQSKVKSYKRQ 1888
Cdd:pfam15921 781 vatEKNKMAGELEVLRSQERRLKEKVANMEValDKASLqfAECQDIIQRQEQESVRLKLQ 840
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1709-1907 |
9.98e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 9.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1709 AEQELLEATERLNLLHSQNtGLLN---QKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAh 1785
Cdd:COG3206 187 LRKELEEAEAALEEFRQKN-GLVDlseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPV- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1786 lermKKTLEQTVRELQARLEEAEQaalRGGKK--QVQKLEAKVRELEAELDAEQKKHAEALKG-VRKHERRVKELAYQAE 1862
Cdd:COG3206 265 ----IQQLRAQLAELEAELAELSA---RYTPNhpDVIALRAQIAALRAQLQQEAQRILASLEAeLEALQAREASLQAQLA 337
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622840248 1863 EDRKNLARMQdlvdKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQ 1907
Cdd:COG3206 338 QLEARLAELP----ELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1756-1897 |
1.18e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1756 REAEEKAKKAITDAAMMAEELKKEQDTSA--HLERMKKTLEQTVRE-------LQARLEEAEQA---ALRGGKKQVQKLE 1823
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAkeEIHKLRNEFEKELRErrnelqkLEKRLLQKEENldrKLELLEKREEELE 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622840248 1824 AKVRELEAELDAEQKKHAEALKGVRKHERRVKELA-YQAEEDRKNLarMQDLVDKLQSKVKSYKRQFE-EAEQQAN 1897
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEEQLQELERISgLTAEEAKEIL--LEKVEEEARHEAAVLIKEIEeEAKEEAD 187
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1703-1912 |
1.31e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 50.29 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1703 ERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAE------EKAKKAIT--------- 1767
Cdd:PLN02939 141 EKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEileeqlEKLRNELLirgateglc 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1768 --------------------DAAMMAEELKKEQDTS---AHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEA 1824
Cdd:PLN02939 221 vhslskeldvlkeenmllkdDIQFLKAELIEVAETEervFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWWE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1825 KVRELEAELDAEQKKHAEA---LKGVRKHERRVKELAYQAEEdrKNLARMQ-DLVDKLQSKVKSYKRQFEEAEQQANTNL 1900
Cdd:PLN02939 301 KVENLQDLLDRATNQVEKAalvLDQNQDLRDKVDKLEASLKE--ANVSKFSsYKVELLQQKLKLLEERLQASDHEIHSYI 378
|
250
....*....|..
gi 1622840248 1901 AKYRKAQHELDD 1912
Cdd:PLN02939 379 QLYQESIKEFQD 390
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
844-1548 |
1.45e-05 |
|
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: 50.43 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 844 KPLLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSVTQEkndlaLQLQAEQDNLADAEErchllikSKVQLE 923
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS-----LATRLELDGFERGPF-------SERQIK 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 924 GKVKELSERLEDE----EEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARL 999
Cdd:TIGR00606 394 NFHTLVIERQEDEaktaAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1000 TKEKKALqeahQQALGDLQAEEDrvSALTKAKLRLEQQVEDLECSLEQeKKLRMDTERAKRKLEGDLKLTQESVADATQD 1079
Cdd:TIGR00606 474 LELDQEL----RKAERELSKAEK--NSLTETLKKEVKSLQNEKADLDR-KLRKLDQEMEQLNHHTTTRTQMEMLTKDKMD 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1080 KQQLEEKLKKKDS-ELSQLSLRVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLE 1158
Cdd:TIGR00606 547 KDEQIRKIKSRHSdELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYED 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1159 EAGGASagqreGSRKREAELGRLRRELEEAAlRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDL 1238
Cdd:TIGR00606 627 KLFDVC-----GSQDEESDLERLKEEIEKSS-KQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDL 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1239 AANVETLTRAKASAEKLCRTYEDQLSEAKIKVE----ELQRQLADASTQRGRLQ---TESGELSHLLEEKECLISQLSRG 1311
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPgrqsIIDLKEKEIPELRNKLQkvnRDIQRLKNDIEEQETLLGTIMPE 780
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1312 KALAA--------------QSLEELRRQLEEESKAKSA-LAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVA 1376
Cdd:TIGR00606 781 EESAKvcltdvtimerfqmELKDVERKIAQQAAKLQGSdLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQ 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1377 QWRSKYE---------ADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELEraTSAAA 1447
Cdd:TIGR00606 861 HLKSKTNelkseklqiGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKE--TSNKK 938
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1448 ALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRLQHSHEEALEALETLKRENKNLQEEI-------SDLT 1520
Cdd:TIGR00606 939 AQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIdtqkiqeRWLQ 1018
|
730 740 750
....*....|....*....|....*....|
gi 1622840248 1521 DQLSLSGKS--IQELEKAKKALEGEKSEIQ 1548
Cdd:TIGR00606 1019 DNLTLRKREneLKEVEEELKQHLKEMGQMQ 1048
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
853-1071 |
1.66e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 853 EEELAALRAELRglrgalaAAEAKRQELEETH--VSVTQEKNDLALQLQAEQDNLADAEERchlliksKVQLEGKVKELS 930
Cdd:COG3206 181 EEQLPELRKELE-------EAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAE-------LAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 931 ERLEDEEEVNADLAArrrklEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAh 1010
Cdd:COG3206 247 AQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEA- 320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622840248 1011 qqalgDLQAEEDRVSALTKAKLRLEQQVEDLEcSLEQE-KKLRMDTERAKRKLEGDLKLTQE 1071
Cdd:COG3206 321 -----ELEALQAREASLQAQLAQLEARLAELP-ELEAElRRLEREVEVARELYESLLQRLEE 376
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1576-1904 |
1.68e-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: 49.74 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1576 KAEVDRKLAEKDEECANL--RRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLelqlghatRQATEAQAATRLM 1653
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVerRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--------RQEERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1654 QAQLKEEQAGRDEEQRLAAELREQAQALERRAALLAAELEElraaleQGERSRRLAEQELleatERLNLLHSQNTGLLNQ 1733
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKIL------EEERQRKIQQQKV----EMEQIRAEQEEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1734 KKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERM-KKTLEQTVRE-LQARLEEAEQAA 1811
Cdd:pfam17380 437 VRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQrRKILEKELEErKQAMIEEERKRK 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1812 LRggKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRkheRRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFE- 1890
Cdd:pfam17380 517 LL--EKEMEERQKAIYEEERRREAEEERRKQQEMEER---RRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEy 591
|
330
....*....|....
gi 1622840248 1891 EAEQQANTNLAKYR 1904
Cdd:pfam17380 592 EATTPITTIKPIYR 605
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
952-1203 |
1.78e-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: 49.38 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 952 DECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEahqqalgDLQAEEDRVSALTKAK 1031
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ-------ELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1032 LRLEQQVEDLEcslEQEKKLRMDTERAKRKLEGDLKLTQESVADATQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQL 1111
Cdd:COG4942 93 AELRAELEAQK---EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1112 QKKIKELQARAEELEEELEAeraararVEKQRAEAARELEELSERLEEAGGASAGQREGSRKREAELGRLRRELEEAALR 1191
Cdd:COG4942 170 EAERAELEALLAELEEERAA-------LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
250
....*....|..
gi 1622840248 1192 HEATVAALRRKQ 1203
Cdd:COG4942 243 TPAAGFAALKGK 254
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1490-1930 |
1.79e-05 |
|
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: 50.12 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1490 RLQHSHEEALEALETLKRENKN-------LQEEISDLT-------DQLSLSGKSIQELEKAKKALEGEKSEIQAALEEAE 1555
Cdd:pfam15921 118 KLQEMQMERDAMADIRRRESQSqedlrnqLQNTVHELEaakclkeDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1556 GALELEETKTLRIQ-LELSQVKAEVDRKLAEKDEECANLRrNHQRAVESLQASLDAETRARNEAL--RLKKKMEGDLNDL 1632
Cdd:pfam15921 198 EASGKKIYEHDSMStMHFRSLGSAISKILRELDTEISYLK-GRIFPVEDQLEALKSESQNKIELLlqQHQDRIEQLISEH 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1633 ELQLGHATRQATEAQAATRLMQAQLK--EEQAgRDEEQRLAAELREQAQALERRAALLAAELEELRAALEQGERSRRLAE 1710
Cdd:pfam15921 277 EVEITGLTEKASSARSQANSIQSQLEiiQEQA-RNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAN 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1711 QELLEATERLNLLHSQNTGLLNQKKKLEADLaqlsgeveeaaqERREAEEKAKKaitdaammaEELKK--EQDTSAHLer 1788
Cdd:pfam15921 356 SELTEARTERDQFSQESGNLDDQLQKLLADL------------HKREKELSLEK---------EQNKRlwDRDTGNSI-- 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1789 mkkTLEQTVRELQARleeaeqaalrggKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNL 1868
Cdd:pfam15921 413 ---TIDHLRRELDDR------------NMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEML 477
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622840248 1869 ARmqdLVDKLQSKvksyKRQFEEAEQQANTNLAkyrkaqhELDDAEERADMAETQANKLRAR 1930
Cdd:pfam15921 478 RK---VVEELTAK----KMTLESSERTVSDLTA-------SLQEKERAIEATNAEITKLRSR 525
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1701-1941 |
1.82e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.75 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1701 QGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQ 1780
Cdd:COG1340 26 ELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1781 DTSAHLERMKKTLEQ--------------------TVRELQARLEEAEQAAlrggkkqvqKLEAKVRELEAELDAEQKKh 1840
Cdd:COG1340 106 KAGGSIDKLRKEIERlewrqqtevlspeeekelveKIKELEKELEKAKKAL---------EKNEKLKELRAELKELRKE- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1841 aealkgVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMA 1920
Cdd:COG1340 176 ------AEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKL 249
|
250 260
....*....|....*....|..
gi 1622840248 1921 ETQANKL-RARTRDALGPKHKE 1941
Cdd:COG1340 250 RKKQRALkREKEKEELEEKAEE 271
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
842-1106 |
2.18e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 842 KMKPLLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQ 921
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 922 LEGKVKELSERLEDEEEVNADlaaRRRKLEDECTELKKDIDDLELTLAKAEKEKQATE-NKVKnlTEEMAALDESVARLT 1000
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAE---ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEeNKIK--AAEEAKKAEEDKKKA 1677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1001 KEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADATQDK 1080
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
250 260
....*....|....*....|....*...
gi 1622840248 1081 --QQLEEKLKKKDSELSQLSLRVEDEQL 1106
Cdd:PTZ00121 1758 kiAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
848-1309 |
2.44e-05 |
|
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: 49.68 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 848 RSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSVTQEKNDLALQLQAEQ-------DNLADAEERCHLLIKSKV 920
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDkefaetrDELKDYREKLEKLKREIN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 921 QLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLT 1000
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1001 KEKKALQ------EAHQQALGDLQAEEDRVSALTKAKLR--------LEQQVEDLECSLEQEKKLRM------DTERAKR 1060
Cdd:TIGR02169 483 KELSKLQrelaeaEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqLGSVGERYATAIEVAAGNRLnnvvveDDAVAKE 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1061 KLEgdlKLTQESVADAT-------QDKQQLEEKLKKK------------------------------------------- 1090
Cdd:TIGR02169 563 AIE---LLKRRKAGRATflplnkmRDERRDLSILSEDgvigfavdlvefdpkyepafkyvfgdtlvvedieaarrlmgky 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1091 -----DSELSQLS-------LRVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLE 1158
Cdd:TIGR02169 640 rmvtlEGELFEKSgamtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG 719
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1159 EA---GGASAGQREGSRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELG---------------EQVDSLQRV 1220
Cdd:TIGR02169 720 EIekeIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHkleealndlearlshSRIPEIQAE 799
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1221 RQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTE---------- 1290
Cdd:TIGR02169 800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEleeleaalrd 879
|
570 580
....*....|....*....|
gi 1622840248 1291 -SGELSHLLEEKECLISQLS 1309
Cdd:TIGR02169 880 lESRLGDLKKERDELEAQLR 899
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1474-1679 |
2.46e-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: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1474 LEAAQREARGLGTELFRLQHSHEEALEALETLKRENKNLQEEISDLTDQLSLSGKSIQELEKAKKALEGEKSEIQAALEE 1553
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1554 AEGALELEETKTlRIQLELSQ-------VKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAEtraRNEALRLKKKME 1626
Cdd:COG4942 109 LLRALYRLGRQP-PLALLLSPedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE---RAELEALLAELE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622840248 1627 GDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELREQAQ 1679
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1203-1447 |
2.62e-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: 48.61 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1203 QAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLAdasT 1282
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA---E 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1283 QRGRLQTESGELSHLLEEKECLISQLSRGKALAAQSLEELRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQA 1362
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1363 ELQRLLskanAEVAQWRSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANakcsSLEKAKLRLQTESEDVTLELERA 1442
Cdd:COG4942 175 ELEALL----AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE----ELEALIARLEAEAAAAAERTPAA 246
|
....*
gi 1622840248 1443 TSAAA 1447
Cdd:COG4942 247 GFAAL 251
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1175-1891 |
2.93e-05 |
|
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: 49.45 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1175 EAELGRLRRELEEaalrHEATVAALRRKQAEGAAELGEQVDSLQ-RVRQKLEKEKSELRMEVDDLAANVETLTRAKASAe 1253
Cdd:pfam12128 257 ELRLSHLHFGYKS----DETLIASRQEERQETSAELNQLLRTLDdQWKEKRDELNGELSAADAAVAKDRSELEALEDQH- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1254 klcRTYEDQ-LSEAKIKVEELQRQLADASTQRGRLQTESGELSHLLEEKECLISQLS-RGKALAAQSLEELRRQLEEESK 1331
Cdd:pfam12128 332 ---GAFLDAdIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKeQNNRDIAGIKDKLAKIREARDR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1332 AKSALAHAVQALrhdCDLLREQHEEEAEAQAELQRLLSKANAEVaqwrsKYEADAIQRTEELEEAKKKLALRLQEAEEGV 1411
Cdd:pfam12128 409 QLAVAEDDLQAL---ESELREQLEAGKLEFNEEEYRLKSRLGEL-----KLRLNQATATPELLLQLENFDERIERAREEQ 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1412 EAANAKCSSLEKAKLRLQTESEDVTLELERATsaAAALDKKQRHLERALEERRRQEEEMQRELEAA----QREARGLGTE 1487
Cdd:pfam12128 481 EAANAEVERLQSELRQARKRRDQASEALRQAS--RRLEERQSALDELELQLFPQAGTLLHFLRKEApdweQSIGKVISPE 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1488 LFRLQHSHEEALEAleTLKRENK----NLQEEISDLTDQLSLSGKSIQELEKAKKALEGEKSEIQaaleeaegaleleet 1563
Cdd:pfam12128 559 LLHRTDLDPEVWDG--SVGGELNlygvKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQA--------------- 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1564 ktlRIQLELSQVKAEVDR-KLAEKDEECA--NLRRNHQRAVESLQASLDAETRARNEAlrlKKKMEGDLNDLELQLghat 1640
Cdd:pfam12128 622 ---AAEEQLVQANGELEKaSREETFARTAlkNARLDLRRLFDEKQSEKDKKNKALAER---KDSANERLNSLEAQL---- 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1641 rqateaqaatrlmQAQLKEEQAGRDEEQRLAAELREQAQALERRAALLAAELEELRAALEQGERSRRLAEQELLEaTERL 1720
Cdd:pfam12128 692 -------------KQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALE-TWYK 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1721 NLLHSQntGLLNQK-KKLEADLAQLSGEVEEAAQERREAEEKAKkaitdaaMMAEELKKEQDtsaHLERMKKTLEQTVRE 1799
Cdd:pfam12128 758 RDLASL--GVDPDViAKLKREIRTLERKIERIAVRRQEVLRYFD-------WYQETWLQRRP---RLATQLSNIERAISE 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1800 LQARLEEAEQAAlrggKKQVQKLEakvRELEAeLDAEQKKHAEALKGVRKHERRVKELA--YQAEEDRKNLARMQDLVDK 1877
Cdd:pfam12128 826 LQQQLARLIADT----KLRRAKLE---MERKA-SEKQQVRLSENLRGLRCEMSKLATLKedANSEQAQGSIGERLAQLED 897
|
730
....*....|....
gi 1622840248 1878 LQSKVKSYKRQFEE 1891
Cdd:pfam12128 898 LKLKRDYLSESVKK 911
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
907-1094 |
3.09e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 907 DAEERCHLLIKSKVQLEGKVKELSERLEdeeevnaDLAARRRKLEDECTELKK--DIDDLELTLAKAEKEKQATENKVKN 984
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLE-------ALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 985 LTE---EMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDterAKRK 1061
Cdd:COG4913 680 LDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE---ERFA 756
|
170 180 190
....*....|....*....|....*....|...
gi 1622840248 1062 LEGDLKLTQESVADATQDKQQLEEKLKKKDSEL 1094
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1747-1924 |
3.17e-05 |
|
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: 48.79 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1747 EVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEE----AEQAALRGGKKQVQKL 1822
Cdd:pfam15709 349 EVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERkqrlQLQAAQERARQQQEEF 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1823 EAKVRELeaeldaEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQdlvdklQSKVKSYKRQFEEAEQqantnlak 1902
Cdd:pfam15709 429 RRKLQEL------QRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMA------EEERLEYQRQKQEAEE-------- 488
|
170 180
....*....|....*....|..
gi 1622840248 1903 yrKAQHElddAEERADMAETQA 1924
Cdd:pfam15709 489 --KARLE---AEERRQKEEEAA 505
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
849-1031 |
3.21e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 849 SAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSVTQEKNDLALQLQAEQDNLADAEERchlLIKSKVQLEGKVKE 928
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---IAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 929 LSERL------------------------------------EDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAE 972
Cdd:COG3883 88 LGERAralyrsggsvsyldvllgsesfsdfldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622840248 973 KEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAK 1031
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
921-1171 |
3.63e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 921 QLEGKVKELSERLEDEEEVNADLAARRRKLED---ECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALdesvA 997
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEElneEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER----A 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 998 RLTKEKKALQEAHQQALG--DLQAEEDRVSALTKAKLRLEQQVEDLecsleqeKKLRMDTERAKRKLEGDLKLTQESVAD 1075
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGseSFSDFLDRLSALSKIADADADLLEEL-------KADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1076 ATQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSE 1155
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
250
....*....|....*.
gi 1622840248 1156 RLEEAGGASAGQREGS 1171
Cdd:COG3883 246 AAGAGAAGAAGAAAGS 261
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1709-1925 |
4.20e-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: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1709 AEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLER 1788
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1789 MK--KTLEQTVRELQA--RLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEED 1864
Cdd:COG3883 108 LLgsESFSDFLDRLSAlsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622840248 1865 RKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQAN 1925
Cdd:COG3883 188 SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
850-1118 |
4.41e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 850 AQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLE------ 923
Cdd:PRK04863 275 MRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEkieryq 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 924 GKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDL--------------------------------------E 965
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELksqladyqqaldvqqtraiqyqqavqalerakqlcglpD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 966 LTLAKAEKEKQATENKVKNLTEEMAALDE--SVARLTKEK--KALQ------------EAHQQALGDL-QAEEDRVSALT 1028
Cdd:PRK04863 435 LTADNAEDWLEEFQAKEQEATEELLSLEQklSVAQAAHSQfeQAYQlvrkiagevsrsEAWDVARELLrRLREQRHLAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1029 KAKLRleQQVEDLECSLEQEKKLrmdtERAKRKLEGDLKLTQESVADATQDKQQLEEKLKKKDSELSQLSLRVEDEQLLG 1108
Cdd:PRK04863 515 LQQLR--MRLSELEQRLRQQQRA----ERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQL 588
|
330
....*....|
gi 1622840248 1109 AQLQKKIKEL 1118
Cdd:PRK04863 589 EQLQARIQRL 598
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1453-1882 |
6.07e-05 |
|
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: 48.19 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1453 QRHLERALEERRRQEEEMQREL----EAAQREARGLGTELFRLQHSHEE---ALEALETLKRENKNLQEeisDLTDQLSl 1525
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLnesnELHEKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQE---DLRNQLQ- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1526 sgKSIQELEKAK----KALEGEKSEI-QAALEEAEGALELEETKTLRIQLELSQVK-----------------AEVDRKL 1583
Cdd:pfam15921 149 --NTVHELEAAKclkeDMLEDSNTQIeQLRKMMLSHEGVLQEIRSILVDFEEASGKkiyehdsmstmhfrslgSAISKIL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1584 AEKDEECANLrRNHQRAVESLQASLDAETRARNEAL--RLKKKMEGDLNDLELQLGHATRQATEAQAATRLMQAQLK--E 1659
Cdd:pfam15921 227 RELDTEISYL-KGRIFPVEDQLEALKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEiiQ 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1660 EQAgRDEEQRLAAELREQAQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEA 1739
Cdd:pfam15921 306 EQA-RNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1740 DLAQLSGEVE-EAAQERREAEEKAKKAITdaammAEELKKE-QDTSAHLERMKKTLEQTVRELQARLEEaEQAALRGGKK 1817
Cdd:pfam15921 385 DLHKREKELSlEKEQNKRLWDRDTGNSIT-----IDHLRRElDDRNMEVQRLEALLKAMKSECQGQMER-QMAAIQGKNE 458
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622840248 1818 QVQKLEAKVRELEAELDAeQKKHAEALKG----VRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKV 1882
Cdd:pfam15921 459 SLEKVSSLTAQLESTKEM-LRKVVEELTAkkmtLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV 526
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
780-1118 |
6.21e-05 |
|
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: 48.18 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 780 LEELRDQRLAKVLTLLQAR----SRGRLMRLEYQRLLGGRDALFTIQWNIRafnavKNWSWMKlffKMKPLLRSAQAE-E 854
Cdd:pfam05483 337 MEELNKAKAAHSFVVTEFEattcSLEELLRTEQQRLEKNEDQLKIITMELQ-----KKSSELE---EMTKFKNNKEVElE 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 855 ELAALRAELRGLRGALAAAEAKRQELEEThvsvtqeKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLE 934
Cdd:pfam05483 409 ELKKILAEDEKLLDEKKQFEKIAEELKGK-------EQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 935 DEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQAL 1014
Cdd:pfam05483 482 KEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKG 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1015 GDLQAEEDRVsaltkaklrlEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADATQDKQQLEEKLKKKDSEL 1094
Cdd:pfam05483 562 DEVKCKLDKS----------EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQL 631
|
330 340
....*....|....*....|....
gi 1622840248 1095 SQLSLRVEDEQLLGAQLQKKIKEL 1118
Cdd:pfam05483 632 NAYEIKVNKLELELASAKQKFEEI 655
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
885-1406 |
6.37e-05 |
|
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: 48.18 E-value: 6.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 885 VSVTQEKN---DLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDI 961
Cdd:pfam05483 247 IQITEKENkmkDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 962 DDLeltlaKAEKEKQATE-NKVKN----LTEEMAALDESVARLTKEKKALQEAHQQALG----DLQAEEDRVSALTKAKL 1032
Cdd:pfam05483 327 CQL-----TEEKEAQMEElNKAKAahsfVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEEMTKFKN 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1033 RLEQQVEDLECSLEQEKKLrMDTERAKRKLEGDLKLTQesvadatqdkQQLEEKLKKKDSELSQLSLRVEDEQLLGAQLQ 1112
Cdd:pfam05483 402 NKEVELEELKKILAEDEKL-LDEKKQFEKIAEELKGKE----------QELIFLLQAREKEIHDLEIQLTAIKTSEEHYL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1113 KKIKELQARAEELEEELEAERAARARV---EKQRAEAARELEELSERLEEAGGASAGQREGSRKR----EAELGRLRREL 1185
Cdd:pfam05483 471 KEVEDLKTELEKEKLKNIELTAHCDKLlleNKELTQEASDMTLELKKHQEDIINCKKQEERMLKQienlEEKEMNLRDEL 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1186 E---EAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRTYEDQ 1262
Cdd:pfam05483 551 EsvrEEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQ 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1263 LSEAKIKVEELQRQLADASTQRGRL-QTESGELSHLLEEKECLISQLSRGKALAAQSLEELRRQLEEESKAKSALAHAVQ 1341
Cdd:pfam05483 631 LNAYEIKVNKLELELASAKQKFEEIiDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALME 710
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622840248 1342 ALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELE---EAKKKLALRLQE 1406
Cdd:pfam05483 711 KHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEiekEEKEKLKMEAKE 778
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1664-1941 |
7.50e-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: 48.02 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1664 RDEEQRLAAELREQAQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHsqnTGLLNQKK-------- 1735
Cdd:COG3096 280 RRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQ---TALRQQEKieryqedl 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1736 -KLEADLAQLSGEVEEAAQERREAEEKAKKAITDaammAEELK----------KEQDTSA--------HLERMKKTLEQT 1796
Cdd:COG3096 357 eELTERLEEQEEVVEEAAEQLAEAEARLEAAEEE----VDSLKsqladyqqalDVQQTRAiqyqqavqALEKARALCGLP 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1797 vrELQARLEEAEQAALRGgkkQVQKLEAKVRELEAEL---DAEQKKHAEALKGVRKH----ER-----RVKELAYQAEED 1864
Cdd:COG3096 433 --DLTPENAEDYLAAFRA---KEQQATEEVLELEQKLsvaDAARRQFEKAYELVCKIagevERsqawqTARELLRRYRSQ 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1865 RKNLARMQDLVDKLQ------SKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRA------RTR 1932
Cdd:COG3096 508 QALAQRLQQLRAQLAeleqrlRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEqrselrQQL 587
|
....*....
gi 1622840248 1933 DALGPKHKE 1941
Cdd:COG3096 588 EQLRARIKE 596
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
845-1119 |
7.96e-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: 48.02 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 845 PLLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSVTQ----------------EKNDLALQLQAEQDNLADA 908
Cdd:COG3096 776 PLFGRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvgghlavafapdpeaELAALRQRRSELERELAQH 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 909 EERCHLL------IKSKVQLEGKV---------KELSERLED-EEEVNADLAARR---------RKLEDECTELKKD--- 960
Cdd:COG3096 856 RAQEQQLrqqldqLKEQLQLLNKLlpqanlladETLADRLEElREELDAAQEAQAfiqqhgkalAQLEPLVAVLQSDpeq 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 961 IDDLELTLAKAEKEKQATENKVKNLTEEMA-----ALDESVARLTkEKKALQEAHQQALgdLQAEEDRvsalTKAKLRLE 1035
Cdd:COG3096 936 FEQLQADYLQAKEQQRRLKQQIFALSEVVQrrphfSYEDAVGLLG-ENSDLNEKLRARL--EQAEEAR----REAREQLR 1008
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1036 QQVEDLECSLE--------QEKKLRMDTERAKRKLEGDLKLTQESVADATQDKQQLEEKLKKKDSELSQLS---LRVEDE 1104
Cdd:COG3096 1009 QAQAQYSQYNQvlaslkssRDAKQQTLQELEQELEELGVQADAEAEERARIRRDELHEELSQNRSRRSQLEkqlTRCEAE 1088
|
330
....*....|....*
gi 1622840248 1105 QllgAQLQKKIKELQ 1119
Cdd:COG3096 1089 M---DSLQKRLRKAE 1100
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1740-1936 |
9.92e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.76 E-value: 9.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1740 DLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQdtSAHLERMKKTLEQTVRELQARleEAEQAALRGGKKQV 1819
Cdd:TIGR02794 44 DPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQR--AAEQARQKELEQRAAAEKAAK--QAEQAAKQAEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1820 QKLEAKVRELeaeldAEQKKHAEALKGVRKHErrvkELAYQAEEDRKN-----------LARMQDLVDKLQSKVKSYKRQ 1888
Cdd:TIGR02794 120 QAEEAKAKQA-----AEAKAKAEAEAERKAKE----EAAKQAEEEAKAkaaaeakkkaeEAKKKAEAEAKAKAEAEAKAK 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622840248 1889 FEEAEQQANTNLAKYRKAQHELDDAE-ERADMAETQANKLRARTRDALG 1936
Cdd:TIGR02794 191 AEEAKAKAEAAKAKAAAEAAAKAEAEaAAAAAAEAERKADEAELGDIFG 239
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
916-1251 |
1.01e-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: 47.43 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 916 IKSKVQLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEmaALDES 995
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQE--ERKRE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 996 VARLTKEKKALQEAHQQALGDLQAEEDR--------VSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAK----RKLE 1063
Cdd:pfam17380 362 LERIRQEEIAMEISRMRELERLQMERQQknervrqeLEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARqrevRRLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1064 GDLKLTQESVADATQDKQQLEEKLKKKDSELSQLSLRVEDEQllgaQLQKKIKELQARAEELEEEleaeraararvEKQR 1143
Cdd:pfam17380 442 EERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK----RDRKRAEEQRRKILEKELE-----------ERKQ 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1144 AEAARELEELSERLEEAGGASAGQREGSRKREAELGRLRRELEEAALRHEATvaalrRKQAEGAAELGEQVDSLQRVRQK 1223
Cdd:pfam17380 507 AMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQM-----RKATEERSRLEAMEREREMMRQI 581
|
330 340
....*....|....*....|....*...
gi 1622840248 1224 LEKEKSELRMEVDDLAANVETLTRAKAS 1251
Cdd:pfam17380 582 VESEKARAEYEATTPITTIKPIYRPRIS 609
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1738-1913 |
1.29e-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: 47.25 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1738 EADLAQLS---GEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLErmKKTLEQTVRELQARLEEAEQAA--- 1811
Cdd:COG3096 835 EAELAALRqrrSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLA--DETLADRLEELREELDAAQEAQafi 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1812 ----------------LRGGKKQVQKLEAKVRELEAELDaEQKKHAEALKGVRKherRVKELAYQAEEDRknLARMQDLV 1875
Cdd:COG3096 913 qqhgkalaqleplvavLQSDPEQFEQLQADYLQAKEQQR-RLKQQIFALSEVVQ---RRPHFSYEDAVGL--LGENSDLN 986
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622840248 1876 DKLqskvksyKRQFEEAEQQANTNLAKYRKAQHELDDA 1913
Cdd:COG3096 987 EKL-------RARLEQAEEARREAREQLRQAQAQYSQY 1017
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
855-1047 |
1.36e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 855 ELAALRAELRGLRGALAAAEAKRQELEETHVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSkvQLEGKVKELSERlE 934
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LLEERFAAALGD-A 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 935 DEEEVNADLAARRRKLEdecTELKKDIDDLELTLAKAekeKQATENKVKNLTEEMAALDESVARLT------------KE 1002
Cdd:COG4913 763 VERELRENLEERIDALR---ARLNRAEEELERAMRAF---NREWPAETADLDADLESLPEYLALLDrleedglpeyeeRF 836
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622840248 1003 KKALQEAHQQALGDLQaeedrvSALTKAKLRLEQQVEDLECSLEQ 1047
Cdd:COG4913 837 KELLNENSIEFVADLL------SKLRRAIREIKERIDPLNDSLKR 875
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
922-1113 |
1.52e-04 |
|
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: 46.74 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 922 LEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTK 1001
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1002 EKKALQE---AHQQALGDLQ---AEEDRV-SALTKAKLRLEQQVEDlecSLEQEKKLRMDTERAKRKLEGDLKLTQESVA 1074
Cdd:pfam10174 423 RVKSLQTdssNTDTALTTLEealSEKERIiERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTEKESSLI 499
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622840248 1075 DATQDKQQLEEKLKKKDSELSQLSL----RVEDEQLLGAQLQK 1113
Cdd:pfam10174 500 DLKEHASSLASSGLKKDSKLKSLEIaveqKKEECSKLENQLKK 542
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1670-1867 |
1.55e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1670 LAAELREQAQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLsgEVE 1749
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL--EKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1750 EAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVREL 1829
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622840248 1830 EAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKN 1867
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
967-1171 |
1.92e-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: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 967 TLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSAL----TKAKLRLEQQVEDLE 1042
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLqaeiAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1043 CSLEQEKKLRMDTERAKRKLEGD---------------LKLTQESVADATQDKQQLEEKLKKKDSELSQLSLRVEDEQLL 1107
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSEsfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622840248 1108 GAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGS 1171
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1740-1910 |
2.07e-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: 44.92 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1740 DLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAalrggkkqv 1819
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ--------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1820 QKLEAKVRELEA---ELDAEQKKHAEAlkgvrkhERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQA 1896
Cdd:COG1579 82 LGNVRNNKEYEAlqkEIESLKRRISDL-------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
170
....*....|....
gi 1622840248 1897 NTNLAKYRKAQHEL 1910
Cdd:COG1579 155 EAELEELEAEREEL 168
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
982-1455 |
2.09e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 982 VKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLEcslEQEKKLRMDTERAKRK 1061
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELE---AELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1062 LEgdlkltqesVADATQDKQQLEEKLKKKDSELSQLSLRVEDEQllgaQLQKKIKELQARAEELEEELEAERAARARVEK 1141
Cdd:COG4717 125 LQ---------LLPLYQELEALEAELAELPERLEELEERLEELR----ELEEELEELEAELAELQEELEELLEQLSLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1142 QRAEAARELEELSERLEEAggasagQREGSRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVR 1221
Cdd:COG4717 192 EELQDLAEELEELQQRLAE------LEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1222 QKLEKEKSE----LRMEVDDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSHL 1297
Cdd:COG4717 266 GSLLSLILTiagvLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1298 LEEKECLISQLSRgkalAAQSLEELRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQ 1377
Cdd:COG4717 346 IEELQELLREAEE----LEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1378 WRSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLE------KAKLRLQTESEDVTLELERATSAAAALDK 1451
Cdd:COG4717 422 LEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEedgelaELLQELEELKAELRELAEEWAALKLALEL 501
|
....
gi 1622840248 1452 KQRH 1455
Cdd:COG4717 502 LEEA 505
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
858-1113 |
2.21e-04 |
|
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: 46.28 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 858 ALRAELRGLRGALAAAEAKRQELEETHVSVTQE-----KNDLALQLQAEQDNLADAEERCHLLIKSKVQLE----GKVKE 928
Cdd:pfam07111 112 AGQAEAEGLRAALAGAEMVRKNLEEGSQRELEEiqrlhQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkraGEAKQ 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 929 LSERLEDEEEVNADLAARRRKLEDECT---ELKKDIDDL---ELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKE 1002
Cdd:pfam07111 192 LAEAQKEAELLRKQLSKTQEELEAQVTlveSLRKYVGEQvppEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVR 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1003 KK------ALQEAHQ----QALGDLQAEEDRvsaltKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQES 1072
Cdd:pfam07111 272 VQslthmlALQEEELtrkiQPSDSLEPEFPK-----KCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQ 346
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1622840248 1073 VADATQDKQQLEEKLKKKDSELSQLSLRVEDEQLLGAQLQK 1113
Cdd:pfam07111 347 VTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQE 387
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1708-1932 |
2.28e-04 |
|
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: 46.16 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1708 LAEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKaitdaammaeelKKEQDTSAHLE 1787
Cdd:NF033838 101 LYELNVLKEKSEAELTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKD------------QKEEDRRNYPT 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1788 RMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKlEAKVRELEAELDAEQKKhAEALKGVRKHERRVKELAYQAEEDRKN 1867
Cdd:NF033838 169 NTYKTLELEIAESDVEVKKAELELVKEEAKEPRD-EEKIKQAKAKVESKKAE-ATRLEKIKTDREKAEEEAKRRADAKLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1868 LARMQDLVDKLQSKVKSYKRQF---EEAEQQANTNLAKYR--------------KAQHELDDAEERADMAETQANKLRAR 1930
Cdd:NF033838 247 EAVEKNVATSEQDKPKRRAKRGvlgEPATPDKKENDAKSSdssvgeetlpspslKPEKKVAEAEKKVEEAKKKAKDQKEE 326
|
..
gi 1622840248 1931 TR 1932
Cdd:NF033838 327 DR 328
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
984-1248 |
2.33e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 984 NLTEEMAALDESVARLTKEKKALQEAHQQALGDLQA--EEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRK 1061
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1062 LEGDLKLTQESVADATQDK--QQLEEKLKKKDSELSQLSLRVEDEQLLGAQLQKKIKELQARAEEleeeleaeraararv 1139
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQ--------------- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1140 EKQRAEAARELeelserleeaggasagQREGSRKREAElgrLRRELEEAalrhEATVAALRRKQAEgAAELGEQVDSLQR 1219
Cdd:COG3206 310 EAQRILASLEA----------------ELEALQAREAS---LQAQLAQL----EARLAELPELEAE-LRRLEREVEVARE 365
|
250 260
....*....|....*....|....*....
gi 1622840248 1220 VRQKLEKEKSELRMEVDDLAANVETLTRA 1248
Cdd:COG3206 366 LYESLLQRLEEARLAEALTVGNVRVIDPA 394
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
946-1097 |
2.61e-04 |
|
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: 45.79 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 946 RRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKE----KKALQEAhQQALGDLQAEE 1021
Cdd:pfam05667 329 LQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQykvkKKTLDLL-PDAEENIAKLQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1022 DRVSALTKAKLRLEQQ-----VEDLEcSLEQEKKLRMDTE-RAKRKLEgDLKLTQESVadatqdkQQLEEKLKKKDSELS 1095
Cdd:pfam05667 408 ALVDASAQRLVELAGQwekhrVPLIE-EYRALKEAKSNKEdESQRKLE-EIKELREKI-------KEVAEEAKQKEELYK 478
|
..
gi 1622840248 1096 QL 1097
Cdd:pfam05667 479 QL 480
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
858-1548 |
2.64e-04 |
|
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: 46.19 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 858 ALRAELRGL-RGALA------AAEAKRQELEETHVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKS----KVQLEGKV 926
Cdd:TIGR00606 374 ATRLELDGFeRGPFSerqiknFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTielkKEILEKKQ 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 927 KELSERLEDEEEVNADLAaRRRKLEDECTELKKDIDDLE--LTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKK 1004
Cdd:TIGR00606 454 EELKFVIKELQQLEGSSD-RILELDQELRKAERELSKAEknSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTT 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1005 ALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRmDTERAKRKLEGDLKLTQESVADATQDKQQLE 1084
Cdd:TIGR00606 533 TRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLH-SKSKEINQTRDRLAKLNKELASLEQNKNHIN 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1085 EKLKKKDSELSQLSLRV------EDEQLLGAQLQKKIKElqaraeeleeeleaeraararVEKQRAEAARELEELSERLE 1158
Cdd:TIGR00606 612 NELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEK---------------------SSKQRAMLAGATAVYSQFIT 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1159 EAGGASAG-----QREGSRKREAE--LGRLRRELEEAALRHEATVAALRRKQAEGAAELGeQVDSLQRVRQKLEKEKSEL 1231
Cdd:TIGR00606 671 QLTDENQSccpvcQRVFQTEAELQefISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLG-LAPGRQSIIDLKEKEIPEL 749
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1232 RMEVDDLAANVETLTRAKASAEKLCRTYEDQLSEAKI------KVEELQRQLADA----STQRGRLQTESGELSH----- 1296
Cdd:TIGR00606 750 RNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVcltdvtIMERFQMELKDVerkiAQQAAKLQGSDLDRTVqqvnq 829
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1297 -LLEEKECLISQLSRGKALAAQSLEELRRQLEEESKAKSALAHAVQALRH--DCDLLREQHEEEAEAQAELQRLLSKANA 1373
Cdd:TIGR00606 830 eKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNlqRRQQFEEQLVELSTEVQSLIREIKDAKE 909
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1374 EVAQWRSKYEADaIQRTEEL----EEAKKKLALRLQEAEEGVEAANAKCSSLEKA--------KLRLQTESEDVTLELER 1441
Cdd:TIGR00606 910 QDSPLETFLEKD-QQEKEELisskETSNKKAQDKVNDIKEKVKNIHGYMKDIENKiqdgkddyLKQKETELNTVNAQLEE 988
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1442 ATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRLQHSHEEALEALETLKRENKNLQEEISDLTD 1521
Cdd:TIGR00606 989 CEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKR 1068
|
730 740
....*....|....*....|....*..
gi 1622840248 1522 QLSLSGKSIQELEKAKKALEGEKSEIQ 1548
Cdd:TIGR00606 1069 NHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1000-1855 |
3.38e-04 |
|
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: 45.81 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1000 TKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSL--------EQEKKLRMDTERAKRKLEGDLKLTQE 1071
Cdd:TIGR00606 247 LDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMekvfqgtdEQLNDLYHNHQRTVREKERELVDCQR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1072 SVADATQDKQQLEEKLKKKDSELSQLSLRVE--DEQLLGAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARE 1149
Cdd:TIGR00606 327 ELEKLNKERRLLNQEKTELLVEQGRLQLQADrhQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1150 LEELSERLEEAGGASAGQREGSRKREAELGRLRRELEEAALRHEATVAALRRKQAEGaAELGEQVDSLQRVRQKLEKEKS 1229
Cdd:TIGR00606 407 AKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL-QQLEGSSDRILELDQELRKAER 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1230 ELRMEvdDLAANVETLTRAKASaeklcrtyedqLSEAKIKVEELQRQLADASTQRGRLQTESGELSHLLEEKECLISQLS 1309
Cdd:TIGR00606 486 ELSKA--EKNSLTETLKKEVKS-----------LQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIR 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1310 RGKALAAQ---SLEELRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSKANAEVAQWRSK----- 1381
Cdd:TIGR00606 553 KIKSRHSDeltSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvc 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1382 ----YEADAIQRTEELEEAKKKLALRLQEAE------EGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAaldK 1451
Cdd:TIGR00606 633 gsqdEESDLERLKEEIEKSSKQRAMLAGATAvysqfiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAP---D 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1452 KQRHLERALEERRRQEEEMQRELEAAQREarglgtelfrLQHSHEEALEALETLKRENKNLQEEISDLTDQLSLSGKSIQ 1531
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEMLGLAPGRQSI----------IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMP 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1532 ELEKAKKALE--GEKSEIQAALEEAEGALELEETKTLRIQLELSQvkAEVDRKLAEKDEEcanLRRNHQRAVESLQASLD 1609
Cdd:TIGR00606 780 EEESAKVCLTdvTIMERFQMELKDVERKIAQQAAKLQGSDLDRTV--QQVNQEKQEKQHE---LDTVVSKIELNRKLIQD 854
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1610 aetraRNEALRLKKKMEGDLNDLELQLGHATRQATEaqaatrlMQAQLKEEQAgrdEEQRLAAELREQAQALERRAALLA 1689
Cdd:TIGR00606 855 -----QQEQIQHLKSKTNELKSEKLQIGTNLQRRQQ-------FEEQLVELST---EVQSLIREIKDAKEQDSPLETFLE 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1690 AELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLN--------QKKKLEADLAQLSGEVEEAAQERREAEEK 1761
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENkiqdgkddYLKQKETELNTVNAQLEECEKHQEKINED 999
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1762 AKKAITDAAMMAEELKKEQDtsaHLERMKKtlEQTVRELQarlEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHA 1841
Cdd:TIGR00606 1000 MRLMRQDIDTQKIQERWLQD---NLTLRKR--ENELKEVE---EELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHV 1071
|
890
....*....|....
gi 1622840248 1842 EALKGVRKHERRVK 1855
Cdd:TIGR00606 1072 LALGRQKGYEKEIK 1085
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1421-1918 |
3.66e-04 |
|
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: 45.73 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1421 LEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAA------QREARGLGTELFRLQH- 1493
Cdd:TIGR00618 196 AELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQeeqlkkQQLLKQLRARIEELRAq 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1494 --SHEEALEALEtLKRENKNLQEEISDLTDQLSLSGKSIQELEKAKKALEGEKSEIQAALEEAEGALELEET-KTLRIQL 1570
Cdd:TIGR00618 276 eaVLEETQERIN-RARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLlQTLHSQE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1571 ELSQVKAEVDRK-LAEKDEECANLRRNHQRAvESLQASLDAETRARNEALRLKKKMEGDL------NDLELQLGHATRQ- 1642
Cdd:TIGR00618 355 IHIRDAHEVATSiREISCQQHTLTQHIHTLQ-QQKTTLTQKLQSLCKELDILQREQATIDtrtsafRDLQGQLAHAKKQq 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1643 -------ATEAQAATRLMQAQLKEEQAGRDEEQRLAAELREQAQALERRAALLAAELEELRAALEQGERSRRLAEQELLE 1715
Cdd:TIGR00618 434 elqqryaELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHP 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1716 ATERLNLLHSQNT-----GLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMA----------------- 1773
Cdd:TIGR00618 514 NPARQDIDNPGPLtrrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTqcdnrskedipnlqnit 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1774 EELKKEQDTSAHLERMKKTLEQT-VRELQARLEEAEQAALRGGKKQVQKLE--AKVRELEAELDAEQKKHAEALKGVRKH 1850
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHAlLRKLQPEQDLQDVRLHLQQCSQELALKltALHALQLTLTQERVREHALSIRVLPKE 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1851 ERRVKELAYQAEE--------DRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQANTNLAKYRK----AQHELDDAEERAD 1918
Cdd:TIGR00618 674 LLASRQLALQKMQsekeqltyWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAredaLNQSLKELMHQAR 753
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1570-1865 |
3.85e-04 |
|
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: 45.39 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1570 LELSQVKAEVDRKLAE--------KDEECANLRRNHQRAVESLQASLDAETRaRNEALRLKKKMEGDLNDLELQLGHATR 1641
Cdd:NF033838 135 LEPGKKVAEATKKVEEaekkakdqKEEDRRNYPTNTYKTLELEIAESDVEVK-KAELELVKEEAKEPRDEEKIKQAKAKV 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1642 QATEAQAaTRLMQAQLKEEQAGRDEEQRLAAELREQAQALERRAALLAAELeelraaleqgeRSRRLAEQELLEATERLN 1721
Cdd:NF033838 214 ESKKAEA-TRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKR-----------RAKRGVLGEPATPDKKEN 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1722 LLHSQNTGLlnQKKKLEADLAQLSGEVEEAAQERREAEEKAKKaitdaammaeelKKEQDTSAHLERMKKTLEQTVRELQ 1801
Cdd:NF033838 282 DAKSSDSSV--GEETLPSPSLKPEKKVAEAEKKVEEAKKKAKD------------QKEEDRRNYPTNTYKTLELEIAESD 347
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622840248 1802 ARLEEAEQAALRGGKKQVQKlEAKVRELEAELDAEqKKHAEALKGVRKHERRVKELAYQ--AEEDR 1865
Cdd:NF033838 348 VKVKEAELELVKEEAKEPRN-EEKIKQAKAKVESK-KAEATRLEKIKTDRKKAEEEAKRkaAEEDK 411
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1709-1869 |
3.98e-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: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1709 AEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQdtsAHLER 1788
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE---ARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1789 MKKTLEQ--TVRELQARLEEAEQAALRGGK---------KQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKEL 1857
Cdd:COG1579 78 YEEQLGNvrNNKEYEALQKEIESLKRRISDledeilelmERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170
....*....|..
gi 1622840248 1858 AYQAEEDRKNLA 1869
Cdd:COG1579 158 LEELEAEREELA 169
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
920-1107 |
4.03e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 45.23 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 920 VQLEGKVKELSERLEDEEEVNADLAAR-------RRKLEDECTELKKDIDDLELTLAKA----EKEKQATENKVKNLTEE 988
Cdd:pfam09726 398 VRLEQDIKKLKAELQASRQTEQELRSQissltslERSLKSELGQLRQENDLLQTKLHNAvsakQKDKQTVQQLEKRLKAE 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 989 MAALDESVARLTKEKKALQEahqqalgdlqaEEDrvsalTKAKLRLEQQVEDLECSlEQEKKLRMDTERAKRKLEGDLKL 1068
Cdd:pfam09726 478 QEARASAEKQLAEEKKRKKE-----------EEA-----TAARAVALAAASRGECT-ESLKQRKRELESEIKKLTHDIKL 540
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622840248 1069 TQESVADATQDKQQLEE-KLKKKDSE--LSQLSLRVEDEQLL 1107
Cdd:pfam09726 541 KEEQIRELEIKVQELRKyKESEKDTEvlMSALSAMQDKNQHL 582
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1733-1845 |
5.01e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.86 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1733 QKKKLEADLAQLSGEV--EEAAQERREAEEKAK----KAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEE 1806
Cdd:COG2268 224 EEAELEQEREIETARIaeAEAELAKKKAEERREaetaRAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREE 303
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1622840248 1807 AEQAALRGGKKQVQKLEAKVRElEAELDAEQ---KKHAEALK 1845
Cdd:COG2268 304 AELEADVRKPAEAEKQAAEAEA-EAEAEAIRakgLAEAEGKR 344
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1388-1624 |
5.19e-04 |
|
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: 45.01 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1388 QRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQE 1467
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTR 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1468 EEMQRELEAAQREARGLGTELFRLQHSHEEALEALETLKRENKNLQEEISDLTDQLSLSGKSIQELEKAKKALEGEKSEI 1547
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1548 QAALEEAEGALELEETKT--LRIQLELSQVK----------AEVDRKLAEKDEECANLrRNHQRAVESLQASLDAE---T 1612
Cdd:TIGR04523 544 EDELNKDDFELKKENLEKeiDEKNKEIEELKqtqkslkkkqEEKQELIDQKEKEKKDL-IKEIEEKEKKISSLEKElekA 622
|
250
....*....|..
gi 1622840248 1613 RARNEALRLKKK 1624
Cdd:TIGR04523 623 KKENEKLSSIIK 634
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1708-1930 |
5.67e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1708 LAEQELLEATERLNLLHSQNT-GLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKaitdaammaeeLKKEQDTSAhl 1786
Cdd:PRK11281 48 LNKQKLLEAEDKLVQQDLEQTlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEA-----------LKDDNDEET-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1787 ermKKTLE-QTVRELQARLEEAE------QAALRGGKKQVQKLEAKVRELEAELDAEQKKHAE---ALKGVR------KH 1850
Cdd:PRK11281 115 ---RETLStLSLRQLESRLAQTLdqlqnaQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQirnLLKGGKvggkalRP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1851 ERRVK---ELAY---QAEEDRKNLA---RMQDLvDKLQSKVKSYKRQFEEAEQQANTNL--AKYRK-AQHELDDAEERAD 1918
Cdd:PRK11281 192 SQRVLlqaEQALlnaQNDLQRKSLEgntQLQDL-LQKQRDYLTARIQRLEHQLQLLQEAinSKRLTlSEKTVQEAQSQDE 270
|
250
....*....|..
gi 1622840248 1919 MAETQANKLRAR 1930
Cdd:PRK11281 271 AARIQANPLVAQ 282
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
941-1090 |
6.09e-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: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 941 ADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEmaaLDESVARLTKEKKALQEAH-QQALGDLQA 1019
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE---IEEVEARIKKYEEQLGNVRnNKEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622840248 1020 EEDrvsALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADATQDKQQLEEKLKKK 1090
Cdd:COG1579 97 EIE---SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
936-1112 |
6.71e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 936 EEEVNADL--AARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQA 1013
Cdd:PRK11281 38 EADVQAQLdaLNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1014 LGDLQAEEdrvsaltkaklrLEQQVEDLECSLEQEKK-----------LRMDTERAkrklegdlkltQESVADATQDKQQ 1082
Cdd:PRK11281 118 LSTLSLRQ------------LESRLAQTLDQLQNAQNdlaeynsqlvsLQTQPERA-----------QAALYANSQRLQQ 174
|
170 180 190
....*....|....*....|....*....|
gi 1622840248 1083 LEEKLkkKDSELSQLSLRVEDEQLLGAQLQ 1112
Cdd:PRK11281 175 IRNLL--KGGKVGGKALRPSQRVLLQAEQA 202
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
934-1085 |
7.70e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 934 EDEEEVN---ADLAARRRKLEDEctelkkdiddleltLAKAEKEKQATENKVKNLTEEMAALDEsvaRLTKEKKALQEAH 1010
Cdd:PRK00409 513 EDKEKLNeliASLEELERELEQK--------------AEEAEALLKEAEKLKEELEEKKEKLQE---EEDKLLEEAEKEA 575
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622840248 1011 QQALGDLQAEEDRVsaltkakLRLEQQVEDLECSLEQEKKLrmdtERAKRKLEGDLKLTQESVADATQDKQQLEE 1085
Cdd:PRK00409 576 QQAIKEAKKEADEI-------IKELRQLQKGGYASVKAHEL----IEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
921-1240 |
8.43e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 921 QLEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLT 1000
Cdd:COG4372 49 QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1001 KEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADATQDK 1080
Cdd:COG4372 129 QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1081 QQLEEKLKKKDSELSQLSLRVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEA 1160
Cdd:COG4372 209 IESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1161 GGASAGQREGSRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAA 1240
Cdd:COG4372 289 EEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1748-1940 |
8.85e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 44.54 E-value: 8.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1748 VEEAAQERREAEE-KAKKAITDAAMMAEELKKEQDTSAHL-ERMKKTLEqTVRELQARLEEAEQAALRGGKKQVQK---- 1821
Cdd:PLN03188 1041 TDESPEKKLEQERlRWTEAESKWISLAEELRTELDASRALaEKQKHELD-TEKRCAEELKEAMQMAMEGHARMLEQyadl 1119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1822 ------LEAKVRELEAELDAEQKKHAEAlkGVRKHERR--------VKELAYQAEEDRKNLarmQDLVDKLQSKVksykR 1887
Cdd:PLN03188 1120 eekhiqLLARHRRIQEGIDDVKKAAARA--GVRGAESKfinalaaeISALKVEREKERRYL---RDENKSLQAQL----R 1190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622840248 1888 QFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRaRTRDALGPKHK 1940
Cdd:PLN03188 1191 DTAEAVQAAGELLVRLKEAEEALTVAQKRAMDAEQEAAEAY-KQIDKLKRKHE 1242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1799-1936 |
8.98e-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: 42.99 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1799 ELQARLEEAEQAaLRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDL--VD 1876
Cdd:COG1579 14 ELDSELDRLEHR-LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeYE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1877 KLQSKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDALG 1936
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
960-1073 |
9.19e-04 |
|
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: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 960 DIDDLELTLAKAEKEKQATENkvknltEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVE 1039
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKK------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100 110
....*....|....*....|....*....|....
gi 1622840248 1040 DLEcslEQEKKLrmdtERAKRKLEGDLKLTQESV 1073
Cdd:COG0542 486 KIP---ELEKEL----AELEEELAELAPLLREEV 512
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
869-1119 |
9.63e-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: 43.96 E-value: 9.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 869 ALAAAEAKRQELEETHvsvtQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNADLAARRR 948
Cdd:pfam05557 32 LEKKASALKRQLDRES----DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 949 KLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQ---------------- 1012
Cdd:pfam05557 108 CLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRikelefeiqsqeqdse 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1013 ALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKlTQESVADATQDKQQLEEKLK--KK 1090
Cdd:pfam05557 188 IVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEK-YREEAATLELEKEKLEQELQswVK 266
|
250 260
....*....|....*....|....*....
gi 1622840248 1091 DSELSQLSLRVEDEqllgaqLQKKIKELQ 1119
Cdd:pfam05557 267 LAQDTGLNLRSPED------LSRRIEQLQ 289
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1629-1928 |
1.15e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1629 LNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAaELREqAQALERRAALLAAELEELRAALEQGERSRRL 1708
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA-EYSW-DEIDVASAEREIAELEAELERLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1709 AEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAammAEELKKEQDTSAHLER 1788
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL---LEERFAAALGDAVERE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1789 MKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQK--KHAEALKGVRKHERRVKELAYQAEEDRK 1866
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEylALLDRLEEDGLPEYEERFKELLNENSIE 846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1867 NLArmqDLVDKLQSKVKSYKRQFE-------------------EAEQQANTNLAKYRKAQHELDDAEERADMAETQANKL 1927
Cdd:COG4913 847 FVA---DLLSKLRRAIREIKERIDplndslkripfgpgrylrlEARPRPDPEVREFRQELRAVTSGASLFDEELSEARFA 923
|
.
gi 1622840248 1928 R 1928
Cdd:COG4913 924 A 924
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
922-1119 |
1.16e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 922 LEGKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDI----DDLELTLAKAEKEKQATENKVKNLTEEMAALDESVA 997
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIkaeiEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 998 RLTKEKKALQEAHQ--QALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKlRMDterakrklegdlkltqeSVAD 1075
Cdd:PHA02562 273 QFQKVIKMYEKGGVcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEE-IMD-----------------EFNE 334
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622840248 1076 ATQDKQQLEEKLKKKDSELSQLSLRVEDeqllgaqLQKKIKELQ 1119
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLITLVDKAKK-------VKAAIEELQ 371
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
854-1088 |
1.51e-03 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 43.51 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 854 EELAALRAELRGLRGALAAAEA--------KRQELEETHVSVTQEKNDLALQLQAE-QDN------LADAEERchlLIKS 918
Cdd:pfam15070 53 QELETSLAELKNQAAVPPAEEEqppagpseEEQRLQEEAEQLQKELEALAGQLQAQvQDNeqlsrlNQEQEQR---LLEL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 919 KVQLEGKVKELSERLEDEEEVNADLA------ARRRKLEDECTEL-----KKDIDDLELTLA-KAEKE-KQATENKVKNL 985
Cdd:pfam15070 130 ERAAERWGEQAEDRKQILEDMQSDRAtisralSQNRELKEQLAELqngfvKLTNENMELTSAlQSEQHvKKELAKKLGQL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 986 TEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVedlecsLEQEKKL-RMDTERAKRKLEG 1064
Cdd:pfam15070 210 QEELGELKETLELKSQEAQSLQEQRDQYLAHLQQYVAAYQQLASEKEELHKQY------LLQTQLMdRLQHEEVQGKVAA 283
|
250 260
....*....|....*....|....*....
gi 1622840248 1065 D-----LKLTQESVADATQDKQQLEEKLK 1088
Cdd:pfam15070 284 EmarqeLQETQERLEALTQQNQQLQAQLS 312
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1664-1930 |
1.55e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1664 RDEEQRLAAELREQAQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLhsqNTGLLNQKK-------- 1735
Cdd:PRK04863 281 RRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLV---QTALRQQEKieryqadl 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1736 -KLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRelqaRLEEAEQA---- 1810
Cdd:PRK04863 358 eELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQ----ALERAKQLcglp 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1811 --ALRGGKKQVQKLEAKVREL-EAELDAEQK---------KHAEALKGVRK---------HERRVKELAYQAEEDRKNLA 1869
Cdd:PRK04863 434 dlTADNAEDWLEEFQAKEQEAtEELLSLEQKlsvaqaahsQFEQAYQLVRKiagevsrseAWDVARELLRRLREQRHLAE 513
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622840248 1870 RMQDLVDKLQ------SKVKSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRAR 1930
Cdd:PRK04863 514 QLQQLRMRLSeleqrlRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARER 580
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1735-1909 |
1.58e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 41.48 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1735 KKLEADLAQLSGEVEEAAQERREAEEKAKKAITdAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRG 1814
Cdd:pfam01442 7 DELSTYAEELQEQLGPVAQELVDRLEKETEALR-ERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1815 GKKQVQKLEAKVRELEAELDAEQKKHAEALKGVrkherrvkeLAYQAEEDRKNLA-RMQDLVDKLQSKVKSYKRQFEEAE 1893
Cdd:pfam01442 86 LNADAEELQEKLAPYGEELRERLEQNVDALRAR---------LAPYAEELRQKLAeRLEELKESLAPYAEEVQAQLSQRL 156
|
170
....*....|....*.
gi 1622840248 1894 QQANTNLAKYRKAQHE 1909
Cdd:pfam01442 157 QELREKLEPQAEDLRE 172
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1598-1914 |
1.78e-03 |
|
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: 43.46 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1598 QRAVESLQASLDAETRARNEAL-----RLKKKMEGDLNDLELQLGHATRQATEAQ--AATRLMQAQLKEEQAGRDEEQRL 1670
Cdd:NF033838 68 EKILSEIQKSLDKRKHTQNVALnkklsDIKTEYLYELNVLKEKSEAELTSKTKKEldAAFEQFKKDTLEPGKKVAEATKK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1671 AAELREQAQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNllHSQNTGLLNQ-KKKLEADLAQLSgEVE 1749
Cdd:NF033838 148 VEEAEKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKEEAK--EPRDEEKIKQaKAKVESKKAEAT-RLE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1750 EAAQERREAEEKAKKaiTDAAMMAEELKKEQDTSAHlERMKKTLEQTVRELQARLEEAEQAAlRGGKKQVQKLEAKVREL 1829
Cdd:NF033838 225 KIKTDREKAEEEAKR--RADAKLKEAVEKNVATSEQ-DKPKRRAKRGVLGEPATPDKKENDA-KSSDSSVGEETLPSPSL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1830 EAEldaeqKKHAEALKGVRKHERRVKElayQAEEDRKNLA--RMQDL---VDKLQSKVKSYKRQF--EEAEQQANTNLAK 1902
Cdd:NF033838 301 KPE-----KKVAEAEKKVEEAKKKAKD---QKEEDRRNYPtnTYKTLeleIAESDVKVKEAELELvkEEAKEPRNEEKIK 372
|
330
....*....|..
gi 1622840248 1903 YRKAQHELDDAE 1914
Cdd:NF033838 373 QAKAKVESKKAE 384
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1036-1626 |
1.80e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1036 QQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADATQDKQQLEEKlkkkDSELSQLSLRVEDEQLLGAQLQKKI 1115
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL----KEEIEELEKELESLEGSKRKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1116 KELQARAEELEEELEAERAARARVEKQRAEAareleelserleeaggasagqregsrKREAELGRLRRELEEAALRHEAT 1195
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKELKEKA--------------------------EEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1196 VAALRRkQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKA--------SAEKLCRTYED---QLS 1264
Cdd:PRK03918 316 LSRLEE-EINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAkkeelerlKKRLTGLTPEKlekELE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1265 EAKIKVEELQRQLADASTQRGRLQTESGELSHLLEE-----KEC-----LISQLSRGKALAAQSleelrrqlEEESKAKS 1334
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakGKCpvcgrELTEEHRKELLEEYT--------AELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1335 ALAHAVQALRHdcdlLREQHEEEAEAQAELQRLLskanaevaqwRSKYEADAIqrtEELEEAKKKLAL-RLQEAEEGVEA 1413
Cdd:PRK03918 467 ELKEIEEKERK----LRKELRELEKVLKKESELI----------KLKELAEQL---KELEEKLKKYNLeELEKKAEEYEK 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1414 ANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRLQH 1493
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKD 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1494 SHEEaleaLETLKRENKNLQEEISDLTDQLSLSGKSIQELEKAKKALEGEKSEIQAALEEAEGALELEETKTLRIQLELS 1573
Cdd:PRK03918 610 AEKE----LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEEL 685
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1622840248 1574 QVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALRLKKKME 1626
Cdd:PRK03918 686 EKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
916-1078 |
1.82e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 916 IKSKVQLEGKVKELSERLEDEEEVNAdlaaRRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDes 995
Cdd:PRK12704 54 IKKEALLEAKEEIHKLRNEFEKELRE----RRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 996 varltKEKKALQEAHQQALGDLQaeedRVSALTKAKLRlEQQVEDLECSLEQEKKLRMDTERAKRKLEGDlKLTQESVAD 1075
Cdd:PRK12704 128 -----KKEEELEELIEEQLQELE----RISGLTAEEAK-EILLEKVEEEARHEAAVLIKEIEEEAKEEAD-KKAKEILAQ 196
|
...
gi 1622840248 1076 ATQ 1078
Cdd:PRK12704 197 AIQ 199
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
929-1255 |
1.97e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 929 LSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQE 1008
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1009 AHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSL-EQEKKLRMDTERAKRKLEGDLKLTQESVADATQDKQQLEEKL 1087
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIaEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1088 KKKDSELSQLSLRVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQ 1167
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1168 REGSRKREAELGRLRRELEEAALRHEATVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTR 1247
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
....*...
gi 1622840248 1248 AKASAEKL 1255
Cdd:COG4372 349 GLLDNDVL 356
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1140-1548 |
2.10e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1140 EKQRAEAARELEELSERLEEAGGASAGQREGSRKREAELGRLRRELEEAALRHEATVAALRRKQAEGA-AELGEQVDSLQ 1218
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERlEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1219 RVRQKLEKEKSELRMEVDDL-AANVETLTRAKASAEKLcrtyEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSHL 1297
Cdd:COG4717 167 ELEAELAELQEELEELLEQLsLATEEELQDLAEELEEL----QQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1298 LEEKECLISQLSRGKALAAQSLEELRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEEAEAQAELQRLLSK-ANAEVA 1376
Cdd:COG4717 243 ERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEElEEEELE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1377 QWRSKYEADAIQRTEELEEAKKKLAlRLQEAEEGVEAANakcsslEKAKLRLQTESEDVTLELERATSAAAALDKKQRHL 1456
Cdd:COG4717 323 ELLAALGLPPDLSPEELLELLDRIE-ELQELLREAEELE------EELQLEELEQEIAALLAEAGVEDEEELRAALEQAE 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1457 ERALEERRRQEEEMQRELEAAQREARGLGTELFRLQHSHEEALEALETLKRENKNLQEEISDLTDQLSLSGKSiQELEKA 1536
Cdd:COG4717 396 EYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED-GELAEL 474
|
410
....*....|..
gi 1622840248 1537 KKALEGEKSEIQ 1548
Cdd:COG4717 475 LQELEELKAELR 486
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1733-1934 |
2.57e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.63 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1733 QKKKLEADLAQLSGEVEEAAQERREAE--EKAKKAitdaammAEELKKEQD--TSAHLERMK----KTLEQTVRELQARL 1804
Cdd:PRK05035 442 EQEKKKAEEAKARFEARQARLEREKAAreARHKKA-------AEARAAKDKdaVAAALARVKakkaAATQPIVIKAGARP 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1805 EEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGV--RKHERRVKELAYQAEEDRKNLARMQDLVDklqSKV 1882
Cdd:PRK05035 515 DNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAkaKKAAQQAANAEAEEEVDPKKAAVAAAIAR---AKA 591
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622840248 1883 KSYKRQFEEAEQQANTNLAKYRKAQHELDDAEERADMAETQANKLRARTRDA 1934
Cdd:PRK05035 592 KKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDP 643
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1790-1925 |
2.91e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.35 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1790 KKTLEQTVRELQARLEEAEQ------AALRGGKKQVQKLEAKVRELEAE----LDAEQKKHA-EALKGVRKHERRVKELA 1858
Cdd:COG1842 25 EKMLDQAIRDMEEDLVEARQalaqviANQKRLERQLEELEAEAEKWEEKarlaLEKGREDLArEALERKAELEAQAEALE 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622840248 1859 YQAEEDRKNLARMQDLVDKLQSKVKSYKRQFE---------EAEQQANTNLAKYR--KAQHELDDAEERADMAETQAN 1925
Cdd:COG1842 105 AQLAQLEEQVEKLKEALRQLESKLEELKAKKDtlkarakaaKAQEKVNEALSGIDsdDATSALERMEEKIEEMEARAE 182
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1779-1861 |
3.09e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1779 EQDTSAHLERMKKTLEQTVRELQARLEEAEQAA--LRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKherRVKE 1856
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALAEAQQqeLVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQ---KRKE 220
|
....*
gi 1622840248 1857 LAYQA 1861
Cdd:PRK11448 221 ITDQA 225
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1737-1830 |
3.19e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.79 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1737 LEADLAQLSGEVE-EAAQERREAEEKAKKAITDAAMMAEELKKEQDTS--AHLERMKKTLEQTVRELQARLEEA------ 1807
Cdd:cd16269 187 LQADQALTEKEKEiEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSyeEHLRQLKEKMEEERENLLKEQERAlesklk 266
|
90 100
....*....|....*....|....*
gi 1622840248 1808 EQAAL--RGGKKQVQKLEAKVRELE 1830
Cdd:cd16269 267 EQEALleEGFKEQAELLQEEIRSLK 291
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1728-1936 |
3.79e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 41.24 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1728 TGLLNQKKKLEADLAQLSGEVEEAAQERREAEEK---AKKAITDAAMMAEEL-KKEQDTSAHLERMKKTLEQTVRELQAR 1803
Cdd:pfam06008 8 TGALPAPYKINYNLENLTKQLQEYLSPENAHKIQieiLEKELSSLAQETEELqKKATQTLAKAQQVNAESERTLGHAKEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1804 LEEAEQAAlrggkKQVQKLEAKVRELEAELDAE-----QKKHAEALKGVRkhERRVKELAYQAEEDRKNLARMQDLVDKL 1878
Cdd:pfam06008 88 AEAIKNLI-----DNIKEINEKVATLGENDFALpssdlSRMLAEAQRMLG--EIRSRDFGTQLQNAEAELKAAQDLLSRI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622840248 1879 QSKVKSYKRQFEEAEQQANTNLAKYrkaQHELDDAEERADMAET---QANKLRARTRDALG 1936
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEY---EAKLSDLRELLREAAAktrDANRLNLANQANLR 218
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1221-1454 |
4.10e-03 |
|
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: 41.67 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1221 RQKLEKEKSELRMEVDDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSHLLEE 1300
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1301 KECLISQLSRgkaLAAQSLEELRRQLEEESKAKSALAHAVQALRHdcdllreqheeeaeaqaelqrllskanaeVAQWRS 1380
Cdd:COG4942 102 QKEELAELLR---ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKY-----------------------------LAPARR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622840248 1381 KYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQR 1454
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
969-1208 |
4.13e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.24 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 969 AKAEKEKQATENKVKnlteemaaLDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQE 1048
Cdd:PRK05035 440 AIEQEKKKAEEAKAR--------FEARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAG 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1049 KKLR---MDTERAKRKLEGDLKLTQESVADATQDKQQLEE------KLKKKDSELSQLSLRVEDEQLLgAQLQKKIKELQ 1119
Cdd:PRK05035 512 ARPDnsaVIAAREARKAQARARQAEKQAAAAADPKKAAVAaaiaraKAKKAAQQAANAEAEEEVDPKK-AAVAAAIARAK 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1120 ARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQR-EGSRKR--EAELGRLR-RELEEAALRHEAT 1195
Cdd:PRK05035 591 AKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEpVDPRKAavAAAIARAKaRKAAQQQANAEPE 670
|
250
....*....|...
gi 1622840248 1196 VAALRRKQAEGAA 1208
Cdd:PRK05035 671 EAEDPKKAAVAAA 683
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
853-1001 |
4.55e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 853 EEELAALRAELRGLRGALAAAEAKRQELEEthvSVTQEKNDLAlQLQAEQDNLADAEERchlLIKSKVQLEGKVKELSER 932
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQD---SVANLRASLS-AAEAERSRLQALLAE---LAGAGAAAEGRAGELAQE 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 933 LEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEM-AALDESVARLTK 1001
Cdd:PRK09039 125 LDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLnVALAQRVQELNR 194
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
791-1103 |
4.61e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.20 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 791 VLTLLQARSRGrLMRLEyqRLLGGRDALfTIQWNIRAFNAVKNWSWMKLFFKMKplLRSAQAEEELAALRAELrGLRGAL 870
Cdd:PLN02939 144 ILLLNQARLQA-LEDLE--KILTEKEAL-QGKINILEMRLSETDARIKLAAQEK--IHVEILEEQLEKLRNEL-LIRGAT 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 871 AAAEAKRQELEethVSVTQEKN----DLALQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLEDEEEVNADLAAR 946
Cdd:PLN02939 217 EGLCVHSLSKE---LDVLKEENmllkDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 947 R-----RKLE--------------------DECTELKKDIDDLELTLAKAEKEKQATEnKVKNLTEEMAALDESVARLTK 1001
Cdd:PLN02939 294 QydcwwEKVEnlqdlldratnqvekaalvlDQNQDLRDKVDKLEASLKEANVSKFSSY-KVELLQQKLKLLEERLQASDH 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1002 EKKALQEAHQQALGDLQaeeDRVSALTK--AKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLegdlkltqesvadATQD 1079
Cdd:PLN02939 373 EIHSYIQLYQESIKEFQ---DTLSKLKEesKKRSLEHPADDMPSEFWSRILLLIDGWLLEKKI-------------SNND 436
|
330 340
....*....|....*....|....
gi 1622840248 1080 KQQLEEKLKKKDSELSQLSLRVED 1103
Cdd:PLN02939 437 AKLLREMVWKRDGRIREAYLSCKG 460
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1384-1620 |
4.87e-03 |
|
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: 41.29 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1384 ADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEer 1463
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1464 rRQEEEMQRELEAAQREARGLGTELFRLQHSHEEALEALETLKRENKNLQEEISDLTDQLSLSGKSIQELEKAKKALEGE 1543
Cdd:COG4942 101 -AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622840248 1544 KSEIQAALEEAEGALELEEtktlRIQLELSQVKAEVDRKLAEKDEECANLRRNHQRAVESLQASLDAETRARNEALR 1620
Cdd:COG4942 180 LAELEEERAALEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1655-1888 |
4.94e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.33 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1655 AQLKEEQAGRDEEQRlAAELREQAQALERRAALLAAELEELRAALEQGERSRRLAEQElleaterlnllhsqntgllnQK 1734
Cdd:PRK09510 74 AKRAEEQRKKKEQQQ-AEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALK--------------------QK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1735 KKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEElkkEQDTSAHLERMKKTLEQTVRELQArleEAEQAALRG 1814
Cdd:PRK09510 133 QAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEA---EAAKKAAAEAKKKAEAEAAAKAAA---EAKKKAEAE 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622840248 1815 GKKQVQKLEAKvrelEAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQ 1888
Cdd:PRK09510 207 AKKKAAAEAKK----KAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLFGGLDSGKNAPKTG 276
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1732-1937 |
5.08e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 41.37 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1732 NQKKKLEADLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAA 1811
Cdd:TIGR02794 61 PAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1812 LRggkKQVQKLEAKvreleAELDAEQKKHAEALKGVRKHERRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEE 1891
Cdd:TIGR02794 141 ER---KAKEEAAKQ-----AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAK 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622840248 1892 AEQQANTNLAKYRKAQHELDDAEERADMA-ETQANKLRARTRDALGP 1937
Cdd:TIGR02794 213 AEAEAAAAAAAEAERKADEAELGDIFGLAsGSNAEKQGGARGAAAGS 259
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
846-1169 |
5.10e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 846 LLRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSVTQEKNDLALQLQAEQDNLADAEERchllikskvqlegk 925
Cdd:COG4372 37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE-------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 926 VKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKA 1005
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1006 LQEAHQQALGDLQAEEDRVSALTKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQESVADATQDKQQLEE 1085
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1086 KLKKKDSELSQLSLRVEDEQLLGAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASA 1165
Cdd:COG4372 263 LELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADL 342
|
....
gi 1622840248 1166 GQRE 1169
Cdd:COG4372 343 LQLL 346
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1475-1663 |
5.49e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1475 EAAQREARGLGTELFRLQHSHEEALEALETLKRENK--NLQEEISDLTDQLSLSGKSIQELEKAKKALEGEKSEIQAALE 1552
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1553 EAEGALELEETKTLRIQL--ELSQVKAEVDRKLA----------EKDEECANLRRNHQRAVESLQASLDAE---TRARNE 1617
Cdd:COG3206 251 SGPDALPELLQSPVIQQLraQLAELEAELAELSArytpnhpdviALRAQIAALRAQLQQEAQRILASLEAEleaLQAREA 330
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622840248 1618 ALR-----LKKKMEgDLNDLELQLGHATRQATEAQAA-----TRLMQAQLKEEQAG 1663
Cdd:COG3206 331 SLQaqlaqLEARLA-ELPELEAELRRLEREVEVARELyesllQRLEEARLAEALTV 385
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
847-1105 |
6.03e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.71 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 847 LRSAQAEEELAALRAELRGLRGALAAAEAKRQELEETHVSVTQEKNDLALQLQAEQDNLA---DAEERCHLLIKSKVQLE 923
Cdd:PRK10246 530 SRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNitlQPQDDIQPWLDAQEEHE 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 924 GKVKELSERLEDEEEVNADLAARRR---KLEDECTELKKDIDDLELTLAKAEKEK-------------QATENKVKNLTE 987
Cdd:PRK10246 610 RQLRLLSQRHELQGQIAAHNQQIIQyqqQIEQRQQQLLTALAGYALTLPQEDEEAswlatrqqeaqswQQRQNELTALQN 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 988 EMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALtKAKLRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLK 1067
Cdd:PRK10246 690 RIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSL-HSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQA 768
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1622840248 1068 -----LTQESVADATQDKQQLEEKLKKKDSELSQLSLRVEDEQ 1105
Cdd:PRK10246 769 flaalLDEETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQ 811
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
953-1032 |
6.09e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 40.87 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 953 ECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKALQEAHQQALGDLQAEEDRVSALTKAKL 1032
Cdd:COG4026 129 EYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKRL 208
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
860-1119 |
6.51e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.71 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 860 RAELRGLRGALAAAEAKRQELEETHVSVTQEKNDLALQLQAEQ----DNLADAEERCHLLIKSKVQLEGKVKELSERLEd 935
Cdd:PRK10246 379 REQLRQWQQQLTHAEQKLNALPAITLTLTADEVAAALAQHAEQrplrQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQT- 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 936 eeEVNADLAARRRKLEDE---------CTELKKDIDDLE----------------------------LTLAKAEKEKQAT 978
Cdd:PRK10246 458 --QRNAALNEMRQRYKEKtqqladvktICEQEARIKDLEaqraqlqagqpcplcgstshpaveayqaLEPGVNQSRLDAL 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 979 ENKVKNLTEEMAAL-------------DESVAR-LTKEKKALQEAHQQ---ALGDLQAEEDRVSALTKAKLRLEQQVEDL 1041
Cdd:PRK10246 536 EKEVKKLGEEGAALrgqldaltkqlqrDESEAQsLRQEEQALTQQWQAvcaSLNITLQPQDDIQPWLDAQEEHERQLRLL 615
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622840248 1042 ECSLEQEKKLRmDTERAKRKLEGDLKLTQESVADATqdkQQLEEKLKKKDSELSQLSLRvEDEQLLGAQLQKKIKELQ 1119
Cdd:PRK10246 616 SQRHELQGQIA-AHNQQIIQYQQQIEQRQQQLLTAL---AGYALTLPQEDEEASWLATR-QQEAQSWQQRQNELTALQ 688
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1094-1344 |
6.53e-03 |
|
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: 40.90 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1094 LSQLSLRVEDEQLLgAQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELeelserleeaggasagqregsRK 1173
Cdd:COG4942 16 AAQADAAAEAEAEL-EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI---------------------RA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1174 REAELGRLRRELEEAALRheatVAALRRKQAEGAAELGEQVDSLQRVRQKLEKEKSELRMEVDDLAANVETLTRAKASAE 1253
Cdd:COG4942 74 LEQELAALEAELAELEKE----IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1254 KLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSHLLEEKECLISQLSRGKALAAQSLEELRRQLEEESKAK 1333
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|.
gi 1622840248 1334 SALAHAVQALR 1344
Cdd:COG4942 230 ARLEAEAAAAA 240
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1175-1337 |
6.95e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1175 EAELGRLRRELEEAALRHEATVAALRRKQAEgAAELGEQVDSLQrvrQKLEKEKSELRMEV------------------- 1235
Cdd:COG3883 36 QAELDALQAELEELNEEYNELQAELEALQAE-IDKLQAEIAEAE---AEIEERREELGERAralyrsggsvsyldvllgs 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1236 ---DDLAANVETLTRAKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTESGELSHLLEEKECLISQLSRGK 1312
Cdd:COG3883 112 esfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191
|
170 180
....*....|....*....|....*
gi 1622840248 1313 ALAAQSLEELRRQLEEESKAKSALA 1337
Cdd:COG3883 192 AAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1395-1911 |
7.65e-03 |
|
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: 41.26 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1395 EAKKKLALRLQEAEEGVEaanakcsslekaklRLQTESE-DVTLELERATSAAAALDKKQRHleraleerrrqeeemqre 1473
Cdd:pfam15921 253 ESQNKIELLLQQHQDRIE--------------QLISEHEvEITGLTEKASSARSQANSIQSQ------------------ 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1474 LEAAQREARGLGTELFRLQHSHEEALEALETLKRENKNLQEE-ISDLTDQLSLSGKSIQELEKAKKALEGEKSEIQAALE 1552
Cdd:pfam15921 301 LEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDkIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1553 EAEGALELEETKtlrIQLELSQVKAEVDRKLAEKDEeCANLRR---NHQRAVESLQASLDA-ETRARNEALRLKKKMEGD 1628
Cdd:pfam15921 381 KLLADLHKREKE---LSLEKEQNKRLWDRDTGNSIT-IDHLRReldDRNMEVQRLEALLKAmKSECQGQMERQMAAIQGK 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1629 LNDLElQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELREQAQalerraallaaeleelraaleQGERSRRL 1708
Cdd:pfam15921 457 NESLE-KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ---------------------EKERAIEA 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1709 AEQELLEATERLNL-----LHSQNTG--LLNQKKKLEADLAQLSGEVEEAAQERREAEEkakkaitdaamMAEELKKEQD 1781
Cdd:pfam15921 515 TNAEITKLRSRVDLklqelQHLKNEGdhLRNVQTECEALKLQMAEKDKVIEILRQQIEN-----------MTQLVGQHGR 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1782 TSAHLERMKKTLEQTVRElqARLEEAEQAALRggkkqvQKLEAKVRELEA---ELDAEQKK----HAEALKGVRKHERRV 1854
Cdd:pfam15921 584 TAGAMQVEKAQLEKEIND--RRLELQEFKILK------DKKDAKIRELEArvsDLELEKVKlvnaGSERLRAVKDIKQER 655
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622840248 1855 KELAYQAEEDRKNLARMQDLVDKLQskvKSYKRQFEEAEQQANTNLAKYRKAQHELD 1911
Cdd:pfam15921 656 DQLLNEVKTSRNELNSLSEDYEVLK---RNFRNKSEEMETTTNKLKMQLKSAQSELE 709
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
957-1118 |
8.55e-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: 39.50 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 957 LKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDESVARLTKEKKAlQEAHQQALGDLQAeedRVSALTKAKLRLEQ 1036
Cdd:pfam13851 31 LKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN-YEKDKQSLKNLKA---RLKVLEKELKDLKW 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1037 QVEDLECSLEQekklrmdTERAKRKLEGDLKLTQESVADATQDK--------QQLEEKLKKKDSELSQLSLRVEDEQLLG 1108
Cdd:pfam13851 107 EHEVLEQRFEK-------VERERDELYDKFEAAIQDVQQKTGLKnlllekklQALGETLEKKEAQLNEVLAAANLDPDAL 179
|
170
....*....|
gi 1622840248 1109 AQLQKKIKEL 1118
Cdd:pfam13851 180 QAVTEKLEDV 189
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1598-1811 |
8.61e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1598 QRAVESLQASLdAETRARNEALRLkkkmEGDLNDLELQLGHATRQATEAQAATRLMQAQLKEEQAGRDEEQRLAAELREQ 1677
Cdd:COG3206 188 RKELEEAEAAL-EEFRQKNGLVDL----SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1678 AQalerraallaaeleelraalEQGERSRRL-AEQELLEATERLNLLHSQNTGLLNQKKKLEADLAQLSGEVEEAAQERR 1756
Cdd:COG3206 263 PV--------------------IQQLRAQLAeLEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622840248 1757 EA----EEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAA 1811
Cdd:COG3206 323 EAlqarEASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1170-1442 |
8.75e-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: 41.09 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1170 GSRKREAELGRLRRELEEAALRH---------------------------------EATVAALRRKQAEGAAELGEQVDS 1216
Cdd:COG3096 779 GRAAREKRLEELRAERDELAEQYakasfdvqklqrlhqafsqfvgghlavafapdpEAELAALRQRRSELERELAQHRAQ 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1217 LQRVRQKLEKEKSELRM-----------EVDDLAANVETLTRAKASAEKlCRTYEDQLSEAKIKVEELQRQLADASTQRG 1285
Cdd:COG3096 859 EQQLRQQLDQLKEQLQLlnkllpqanllADETLADRLEELREELDAAQE-AQAFIQQHGKALAQLEPLVAVLQSDPEQFE 937
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1286 RLQTESGELSHLLEEKECLISQLS----RGKALA-AQSLEELRRQLEEESKAKSALAHAVQALRHDCDLLREQHEEeaea 1360
Cdd:COG3096 938 QLQADYLQAKEQQRRLKQQIFALSevvqRRPHFSyEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQ---- 1013
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1361 qaelqrlLSKANAEVAQWRSKYEA------DAIQRTEELE-----EAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQ 1429
Cdd:COG3096 1014 -------YSQYNQVLASLKSSRDAkqqtlqELEQELEELGvqadaEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCE 1086
|
330
....*....|...
gi 1622840248 1430 TESEDVTLELERA 1442
Cdd:COG3096 1087 AEMDSLQKRLRKA 1099
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1737-1916 |
8.76e-03 |
|
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: 40.88 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1737 LEADLAQLSGEVEEAAQE-RREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAeqaalRGG 1815
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEhKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELN-----RLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 1816 KKQVQKLEAKVRELEA-ELDAEQKKHaeALKGvrkherRVKELAYQAEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQ 1894
Cdd:pfam05557 82 KKYLEALNKKLNEKESqLADAREVIS--CLKN------ELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQ 153
|
170 180
....*....|....*....|..
gi 1622840248 1895 QantnLAKYRKAQHELDDAEER 1916
Cdd:pfam05557 154 L----RQNLEKQQSSLAEAEQR 171
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
866-1062 |
9.18e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 9.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 866 LRGALAAAEAKRQELEEthvsvtqekndlalQLQAEQDNLADAEERCHLLIKSKVQLEGKVKELSERLED-----EEEVN 940
Cdd:PRK04863 990 LRQRLEQAEQERTRARE--------------QLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDlgvpaDSGAE 1055
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840248 941 ADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDE----------SVARLTKEKKALQEAH 1010
Cdd:PRK04863 1056 ERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREqvvnakagwcAVLRLVKDNGVERRLH 1135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622840248 1011 QQALGDLQAEEDRvSALTKAKLRLEQQVEDLEcSLEQEKKLRMDTERAKRKL 1062
Cdd:PRK04863 1136 RRELAYLSADELR-SMSDKALGALRLAVADNE-HLRDVLRLSEDPKRPERKV 1185
|
|
| |
