|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-770 |
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: 1331.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEvtSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDLAKKK--DSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14913 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14913 239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 420 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14913 319 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 580 FSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAEAEgGGPKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14913 479 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADAD-SGKKKVAKKKGSSFQTVSALFRENL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 660 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 739
Cdd:cd14913 558 NKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQF 637
|
650 660 670
....*....|....*....|....*....|.
gi 305632842 740 IDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14913 638 IDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-770 |
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: 1320.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 420 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 580 FSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAEAE--GGGPKKGGKKKGSSFQTVSALFRE 657
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGAsaGGGAKKGGKKKGSSFQTVSALFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 658 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 737
Cdd:cd14912 561 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 640
|
650 660 670
....*....|....*....|....*....|...
gi 305632842 738 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14912 641 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
100-770 |
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: 1316.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEvtsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKES---GKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd01377 238 DILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 420 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd01377 318 KEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKP-MGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKvvKGKAEA 578
Cdd:cd01377 398 EQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPK--PKKSEA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 579 HFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSgtqtAEAEGGGPKKGGKKKGSSFQTVSALFREN 658
Cdd:cd01377 476 HFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFK----DYEESGGGGGKKKKKGGSFRTVSQLHKEQ 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 659 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 738
Cdd:cd01377 552 LNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGF 631
|
650 660 670
....*....|....*....|....*....|..
gi 305632842 739 FiDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd01377 632 D-DGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-770 |
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: 1270.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 420 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 580 FSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAEAEGGGPKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 660 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 739
Cdd:cd14910 561 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 305632842 740 IDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14910 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
100-770 |
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: 1269.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEvtSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEE--SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14918 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 420 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 580 FSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAEAEgGGPKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14918 479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEAD-SGAKKGAKKKGSSFQTVSALFRENL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 660 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 739
Cdd:cd14918 558 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQF 637
|
650 660 670
....*....|....*....|....*....|.
gi 305632842 740 IDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14918 638 IDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-770 |
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: 1255.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 420 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 580 FSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAEAEGGGPKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14915 481 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 660 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 739
Cdd:cd14915 561 NKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 305632842 740 IDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14915 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-770 |
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: 1219.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEvTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQ-QPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14923 240 DILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 420 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14923 400 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 580 FSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAEA-EGGGPKKGGKKKGSSFQTVSALFREN 658
Cdd:cd14923 480 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAgDSGGSKKGGKKKGSSFQTVSAVFREN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 659 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 738
Cdd:cd14923 560 LNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQ 639
|
650 660 670
....*....|....*....|....*....|..
gi 305632842 739 FIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14923 640 FIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
101-770 |
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: 1162.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 181 SGAGKTVNTKRVIQYFATIAVTGE--KKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd14927 82 SGAGKTVNTKRVIQYFAIVAALGDgpGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSA 338
Cdd:cd14927 162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 339 IDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQ 418
Cdd:cd14927 242 MDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 419 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14927 322 SVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 499 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKV-VKGKAE 577
Cdd:cd14927 402 LEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPdKKRKYE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 578 AHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSG--TQTAEAEGGGPKKGGKKKGSSFQTVSALF 655
Cdd:cd14927 482 AHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENyvGSDSTEDPKSGVKEKRKKAASFQTVSQLH 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 656 RENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 735
Cdd:cd14927 562 KENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIP 641
|
650 660 670
....*....|....*....|....*....|....*
gi 305632842 736 EGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14927 642 DDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-770 |
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: 1149.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14917 159 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 420 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14917 319 VQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 580 FSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAEAEgGGPKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14917 479 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAP-IEKGKGKAKKGSSFQTVSALHRENL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 660 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 739
Cdd:cd14917 558 NKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 637
|
650 660 670
....*....|....*....|....*....|.
gi 305632842 740 IDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14917 638 IDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-770 |
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: 1135.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNAN-KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14916 160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14916 240 DVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 420 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14916 320 VQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14916 400 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 580 FSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAEAEGGGPKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14916 480 FSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSSFQTVSALHRENL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 660 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 739
Cdd:cd14916 560 NKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 639
|
650 660 670
....*....|....*....|....*....|.
gi 305632842 740 IDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14916 640 IDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
100-770 |
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: 1034.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEevtsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKK-------LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14929 154 MLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14929 233 DILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 420 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14929 313 IEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14929 393 EQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAH 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 580 FSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAEAeGGGPKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14929 473 FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDS-AIQFGEKKRKKGASFQTVASLHKENL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 660 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 739
Cdd:cd14929 552 NKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKF 631
|
650 660 670
....*....|....*....|....*....|.
gi 305632842 740 IDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14929 632 VSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
88-770 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1026.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 88 IEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFML 167
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 168 TDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEevtsgkmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 247
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNV--------GRLEEQILQSNPILEAFGNAKTVRNNNSSRF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 248 GKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQ-GEISVASI 326
Cdd:pfam00063 153 GKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRL-TNPKDYHYLSQsGCYTIDGI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 327 DDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPR 406
Cdd:pfam00063 232 DDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 407 VKVGNEFVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:pfam00063 312 IKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYVN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 486 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSA 564
Cdd:pfam00063 392 EKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 565 NFQKPKVvkgKAEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAE---AEGGGPKKGG 641
Cdd:pfam00063 470 HFQKPRL---QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAEsaaANESGKSTPK 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 642 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 721
Cdd:pfam00063 547 RTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQE 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 305632842 722 FKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:pfam00063 627 FVQRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
81-782 |
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: 992.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 81 NPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISD 160
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 161 NAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAvtgekkkeevTSGKMQGTLEDQIISANPLLEAFGNAKTVR 240
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVS----------GSNTEVGSVEDQILESNPILEAFGNAKTLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 241 NDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQG- 319
Cdd:smart00242 151 NNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQGg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 320 EISVASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQA-EPDGTEVADKAAYLQSLNSADL 398
Cdd:smart00242 230 CLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 399 LKALCYPRVKVGNEFVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQ 478
Cdd:smart00242 310 EKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 479 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYd 557
Cdd:smart00242 390 LCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLN- 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 558 QHLGKSANFQKPKVvkgKAEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAEaegggp 637
Cdd:smart00242 468 QHHKKHPHFSKPKK---KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNA------ 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 638 kkggkKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRI 717
Cdd:smart00242 539 -----GSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRL 613
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305632842 718 LYADFKQRYKVLNASAIPEGQFiDSKKASEKLLASIDIDHTQYKFGHTKVFFKAGLLGLLEEMRD 782
Cdd:smart00242 614 PFDEFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
101-770 |
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: 990.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14934 2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEvtsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14934 82 SGAGKTENTKKVIQYFANIGGTGKQSSDG------KGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAID 340
Cdd:cd14934 156 LAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 341 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQTV 420
Cdd:cd14934 236 VLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 421 EQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 500
Cdd:cd14934 316 EQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 501 QEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGK-AEAH 579
Cdd:cd14934 396 QEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAH 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 580 FSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFsgtqtaEAEGGGPKKGGKKKGSSFQTVSALFRENL 659
Cdd:cd14934 476 FELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLF------KEEEAPAGSKKQKRGSSFMTVSNFYREQL 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 660 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqF 739
Cdd:cd14934 550 NKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-F 628
|
650 660 670
....*....|....*....|....*....|.
gi 305632842 740 IDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14934 629 VDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-770 |
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: 975.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEvtsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAA----KSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14909 157 KLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14909 237 DILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 420 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14909 317 VQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVK-GKAEA 578
Cdd:cd14909 397 EQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 579 HFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAEAEGGGPKKGGKKKGSSFQTVSALFREN 658
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQ 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 659 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 738
Cdd:cd14909 557 LNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE 636
|
650 660 670
....*....|....*....|....*....|..
gi 305632842 739 fiDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14909 637 --DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
30-1116 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 837.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 30 RPFDAKTSVFVAEPKESFVKGTIQsregGKVTVKTEGGATLTVKDDQVFPMNPPKYDKIEDMAMMTHLHEPAVLYNLKER 109
Cdd:COG5022 14 IPDEEKGWIWAEIIKEAFNKGKVT----EEGKKEDGESVSVKKKVLGNDRIKLPKFDGVDDLTELSYLNEPAVLHNLEKR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 110 YAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNT 189
Cdd:COG5022 90 YNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 190 KRVIQYFAtiAVTGekkkeevTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETY 269
Cdd:COG5022 170 KRIMQYLA--SVTS-------SSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 270 LLEKSRVTFQLKAERSYHIFYQITSNKkPELIEMLLITTNPYDYPFVSQGE-ISVASIDDQEELMATDSAIDILGFTNEE 348
Cdd:COG5022 241 LLEKSRVVHQNKNERNYHIFYQLLAGD-PEELKKLLLLQNPKDYIYLSQGGcDKIDGIDDAKEFKITLDALKTIGIDEEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 349 KVSIYKLTGAVMHYGNLKFKqKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQTVEQVTNAVG 428
Cdd:COG5022 320 QDQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 429 ALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEG 508
Cdd:COG5022 399 SLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 509 IEWTFIDFgMDLAACIELIEK--PMGIFSILEEECMFPKATDTSFKNKLYDQ-HLGKSANFQKPKVVKGKaeahFSLIHY 585
Cdd:COG5022 479 IEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNK----FVVKHY 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 586 AGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAEaegggpkkggkkKGSSFQTVSALFRENLNKLMTN 665
Cdd:COG5022 554 AGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE------------SKGRFPTLGSRFKESLNSLMST 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 666 LRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFI---DS 742
Cdd:COG5022 622 LNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwkeDT 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 743 KKASEKLLASIDIDHTQYKFGHTKVFFKAGLLGLLEEMRDDKLAQLITRTQARCRGFLARVEYQRMVERREAIFCIQYNI 822
Cdd:COG5022 702 KNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGF 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 823 RAFMNVKHWPWMKLFFKIKPLLKSAETEKEMATMKEEFQKTKDELaKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGL 902
Cdd:COG5022 782 RLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTI-KREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKR 860
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 903 ADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINaELTAKKRKLEDECSELKKDID-----DLELTLAKVEKEKHATEN 977
Cdd:COG5022 861 FSLLKKETIYLQSAQRVELAERQLQELKIDVKSIS-SLKLVNLELESEIIELKKSLSsdlieNLEFKTELIARLKKLLNN 939
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 978 -KVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQekklRMDLERAK 1056
Cdd:COG5022 940 iDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQ----YGALQEST 1015
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305632842 1057 RKLEgdlklaqesIMDIENEKQQLDEKLKKKEFEISNLQSKIED-EQALGI---QLQKKIKELQ 1116
Cdd:COG5022 1016 KQLK---------ELPVEVAELQSASKIISSESTELSILKPLQKlKGLLLLennQLQARYKALK 1070
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
100-770 |
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: 835.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQ-EAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 179 GESGAGKTVNTKRVIQYFATIAvtgekKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALS-----GSGSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPF----VSQGEISVASIDDQEELMA 334
Cdd:cd00124 156 GRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylNSSGCDRIDGVDDAEEFQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 335 TDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREE--QAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNE 412
Cdd:cd00124 236 LLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 413 FVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQL--DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQ 490
Cdd:cd00124 316 TITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALspTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 491 FFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKP 569
Cdd:cd00124 396 FFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 570 KvvkgKAEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKsamktlahlfsgtqtaeaegggpkkggkkkgssfq 649
Cdd:cd00124 475 R----KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS----------------------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 650 tvSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 729
Cdd:cd00124 516 --GSQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRIL 593
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 305632842 730 NASAiPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd00124 594 APGA-TEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
101-770 |
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: 789.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 181 SGAGKTVNTKRVIQYFATIAVTGEKK-----KEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 255
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVAASKPKGsgavpHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 256 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITtNPYDYPFVSQGEISVASIDDQEELMAT 335
Cdd:cd14911 162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 336 DSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEFV 414
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 415 TKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 494 HHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLgksanfQKPKVVK 573
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS------MHPKFMK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 574 G--KAEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQT---AEAEGGGPKKGGKKKGSSF 648
Cdd:cd14911 474 TdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIvgmAQQALTDTQFGARTRKGMF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 649 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 728
Cdd:cd14911 554 RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 305632842 729 LNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14911 634 LTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-770 |
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: 768.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEevtsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14920 82 SGAGKTENTKKVIQYLAHVASSHKGRKD----HNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLIttNPYD-YPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14920 158 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL--EGFNnYRFLSNGYIPIPGQQDKDNFQETMEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQ 418
Cdd:cd14920 236 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 419 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14920 315 TKEQADFAVEALAKATYERLFRWLVHRINKALDRTK-RQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 497 FVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFQKPKVVK 573
Cdd:cd14920 394 FILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKL-VQEQGSHSKFQKPRQLK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 574 GKAEahFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFS-------GTQTAEAEGGGPKKGGKKKGS 646
Cdd:cd14920 473 DKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKdvdrivgLDQVTGMTETAFGSAYKTKKG 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 647 SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 726
Cdd:cd14920 551 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 305632842 727 KVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14920 631 EILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
101-770 |
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: 714.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14932 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14932 82 SGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMATDSAID 340
Cdd:cd14932 162 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCL-EDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 341 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 420 VEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14932 320 QEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 499 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKvvKGK 575
Cdd:cd14932 400 LEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPK--KLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 576 AEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFS------GTQTAEAEGGGPKKGGKKKGSSFQ 649
Cdd:cd14932 477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKdvdrivGLDKVAGMGESLHGAFKTRKGMFR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 650 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 729
Cdd:cd14932 557 TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 636
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 305632842 730 NASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14932 637 TPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
101-770 |
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: 699.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14921 2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14921 82 SGAGKTENTKKVIQYLAVVASSHKGKKDTSITGE----LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPyDYPFVSQGEISVASIDDQEELMATDSAID 340
Cdd:cd14921 158 IVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFN-NYTFLSNGFVPIPAAQDDEMFQETLEAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 341 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14921 237 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 420 VEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14921 316 KEQADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 499 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKGK 575
Cdd:cd14921 396 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLC-TEQGNHPKFQKPKQLKDK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 576 AEahFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGT-------QTAEAEGGGPKKGGKKKGSSF 648
Cdd:cd14921 475 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldQMAKMTESSLPSASKTKKGMF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 649 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 728
Cdd:cd14921 553 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 305632842 729 LNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14921 633 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-770 |
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: 680.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 179 GESGAGKTVNTKRVIQYFATiaVTGEKKKEEVTsgkmqgtlEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFAT--VGGSSSGETQV--------EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-TSNKKPELIEMLLitTNPYDYPFVSQGE-ISVASIDDQEELMATD 336
Cdd:cd01380 151 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLcAAASLPELKELHL--GSAEDFFYTNQGGsPVIDGVDDAAEFEETR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 337 SAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTK 416
Cdd:cd01380 229 KALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 417 GQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQP--RQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 494
Cdd:cd01380 309 PLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 495 HMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGK-SANFQKPKVVK 573
Cdd:cd01380 389 HVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 574 GKaeahFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKtlahlfsgtqtaeaegggpkkggkkkgssFQTVSA 653
Cdd:cd01380 468 TA----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR-----------------------------KKTVGS 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 654 LFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASA 733
Cdd:cd01380 515 QFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK 594
|
650 660 670
....*....|....*....|....*....|....*..
gi 305632842 734 ipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd01380 595 --EWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-770 |
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: 669.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14919 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEevtsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14919 82 SGAGKTENTKKVIQYLAHVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLIttNPYD-YPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14919 155 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14919 233 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 420 VEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14919 313 KEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 499 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKGK 575
Cdd:cd14919 393 LEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPKQLKDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 576 AEahFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGT-------QTAEAEGGGPKKGGKKKGSSF 648
Cdd:cd14919 472 AD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldQVAGMSETALPGAFKTRKGMF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 649 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 728
Cdd:cd14919 550 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 305632842 729 LNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14919 630 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
101-770 |
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: 667.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd15896 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd15896 82 SGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMATDSAID 340
Cdd:cd15896 162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLL-ENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 341 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQTV 420
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 421 EQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKvvKGKA 576
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVL-QEQGTHPKFFKPK--KLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 577 EAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQT-----AEAEGGGPKKGGKKKGSSFQTV 651
Cdd:cd15896 478 EADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRivgldKVSGMSEMPGAFKTRKGMFRTV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 652 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 731
Cdd:cd15896 558 GQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 637
|
650 660 670
....*....|....*....|....*....|....*....
gi 305632842 732 SAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd15896 638 NAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-770 |
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: 654.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14930 2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEvtsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14930 82 SGAGKTENTKKVIQYLAHVASSPKGRKEP----GVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYdYPFVSQGEiSVASIDDQEELMATDSAID 340
Cdd:cd14930 158 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGP-SSSPGQERELFQETLESLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 341 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQT 419
Cdd:cd14930 236 VLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 420 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd14930 315 KEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 498 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFQKPKVVKG 574
Cdd:cd14930 394 VLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQRPRHLRD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 575 KAEahFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAEAEGGGPKKGG-----KKKGSSFQ 649
Cdd:cd14930 473 QAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDgppggRPRRGMFR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 650 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 729
Cdd:cd14930 551 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 305632842 730 NASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14930 631 TPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-770 |
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: 641.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRgkKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 180 ESGAGKTVNTKRVIQYFATIAVTGekkkeevtsgkmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd01383 79 ESGAGKTETAKIAMQYLAALGGGS-------------SGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQGE-ISVASIDDQEELMATDSA 338
Cdd:cd01383 146 KICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQSNcLTIDGVDDAKKFHELKEA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 339 IDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQ 418
Cdd:cd01383 225 LDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 419 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLDT-KQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd01383 305 TLQQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 498 VLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFqkpkvvKGKA 576
Cdd:cd01383 385 KLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGER 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 577 EAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKtLAHLFSGTQTAEAEGGGPKKGGKKKGSSFQTVSALFR 656
Cdd:cd01383 457 GGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQ-LPQLFASKMLDASRKALPLTKASGSDSQKQSVATKFK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 657 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 736
Cdd:cd01383 536 GQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSA 615
|
650 660 670
....*....|....*....|....*....|....
gi 305632842 737 GQFIDSkkASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd01383 616 SQDPLS--TSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
101-770 |
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: 634.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 181 SGAGKTVNTKRVIQYFATIavtgekkkeevtSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd01381 82 SGAGKTESTKLILQYLAAI------------SGQ-HSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQGE-ISVASIDDQEELMATDSAI 339
Cdd:cd01381 149 IEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGD-ASDYYYLTQGNcLTCEGRDDAAEFADIRSAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQRE--EQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKG 417
Cdd:cd01381 228 KVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 418 QTVEQVTNAVGALAKAVYEKMFLWMVARIN----QQLDTKQPRQYfIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd01381 308 LSAEQALDVRDAFVKGIYGRLFIWIVNKINsaiyKPRGTDSSRTS-IGVLDIFGFENFEVNSFEQLCINFANENLQQFFV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 494 HHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPkvv 572
Cdd:cd01381 387 RHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKP--- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 573 KGKAEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAEAEGGGPKkggkkkgssfQTVS 652
Cdd:cd01381 462 KSDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKS----------PTLS 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 653 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLnAS 732
Cdd:cd01381 532 SQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVL-VP 610
|
650 660 670
....*....|....*....|....*....|....*...
gi 305632842 733 AIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd01381 611 GIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
101-770 |
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: 626.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 181 SGAGKTVNTKRVIQYFAtiAVTGeKKKEEVTSGKmqgtleDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd01378 82 SGAGKTEASKRIMQYIA--AVSG-GSESEVERVK------DMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAID 340
Cdd:cd01378 153 PVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 341 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDgTEVADKAAYLQSLNSADLLKALCYPRVKVGNEF---VTKG 417
Cdd:cd01378 233 VIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 418 QTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQ-YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHhm 496
Cdd:cd01378 312 LNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE-- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 497 FVL--EQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFP-KATDTSFKNKLyDQHLGKSANFQKPKVV 572
Cdd:cd01378 390 LTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGH 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 573 KGKAEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAEAEGGGPkkggkkkgssfqTVS 652
Cdd:cd01378 468 FELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDSKKRPP------------TAG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 653 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 732
Cdd:cd01378 536 TKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPK 615
|
650 660 670
....*....|....*....|....*....|....*...
gi 305632842 733 AIPEGQFIDsKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd01378 616 TWPAWDGTW-QGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
101-770 |
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: 595.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 181 SGAGKTVNTKRVIQYFAtiAVTGEkkkeevtsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14883 82 SGAGKTETTKLILQYLC--AVTNN-----------HSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKK--PELIEmLLITTNPYDYPFVSQ-GEISVASIDDQEELMATDS 337
Cdd:cd14883 149 IKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKE-KLKLGEPEDYHYLNQsGCIRIDNINDKKDFDHLRL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 338 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTK 416
Cdd:cd14883 228 AMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 417 GQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14883 308 PLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 497 FVLEQEEYKKEGIEWTFIDFgMDLAACIELIEK-PMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKvvKGK 575
Cdd:cd14883 388 FKLEQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPD--RRR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 576 AEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQ----TAEAEGGGPKKGGKKKGSSFQTV 651
Cdd:cd14883 464 WKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDllalTGLSISLGGDTTSRGTSKGKPTV 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 652 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 731
Cdd:cd14883 544 GDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDP 623
|
650 660 670
....*....|....*....|....*....|....*....
gi 305632842 732 SAIPEGQFIDsKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14883 624 RARSADHKET-CGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
100-770 |
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: 586.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 179 GESGAGKTVNTKRVIQYFATIAvtgekkKEEVTSGKmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG------GRAVTEGR---SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQGE-ISVASIDDQEELMATDS 337
Cdd:cd01384 152 GRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKD-PKQFHYLNQSKcFELDGVDDAEEYRATRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 338 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKqkqreEQAEPDGTEVADKAAYLQSLNSADLL--------KALCYPRVKV 409
Cdd:cd01384 231 AMDVVGISEEEQDAIFRVVAAILHLGNIEFS-----KGEEDDSSVPKDEKSEFHLKAAAELLmcdekaleDALCKRVIVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 410 GNEFVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 489
Cdd:cd01384 306 PDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 490 QFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQhLGKSANFQK 568
Cdd:cd01384 386 QHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 569 PKvvkgKAEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLF-----SGTQTAeaegggpkkggkk 643
Cdd:cd01384 464 PK----LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFpplprEGTSSS------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 644 kgSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFK 723
Cdd:cd01384 527 --SKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFL 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 305632842 724 QRYKVLnASAIPEGQFiDSKKASEKLLASIDIDhtQYKFGHTKVFFK 770
Cdd:cd01384 605 DRFGLL-APEVLKGSD-DEKAACKKILEKAGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
101-770 |
1.10e-171 |
|
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: 538.21 E-value: 1.10e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKRQEAPPHIFSISDNAY-QFM---LTDRENQSI 175
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYtQLIqsgVLDPSNQSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 176 LITGESGAGKTVNTKRVIQYFATI----AVTGEKKKEEVTSGKMQ--GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14890 82 IISGESGAGKTEATKIIMQYLARItsgfAQGASGEGEAASEAIEQtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 250 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQGEISVASIDDQ 329
Cdd:cd14890 162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQT-PVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 330 EELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGT-EVADKAAYLQSLNSADLLKALCYPRVK 408
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQLF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 409 VGNEFVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 488
Cdd:cd14890 321 VGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 489 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-----KPmGIFSILEEECMFPKA-TDTSFKNKLYDQHLGK 562
Cdd:cd14890 401 QRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgkvngKP-GIFITLDDCWRFKGEeANKKFVSQLHASFGRK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 563 S------------ANFQKPKVvkgKAEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSamktlahlfsgtqta 630
Cdd:cd14890 479 SgsggtrrgssqhPHFVHPKF---DADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQS--------------- 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 631 eaegggpkkggkkkGSSFQTVS--ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRI 708
Cdd:cd14890 541 --------------RRSIREVSvgAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQI 606
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305632842 709 CRKGFPSRILYADFKQRYKVLNASAipegqfiDSKKASEKLLASI-DIDHTQYKFGHTKVFFK 770
Cdd:cd14890 607 RQQGFALREEHDSFFYDFQVLLPTA-------ENIEQLVAVLSKMlGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
103-770 |
2.07e-169 |
|
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: 531.82 E-value: 2.07e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd01382 4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 182 GAGKTVNTKRVIQYFATIAvtgekkkeevtsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd01382 84 GAGKTESTKYILRYLTESW------------GSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLittnpydypfvsqgeiSVASIDDQEELMATDSAIDI 341
Cdd:cd01382 152 VGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMDKAMKK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 342 LGFTNEEKVSIYKLTGAVMHYGNLKFkqkqrEEQAEPD--GTEVADK-------AAYLQSLNSADLLKALCYpRVKVGNE 412
Cdd:cd01382 216 IGLSDEEKLDIFRVVAAVLHLGNIEF-----EENGSDSggGCNVKPKseqsleyAAELLGLDQDELRVSLTT-RVMQTTR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 413 FVTKGQ------TVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQpRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 486
Cdd:cd01382 290 GGAKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET-SSYFIGVLDIAGFEYFEVNSFEQFCINYCNE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 487 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLgKSAN 565
Cdd:cd01382 369 KLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK-NHFR 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 566 FQKPKvvKGKAEAH--------FSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAEAEGGGP 637
Cdd:cd01382 447 LSIPR--KSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKDSKQK 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 638 KKGGkkkgsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRI 717
Cdd:cd01382 525 AGKL-----SFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRT 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 305632842 718 LYADFKQRYKVLNASAIPEgqfIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd01382 600 SFHDLYNMYKKYLPPKLAR---LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
100-770 |
2.83e-168 |
|
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: 529.26 E-value: 2.83e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRgKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 179 GESGAGKTVNTKRVIQYFATIAVTGEKKKEEVtsgkmqgtlEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF--- 255
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRSLV---------EAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFskl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 256 ------GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITS-----------------------NKKPELIEMLLI 306
Cdd:cd14888 151 kskrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMSSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 307 TT-NPYDYPFVSqGEISVASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQA---EPDGTE 382
Cdd:cd14888 231 EPhLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASCTD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 383 VADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIG 461
Cdd:cd14888 310 DLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 462 VLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELI-EKPMGIFSILEEE 540
Cdd:cd14888 390 VLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 541 CMFPKATDTSFKNKLYDQHlgksANFQKPKVVKGKAEAhFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTL 620
Cdd:cd14888 469 CFVPGGKDQGLCNKLCQKH----KGHKRFDVVKTDPNS-FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFI 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 621 AHLFSgtqtaeaEGGGPKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCN 700
Cdd:cd14888 544 SNLFS-------AYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYG 616
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 701 GVLEGIRICRKGFPSRILYADFKQRYKVLnasAIPEGQfidskkasekllasidIDHTQYKFGHTKVFFK 770
Cdd:cd14888 617 GVLQAVQVSRAGYPVRLSHAEFYNDYRIL---LNGEGK----------------KQLSIWAVGKTLCFFK 667
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
850-1927 |
3.35e-166 |
|
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: 537.84 E-value: 3.35e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 850 EKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTER 929
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 930 AEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQ 1009
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1010 TLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEF 1089
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1090 EISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNK 1169
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1170 KREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNL 1249
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1250 EKMCRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKA 1329
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1330 KNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQAAEEHVE 1409
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1410 AVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMK 1489
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1490 NAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLEL 1569
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1570 NQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRN 1649
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1650 TQGILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLIN 1729
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1730 TKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLAL 1809
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1810 KGGKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEA 1889
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 305632842 1890 EEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLRVK 1927
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
100-770 |
8.93e-166 |
|
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: 521.64 E-value: 8.93e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 180 ESGAGKTVNTKRVIQYFATIAVTgekkkeevTSGkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS--------TNG-----VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSnkKPELIEMLLITTNPyDYPFVSQGE-ISVASIDDQEELMATDSA 338
Cdd:cd14872 148 RICGASTENYLLEKSRVVYQIKGERNFHIFYQLLA--SPDPASRGGWGSSA-AYGYLSLSGcIEVEGVDDVADFEEVVLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 339 IDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEP----DGTEVADKAAYLQsLNSADLLKALCYPRVKVgnefv 414
Cdd:cd14872 225 MEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGstvaNRDVLKEVATLLG-VDAATLEEALTSRLMEI----- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 415 tKGQ-------TVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 486
Cdd:cd14872 299 -KGCdptriplTPAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 487 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEK-PMGIFSILEEECMFPKATDTSFKNKLyDQHLGKSAN 565
Cdd:cd14872 378 KLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAA-NQTHAAKST 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 566 FQKPKVvkGKAEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSgtqtaeaegggpkKGGKKKG 645
Cdd:cd14872 456 FVYAEV--RTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFP-------------PSEGDQK 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 646 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 725
Cdd:cd14872 521 TSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKR 600
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 305632842 726 YKVLNaSAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14872 601 YRFLV-KTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
100-770 |
2.51e-164 |
|
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: 518.18 E-value: 2.51e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 179 GESGAGKTVNTKRVIQYFATIAvtgekkkeevtSGKMQGTLEdQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA-----------GGLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELiEMLLITTNPYDYPFvSQGEISVASIDDQEELMATDSA 338
Cdd:cd14903 149 GTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEE-RLFLDSANECAYTG-ANKTIKIEGMSDRKHFARTKEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 339 IDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE--PDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTK 416
Cdd:cd14903 227 LSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 417 GQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14903 307 PLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 497 FVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKgka 576
Cdd:cd14903 387 FKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR--- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 577 eAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAEAEGGGPKKGGKKKGS----SFQTVS 652
Cdd:cd14903 463 -TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRggalTTTTVG 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 653 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLnas 732
Cdd:cd14903 542 TQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLF--- 618
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 305632842 733 aIPEGQFIDSKKAS--EKLLASIDIDH-TQYKFGHTKVFFK 770
Cdd:cd14903 619 -LPEGRNTDVPVAErcEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
103-770 |
4.07e-164 |
|
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: 518.85 E-value: 4.07e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESG 182
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 183 AGKTVNTKRVIQYFATIavtgekkkeevtSGKMQGT-LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd01385 84 SGKTESTNFLLHHLTAL------------SQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQGE-ISVASIDDQEELMATDSAID 340
Cdd:cd01385 152 RGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQ-PEDYHYLNQSDcYTLEGEDEKYEFERLKQAME 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 341 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQK--QREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQ 418
Cdd:cd01385 231 MVGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 419 TVEQVTNAVGALAKAVYEKMFLWMVARINQQL----DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 494
Cdd:cd01385 311 KLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 495 HMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKlYDQHLGKSANFQKPKvvk 573
Cdd:cd01385 391 HIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQ--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 574 gKAEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAM-----------------KTLAHLF--------SGTQ 628
Cdd:cd01385 466 -VMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSafvreligidpvavfrwAVLRAFFramaafreAGRR 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 629 TAEAEGGGPKKGGKKKGSSF---------QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRC 699
Cdd:cd01385 545 RAQRTAGHSLTLHDRTTKSLlhlhkkkkpPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRY 624
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305632842 700 NGVLEGIRICRKGFPSRILYADFKQRYKVLnasaIPEGQfIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd01385 625 TGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGL-ISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
101-770 |
1.81e-161 |
|
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: 510.45 E-value: 1.81e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEvtsgkmqgtledQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTGK 260
Cdd:cd01387 82 SGSGKTEATKLIMQYLAAVNQRRNNLVTE------------QILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQI------TSNKKPELIEmllittnPYDYPFVSQG-EISVASIDDQEELM 333
Cdd:cd01387 149 IVGAITSQYLLEKSRIVTQAKNERNYHVFYELlaglpaQLRQKYGLQE-------AEKYFYLNQGgNCEIAGKSDADDFR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 334 ATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEpdGTEVADKA-----AYLQSLNSADLLKALCYPRVK 408
Cdd:cd01387 222 RLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGQE--GVSVGSDAeiqwvAHLLQISPEGLQKALTFKVTE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 409 VGNEFVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 488
Cdd:cd01387 300 TRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 489 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQ 567
Cdd:cd01387 380 QYYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYS 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 568 KPKVvkGKAEahFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSG--TQTAEAEGGGPKKGGKKKG 645
Cdd:cd01387 458 KPRM--PLPE--FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSShrAQTDKAPPRLGKGRFVTMK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 646 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 725
Cdd:cd01387 534 PRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDR 613
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 305632842 726 YKVLNASAIPEGQFIDSKKASEKLLASIDIDhTQYKFGHTKVFFK 770
Cdd:cd01387 614 YRCLVALKLPRPAPGDMCVSLLSRLCTVTPK-DMYRLGATKVFLR 657
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-770 |
6.89e-161 |
|
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: 507.97 E-value: 6.89e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01379 1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 180 ESGAGKTVNTKRVIQYFATIavtgekkkeevtsGKMQ-GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd01379 81 ESGAGKTESANLLVQQLTVL-------------GKANnRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTST 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI----TSNKKpeLIEMLLITTNPYDYPFVSQGEISVASIDD--QEEL 332
Cdd:cd01379 148 GAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIyaglAEDKK--LAKYKLPENKPPRYLQNDGLTVQDIVNNSgnREKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 333 MATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQ----AEPDGTEVADKAAYLQSLNSADLLKALCYPRVK 408
Cdd:cd01379 226 EEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 409 VGNEFVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQP---RQYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:cd01379 306 TRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSasdEPLSIGILDIFGFENFQKNSFEQLCINIAN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 486 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFG-----MDLaacieLIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHl 560
Cdd:cd01379 386 EQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 561 gKSANFQKPKvvkgKAEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAhlfsgtqtaeaegggpkkg 640
Cdd:cd01379 460 -KSKYYWRPK----SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 641 gkkkgssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYA 720
Cdd:cd01379 516 --------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFA 587
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 305632842 721 DFKQRYKVL--NASAIPEGqfidSKKASEKLLASIDIDHtqYKFGHTKVFFK 770
Cdd:cd01379 588 DFLKRYYFLafKWNEEVVA----NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
100-768 |
1.27e-158 |
|
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: 502.40 E-value: 1.27e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAY------RGKKRQEAPPHIFSISDNAYQFMLTDRE-- 171
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 172 --NQSILITGESGAGKTVNTKRVIQYFATIAvTGEKKKEEVTSgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVS-SATTHGQNATE---RENVRDRVLESNPILEAFGNARTNRNNNSSRFGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 250 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNP-YDYPFVSQGEISVASIDD 328
Cdd:cd14901 157 FIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEeYKYLNSSQCYDRRDGVDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 329 QEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAY-LQSLNSADLLKALCYPRV 407
Cdd:cd14901 237 SVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAACdLLGLDMDVLEKTLCTREI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 408 KVGNEFVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQP--RQYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:cd14901 317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 486 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQhLGKSA 564
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 565 NFQKPKVVKGKAEahFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAhlfsgtqtaeaegggpkkggkkk 644
Cdd:cd14901 475 SFSVSKLQQGKRQ--FVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS----------------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 645 gssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQ 724
Cdd:cd14901 530 ----STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVH 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 305632842 725 RYKVLNAS------AIPEGQFIDSKKASEKLLASIDIDHTQykFGHTKVF 768
Cdd:cd14901 606 TYSCLAPDgasdtwKVNELAERLMSQLQHSELNIEHLPPFQ--VGKTKVF 653
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
101-770 |
5.10e-156 |
|
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: 495.47 E-value: 5.10e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 180 ESGAGKTVNTKRVIQYFATIAvtgeKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVIS----QQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQ-GEISVASIDDQEELMATDSA 338
Cdd:cd14873 158 NIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLST-PENYHYLNQsGCVEDKTISDQESFREVITA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 339 IDILGFTNEEKVSIYKLTGAVMHYGNLKFkqkqreeqAEPDGTEVADK-----AAYLQSLNSADLLKALCYPRVKVGNEF 413
Cdd:cd14873 237 MEVMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKtalgrSAELLGLDPTQLTDALTQRSMFLRGEE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 414 VTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQyFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14873 309 ILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK-SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 494 HHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKVvk 573
Cdd:cd14873 388 KHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKPRV-- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 574 gkAEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAEAEGGGPKKGGKKKgssfQTVSA 653
Cdd:cd14873 464 --AVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRR----PTVSS 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 654 LFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL-NAS 732
Cdd:cd14873 538 QFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLmRNL 617
|
650 660 670
....*....|....*....|....*....|....*...
gi 305632842 733 AIPEgqfiDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14873 618 ALPE----DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
106-770 |
1.60e-155 |
|
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: 494.28 E-value: 1.60e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNpevVTAYRGKKRQEA-----PPHIFSISDNAYQFMLTDR----ENQSI 175
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYD---VPGFDSQRKEEAtasspPPHVFSIAERAYRAMKGVGkgqgTPQSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 176 LITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 255
Cdd:cd14892 84 VVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 256 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpELIEMLLITTNPYDYPFVSQGE-ISVASIDDQEELMA 334
Cdd:cd14892 164 NSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD-ANENAALELTPAESFLFLNQGNcVEVDGVDDATEFKQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 335 TDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVAD--KAAYLQSLNSADLLKALCYpRVKVGne 412
Cdd:cd14892 243 LRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNvaKAAGLLGVDAAELMFKLVT-QTTST-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 413 fvTKGQTVE------QVTNAVGALAKAVYEKMFLWMVARIN----QQL------DTKQPRQYFIGVLDIAGFEIFDFNSL 476
Cdd:cd14892 320 --ARGSVLEikltarEAKNALDALCKYLYGELFDWLISRINachkQQTsgvtggAASPTFSPFIGILDIFGFEIMPTNSF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 477 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEK-PMGIFSILEEECMFP-KATDTSFKNK 554
Cdd:cd14892 398 EQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 555 LYDQHLGKSANFQKPKVvkgkAEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMktlahlfsgtqtaeaeg 634
Cdd:cd14892 477 YHQTHLDKHPHYAKPRF----ECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK----------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 635 ggpkkggkkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFP 714
Cdd:cd14892 536 --------------------FRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFP 595
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305632842 715 SRILYADFKQRYKVL-------NASAIPEGQFIDSKKASEKLLASIDIDHTQykFGHTKVFFK 770
Cdd:cd14892 596 IRRQFEEFYEKFWPLarnkagvAASPDACDATTARKKCEEIVARALERENFQ--LGRTKVFLR 656
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
102-770 |
3.03e-147 |
|
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: 470.71 E-value: 3.03e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKK-RQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 181 SGAGKTVNTKRVIQYFATIavtgekkkeevtSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14897 83 SGAGKTESTKYMIKHLMKL------------SPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEEL-----MAT 335
Cdd:cd14897 151 LLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELeyyrqMFH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 336 DSaIDIL---GFTNEEKVSIYKLTGAVMHYGNLKFkqkqrEEQAEPDGTEVADK-----AAYLQSLNSADLLKALCYPRV 407
Cdd:cd14897 230 DL-TNIMkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVN 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 408 KVGNEFVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYF-----IGVLDIAGFEIFDFNSLEQLCIN 482
Cdd:cd14897 304 TIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCIN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 483 FTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDqHLG 561
Cdd:cd14897 384 LSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKLNK-YCG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 562 KSANFQKPKvvKGKAEahFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFsgtqtaeaegggpkkgg 641
Cdd:cd14897 462 ESPRYVASP--GNRVA--FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF----------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 642 kkkgssfqtvSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 721
Cdd:cd14897 521 ----------TSYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYED 590
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 305632842 722 FKQRYKVL-----NASAIPEGQFIDSKKAsekllASIDidhtQYKFGHTKVFFK 770
Cdd:cd14897 591 FVKRYKEIcdfsnKVRSDDLGKCQKILKT-----AGIK----GYQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
102-729 |
2.62e-146 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 467.86 E-value: 2.62e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAY-----------RGKKRQEAPPHIFSISDNAYQFM--- 166
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 167 -LTDRENQSILITGESGAGKTVNTKRVIQYFATiaVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSS 245
Cdd:cd14900 83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQ--AGDNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 246 RFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYqitsnkkpeliEMLLittnpydypfvSQGEISVAS 325
Cdd:cd14900 161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFY-----------EMAI-----------GASEAARKR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 326 iDDQEELMAtdsAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVA-------DKAAYLQSLNSADL 398
Cdd:cd14900 219 -DMYRRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATKL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 399 LKALCYPRVKVGNEFVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQL-----DTKQPRQYFIGVLDIAGFEIFDF 473
Cdd:cd14900 295 EKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEVFPK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 474 NSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFK 552
Cdd:cd14900 375 NSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 553 NKLYdQHLGKSANFQKPKVVKGKaeAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQksamktlahlfSGTQtaea 632
Cdd:cd14900 454 SKLY-RACGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFV-----------YGLQ---- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 633 egggpkkggkkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKG 712
Cdd:cd14900 516 ----------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAG 573
|
650
....*....|....*..
gi 305632842 713 FPSRILYADFKQRYKVL 729
Cdd:cd14900 574 FPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
102-770 |
1.38e-142 |
|
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: 458.73 E-value: 1.38e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRG--KKRQEA------PPHIFSISDNAYQFMLTDREN 172
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEqiIQNGEYfdikkePPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 173 QSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVT-------SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSS 245
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTltssiraTSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 246 RFGKFIRIHFG-TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYP--FVSQGEIS 322
Cdd:cd14907 163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSGDRydYLKKSNCY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 323 -VASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQ--REEQAEPDGTEVADKAAYLQSLNSADLL 399
Cdd:cd14907 243 eVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEELK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 400 KALCYPRVKVGNEFVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQL--------DTKQPRQYFIGVLDIAGFEIF 471
Cdd:cd14907 323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 472 DFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF--IDFgMDLAACIELIEK-PMGIFSILEEECMFPKATD 548
Cdd:cd14907 403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 549 TSFKNKLYDQHlgksANFQKPKVVKGKAEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQ 628
Cdd:cd14907 482 EKLLNKIKKQH----KNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGED 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 629 TaeaEGGGPKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRI 708
Cdd:cd14907 558 G---SQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRV 634
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 305632842 709 CRKGFPSRILYADFKQRYKVLNasaipegqfidskkasekllasididhTQYKFGHTKVFFK 770
Cdd:cd14907 635 RKQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
100-770 |
1.70e-139 |
|
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: 449.78 E-value: 1.70e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 179 GESGAGKTVNTKRVIQYFATIAvtGEKKKEEVtsgkmqgtleDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVA--GGRKDKTI----------AKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSN-KKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDS 337
Cdd:cd14904 149 GKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 338 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVAdKAAYLQSLNSADLLKALCYPRVKVGNEFVTKG 417
Cdd:cd14904 229 SLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLS-QVAKMLGLPTTRIEEALCNRSVVTRNESVTVP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 418 QTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQY-FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14904 308 LAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 497 FVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQH--LGKSANFQKPKVVKg 574
Cdd:cd14904 388 FKTVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVKR- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 575 kaeAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFsgtQTAEAEGGGPKKGGKKKGSSFQTVSAL 654
Cdd:cd14904 466 ---TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELF---GSSEAPSETKEGKSGKGTKAPKSLGSQ 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 655 FRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAI 734
Cdd:cd14904 540 FKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSM 619
|
650 660 670
....*....|....*....|....*....|....*..
gi 305632842 735 PEGqfiDSKKASEKLLASIDIDHT-QYKFGHTKVFFK 770
Cdd:cd14904 620 HSK---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
102-770 |
1.05e-138 |
|
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: 447.82 E-value: 1.05e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFML----TDRENQSILI 177
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 178 TGESGAGKTVNTKRVIQYFAtiavtgekkkeEVTSGKMQgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgT 257
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIM-----------ELCRGNSQ--LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-R 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 258 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQI---TSNKKPELIEMLlittNPYDYPFVSQGEisvasidDQEELMA 334
Cdd:cd14889 149 NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMfagISAEDRENYGLL----DPGKYRYLNNGA-------GCKREVQ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 335 T--------DSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREE-QAEPDGTEVADKAAYLQSLNSADLLKALCYP 405
Cdd:cd14889 218 YwkkkydevCNAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 406 RVKVGNEFVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLdtkQPRQYF------IGVLDIAGFEIFDFNSLEQL 479
Cdd:cd14889 298 VTFTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL---APKDDSsvelreIGILDIFGFENFAVNRFEQA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 480 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLyDQH 559
Cdd:cd14889 375 CINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFPQATDESFVDKL-NIH 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 560 LGKSANFqkpKVVKGKAEAhFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAEAEGGGPKK 639
Cdd:cd14889 454 FKGNSYY---GKSRSKSPK-FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAK 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 640 GGKKKGSSF-----QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFP 714
Cdd:cd14889 530 LPQAGSDNFnstrkQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFS 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 305632842 715 SRILYADFKQRYKVLnasaIPEGQFIDSKKASEKLLASIDIdhTQYKFGHTKVFFK 770
Cdd:cd14889 610 WRPSFAEFAERYKIL----LCEPALPGTKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
24-829 |
2.09e-132 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 435.61 E-value: 2.09e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 24 RIEAQNRPFDAKTSVFV-------------AEPKESFVKGTIQ-SREGGKVTVK---TEGGATLTVKDDQVF----PMNP 82
Cdd:PTZ00014 16 RRNSNVEAFDKSGNVLKgfyvwtdkapavkEDPDLMFAKCLVLpGSTGEKLTLKqidPPTNSTFEVKPEHAFnansQIDP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 83 PKYDkieDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYR-GKKRQEAPPHIFSISDN 161
Cdd:PTZ00014 96 MTYG---DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRdAKDSDKLPPHVFTTARR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 162 AYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAvtgekkkeevtSGKMQGTLEDQIISANPLLEAFGNAKTVRN 241
Cdd:PTZ00014 173 ALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSK-----------SGNMDLKIQNAIMAANPVLEAFGNAKTIRN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 242 DNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEI 321
Cdd:PTZ00014 242 NNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKL-KSLEEYKYINPKCL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 322 SVASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-----PDGTEVADKAAYLQSLNSA 396
Cdd:PTZ00014 321 DVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDaaaisDESLEVFNEACELLFLDYE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 397 DLLKALCYPRVKVGNEFVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSL 476
Cdd:PTZ00014 401 SLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 477 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGI-----EWTfidfgmDLAACIELI-EKPMGIFSILEEECMFPKATDTS 550
Cdd:PTZ00014 481 EQLFINITNEMLQKNFVDIVFERESKLYKDEGIsteelEYT------SNESVIDLLcGKGKSVLSILEDQCLAPGGTDEK 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 551 FKNKLYDQhLGKSANFQKPKVVKGKaeaHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGtqtA 630
Cdd:PTZ00014 555 FVSSCNTN-LKNNPKYKPAKVDSNK---NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEG---V 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 631 EAEGGGPKKGgkkkgssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICR 710
Cdd:PTZ00014 628 EVEKGKLAKG--------QLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQ 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 711 KGFPSRILYADFKQRYKVLNAsAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFKAGLLGLLEEMRDDKLAQ--- 787
Cdd:PTZ00014 700 LGFSYRRTFAEFLSQFKYLDL-AVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAAwep 778
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 305632842 788 LITRTQArcrgFLARVEYQRMVERR-EAIFCIQYNIRAFMNVK 829
Cdd:PTZ00014 779 LVSVLEA----LILKIKKKRKVRKNiKSLVRIQAHLRRHLVIA 817
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
100-770 |
6.75e-132 |
|
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: 429.71 E-value: 6.75e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYR--GKKRQ---EAP----PHIFSISDNAYQFMLTD- 169
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 170 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELG-KLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 250 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQI------TSNKKPELIEMLLITTN-PYDYPFVSQGEI- 321
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLlrggdeEEHEKYEFHDGITGGLQlPNEFHYTGQGGAp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 322 SVASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQRE---EQAEPDGTEVADKAAYLQSLNSADL 398
Cdd:cd14908 240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDgaaEIAEEGNEKCLARVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 399 LKALCYPRVKVGNEFVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQL--DTKQPRQYFIGVLDIAGFEIFDFNSL 476
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 477 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFP-KATDTSFKNK 554
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 555 LYDQHL-------GKSANFQKPKVVKGKaeAHFSLIHYAGVVDYNI-TGWLEKNKDPLNETVVGLYQksamktlahlfSG 626
Cdd:cd14908 479 LYETYLpeknqthSENTRFEATSIQKTK--LIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFE-----------SG 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 627 TQtaeaegggpkkggkkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGI 706
Cdd:cd14908 546 QQ--------------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAV 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 707 RICRKGFPSRILYADFKQRYKVLnASAIPE----------------GQFIDSKKA----SEKLLASIDIDHTQYKFGHTK 766
Cdd:cd14908 600 RVARSGYPVRLPHKDFFKRYRML-LPLIPEvvlswsmerldpqklcVKKMCKDLVkgvlSPAMVSMKNIPEDTMQLGKSK 678
|
....
gi 305632842 767 VFFK 770
Cdd:cd14908 679 VFMR 682
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
100-770 |
2.56e-131 |
|
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: 426.38 E-value: 2.56e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAA--WMIYTYSGLFCVTVNPYKWLPvyNPEVvTAYRGKKRQEAPPHIFSISDNAYQFMLTDRE---NQS 174
Cdd:cd14891 1 AGILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLP--EPDK-SDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 175 ILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQG------TLEDQIISANPLLEAFGNAKTVRNDNSSRFG 248
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 249 KFIRIHFGTTG-KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQ-GEISVASI 326
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLL-LSPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 327 DDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREE----QAEPDGTEVADKAAYLQSLNSADLLKAL 402
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 403 CYPRVKVGNEFVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFD-FNSLEQLCI 481
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 482 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHl 560
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 561 GKSANFQKPKvVKGKAEAhFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMktlahlfsgtqtaeaegggpkkg 640
Cdd:cd14891 475 KRHPCFPRPH-PKDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASSAK----------------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 641 gkkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYA 720
Cdd:cd14891 530 --------------FSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYA 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 305632842 721 DFKQRYKVLNASAI------PEGQFIdskkasEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14891 596 ELVDVYKPVLPPSVtrlfaeNDRTLT------QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
100-727 |
9.50e-130 |
|
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: 424.69 E-value: 9.50e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP---------VYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFML-TD 169
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdlysesqlnAYKASMTSTSPVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 170 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTledQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAVEIGK---RILQTNPILESFGNAQTIRNDNSSRFGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 250 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEmLLITTNPYDYPFVSQGEISVA----- 324
Cdd:cd14902 158 FIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLD-LLGLQKGGKYELLNSYGPSFArkrav 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 325 SIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKqkqrEEQAEPDGTEVA-------DKAAYLQSLNSAD 397
Cdd:cd14902 237 ADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFT----AENGQEDATAVTaasrfhlAKCAELMGVDVDK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 398 LLKALCYPRVKVGNEFVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-------TKQPRQYF--IGVLDIAGF 468
Cdd:cd14902 313 LETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsISDEDEELatIGILDIFGF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 469 EIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKAT 547
Cdd:cd14902 393 ESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 548 DTSFKNKLYDQHLGksanfqkpkvvkgkaEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFS-- 625
Cdd:cd14902 472 NQALSTKFYRYHGG---------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGAde 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 626 --GTQTAEAEGGGPKKGGKKKGSSfqtVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVL 703
Cdd:cd14902 537 nrDSPGADNGAAGRRRYSMLRAPS---VSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVL 613
|
650 660
....*....|....*....|....
gi 305632842 704 EGIRICRKGFPSRILYADFKQRYK 727
Cdd:cd14902 614 EAVRIARHGYSVRLAHASFIELFS 637
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-770 |
8.01e-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: 410.50 E-value: 8.01e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNpevVTAYRGK--KRQEAPPHIFSISDNAYQFMLT-------D 169
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 170 RENQSILITGESGAGKTVNTKRVIQYfatIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNY---LAESSKHTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 250 FIRIHFG-----TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPE-LIEMLLITTNPYDYPFVSQGEISV 323
Cdd:cd14895 155 FVRMFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDmKLELQLELLSAQEFQYISGGQCYQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 324 AS--IDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVA----------------- 384
Cdd:cd14895 235 RNdgVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqqh 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 385 -DKAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQY----- 458
Cdd:cd14895 315 lDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNpnkaa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 459 ------FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPM 531
Cdd:cd14895 395 nkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLEqRPS 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 532 GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKvvKGKAEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGL 611
Cdd:cd14895 474 GIFSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 612 YQKSAMKTLAHLFSGTQTAE-AEGGGPKKGGKKKGSSFQTV--SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAM 688
Cdd:cd14895 551 LGKTSDAHLRELFEFFKASEsAELSLGQPKLRRRSSVLSSVgiGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQF 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 689 EHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASaipegQFIDSKKASEkLLASIDIDHTQykFGHTKVF 768
Cdd:cd14895 631 DMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAA-----KNASDATASA-LIETLKVDHAE--LGKTRVF 702
|
..
gi 305632842 769 FK 770
Cdd:cd14895 703 LR 704
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
100-770 |
6.26e-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: 403.21 E-value: 6.26e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRG-KKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 179 GESGAGKTVNTKRVIQYFATIAvtgekkkeevtSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd14876 81 GESGAGKTEATKQIMRYFASAK-----------SGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQGEISVASIDDQEELMATDSA 338
Cdd:cd14876 150 GGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLG-LKEYKFLNPKCLDVPGIDDVADFEEVLES 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 339 IDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQ-----AEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEF 413
Cdd:cd14876 229 LKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVddaaaISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 414 VTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14876 309 IEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 494 HHMFVLEQEEYKKEGI-----EWTfidfgmDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLYDQhLGKSANFQ 567
Cdd:cd14876 389 DIVFERESKLYKDEGIptaelEYT------SNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSK-LKSNGKFK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 568 KPKVvkgKAEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAEAEGGGPkkggkkkgss 647
Cdd:cd14876 462 PAKV---DSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKGKIAKG---------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 648 fQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 727
Cdd:cd14876 529 -SLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFK 607
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 305632842 728 VLNAsAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14876 608 FLDL-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
100-770 |
4.46e-120 |
|
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: 394.92 E-value: 4.46e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 180 ESGAGKTVNTKRVIQYFATIavtgEKKKEEVTSGKMQGTLedqiisanPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTG 259
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL----YQDQTEDRLRQPEDVL--------PILESFGHAKTILNANASRFGQVLRLHL-QHG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEI-SVASIDDQEELMATDSA 338
Cdd:cd14896 148 VIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYLNQGGAcRLQGKEDAQDFEGLLKA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 339 IDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQ---AEPDGTEVADKAAYLQSlnSADLLKALCYPRVKVGN-EFV 414
Cdd:cd14896 227 LQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevaAVSSWAEIHTAARLLQV--PPERLEGAVTHRVTETPyGRV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 415 TKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYF--IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 492
Cdd:cd14896 305 SRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 493 NHHMFVLEQEEYKKEGIEWTFIDfGMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKV 571
Cdd:cd14896 385 SQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 572 vkgkAEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFsgtQTAEAEGGGPKKGGkkkgssfqTV 651
Cdd:cd14896 463 ----PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLF---QEAEPQYGLGQGKP--------TL 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 652 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 731
Cdd:cd14896 528 ASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGS 607
|
650 660 670
....*....|....*....|....*....|....*....
gi 305632842 732 SAIPEgqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14896 608 ERQEA--LSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
102-729 |
7.03e-114 |
|
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: 377.65 E-value: 7.03e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKR-QEAPPHIFSISDNAYQFMLTDRE--NQSILI 177
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 178 TGESGAGKTVNTKRVIQYFATIAVTgekkKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 257
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAAS----PTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 258 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSN-KKPELIEMLLitTNPYDYPFVSQGEISVasidDQEELMATD 336
Cdd:cd14880 159 AQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGaSADERLQWHL--PEGAAFSWLPNPERNL----EEDCFEVTR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 337 SAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQA---EPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGnef 413
Cdd:cd14880 233 EAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAG--- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 414 vtKGQTV-------EQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPR-QYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:cd14880 310 --KQQQVfkkpcsrAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYAN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 486 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSA 564
Cdd:cd14880 388 EKLQQHFVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 565 NFQKPKVVKgkaEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSgtqtAEAEGGGPKKGGKKK 644
Cdd:cd14880 467 CLGHNKLSR---EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFP----ANPEEKTQEEPSGQS 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 645 GSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQ 724
Cdd:cd14880 540 RAPVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVE 619
|
....*
gi 305632842 725 RYKVL 729
Cdd:cd14880 620 RYKLL 624
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
102-732 |
1.17e-109 |
|
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: 367.38 E-value: 1.17e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKR-QEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 180 ESGAGKTVNTKRVIQYFatIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-GTT 258
Cdd:cd14906 83 ESGSGKTEASKTILQYL--INTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFrSSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 259 GKLASADIETYLLEKSRVTFQL-KAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQ-------- 329
Cdd:cd14906 161 GKIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFKSQssnknsnh 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 330 -------EELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQ---REEQAEPDGTEVADKAAYLQSLNSADLL 399
Cdd:cd14906 241 nnktesiESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 400 KALCYPRVKVGNE--FVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARIN----QQLDTKQPRQY-------FIGVLDIA 466
Cdd:cd14906 321 QALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINrkfnQNTQSNDLAGGsnkknnlFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 467 GFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPK 545
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 546 ATDTSFKNKLYDQHLGKSANFQKPkvvkgKAEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFS 625
Cdd:cd14906 480 GSEQSLLEKYNKQYHNTNQYYQRT-----LAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 626 GTQTAEAegggpkkGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEG 705
Cdd:cd14906 555 QQITSTT-------NTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNT 627
|
650 660
....*....|....*....|....*..
gi 305632842 706 IRICRKGFPSRILYADFKQRYKVLNAS 732
Cdd:cd14906 628 IKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
101-727 |
1.63e-107 |
|
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: 361.34 E-value: 1.63e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAY----------RGKKRQEAPPHIFSISDNAYQFMLTD 169
Cdd:cd14899 2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 170 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKM-----QGTLEDQIISANPLLEAFGNAKTVRNDNS 244
Cdd:cd14899 82 GRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISPpaspsRTTIEEQVLQSNPILEAFGNARTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 245 SRFGKFIRIHF-GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNK----KPELIEMLLITTNPYDYPFVSQG 319
Cdd:cd14899 162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 320 EISVA--SIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQ--KQREEQAEPDGTEVA----------D 385
Cdd:cd14899 242 LCSKRrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhfT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 386 KAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQL--------------- 450
Cdd:cd14899 322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesdv 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 451 DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlAACIELIE-K 529
Cdd:cd14899 402 DDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 530 PMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVV 609
Cdd:cd14899 481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 610 GLYQKSAMKTLAHLFSGTQTAEAEGGGPKKGGKKKGSSFQ-------TVSALFRENLNKLMTNLRSTHPHFVRCIIPNET 682
Cdd:cd14899 561 QLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAksaiaavSVGTQFKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 305632842 683 KTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 727
Cdd:cd14899 641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
102-770 |
2.34e-105 |
|
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: 353.35 E-value: 2.34e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 102 VLYNLKERYAAWMI-YTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEA-PPHIFSISDNAY-QFMLTDRENQSILIT 178
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFnAIFVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 179 GESGAGKTVNTKRVIQYFAtiavtgeKKKEEVTSGKMQGTLEDQIIS----ANPLLEAFGNAKTVRNDNSSRFGKFIRIH 254
Cdd:cd14875 83 GESGSGKTENAKMLIAYLG-------QLSYMHSSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 255 F-GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISV------ASID 327
Cdd:cd14875 156 FdPTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdgKTLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 328 DQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQsLNSADLLKalCYpRV 407
Cdd:cd14875 236 DAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFLTACRLLQ-LDPAKLRE--CF-LV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 408 KVGNEFVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQ----QLDTKQPRqyFIGVLDIAGFEIFDFNSLEQLCINF 483
Cdd:cd14875 312 KSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNAsitpQGDCSGCK--YIGLLDIFGFENFTRNSFEQLCINY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 484 TNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLGK 562
Cdd:cd14875 390 ANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 563 SANFQKPkvvKGKAEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSgTQTAEAEGGgpkkggk 642
Cdd:cd14875 469 SPYFVLP---KSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLS-TEKGLARRK------- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 643 kkgssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADF 722
Cdd:cd14875 538 ------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQF 611
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 305632842 723 -KQRYKVLNASAIPEGQFIDSKKASEKLLAS----IDIDHTQYKFGHTKVFFK 770
Cdd:cd14875 612 cRYFYLIMPRSTASLFKQEKYSEAAKDFLAYyqrlYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
106-770 |
3.80e-104 |
|
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: 349.19 E-value: 3.80e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKRQ-----EAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEVtsgkmqgtledqIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSSTDVQSL------------ILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYdYPFVSQGEISVA-SIDDQEELMATDSA 338
Cdd:cd14886 155 GLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLES-YNFLNASKCYDApGIDDQKEFAPVRSQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 339 IDILgFTNEEKVSIYKLTGAVMHYGNLKFKQKQR---EEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVT 415
Cdd:cd14886 234 LEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETII 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 416 KGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 495
Cdd:cd14886 313 SPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 496 MFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKP-MGIFSILEEECMFPKATDTSFKNKLyDQHLgKSANFqkpkvVKG 574
Cdd:cd14886 393 VFKSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSF-----IPG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 575 K-AEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAEAEGGGpkkggkkkgssfQTVSA 653
Cdd:cd14886 465 KgSQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMKG------------KFLGS 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 654 LFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL---N 730
Cdd:cd14886 533 TFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishN 612
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 305632842 731 ASAIPEGQfiDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14886 613 SSSQNAGE--DLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
102-770 |
3.85e-101 |
|
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: 341.60 E-value: 3.85e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd01386 3 VLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 182 GAGKTVNTKRVIQYFATIAVTGEKKkeeVTSGKMQgtledqiiSANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd01386 83 GSGKTTNCRHILEYLVTAAGSVGGV---LSVEKLN--------AALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFvsqGEISVASIDD----QEELMATDS 337
Cdd:cd01386 152 ASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSF---GIVPLQKPEDkqkaAAAFSKLQA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 338 AIDILGFTNEEKVSIYKLTGAVMHYGN---LKFKQKQREEQAEPdgtEVADKAAYLQSLNSADLLKALCYPRVKVGNEFV 414
Cdd:cd01386 229 AMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 415 TKGQTVEQVTN------------AVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SL 476
Cdd:cd01386 306 TTSSGQESPARsssggpkltgveALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqrgaTF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 477 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK---------------PMGIFSILEEEC 541
Cdd:cd01386 386 EDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGLLWLLDEEA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 542 MFPKATDTSFKNKLYdQHLGKSANFQKPKVVKgKAEA--HFSLIHYAGV--VDYNITGWLEKNK-DPLNETVVGLYQKSA 616
Cdd:cd01386 466 LYPGSSDDTFLERLF-SHYGDKEGGKGHSLLR-RSEGplQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQESQ 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 617 MKTLAHLFSGtqtaeaegggpkkggkkkgssfqtVSALFRENLNKLMTNLRSTHPHFVRCIIPN------ETKTPGAMEH 690
Cdd:cd01386 544 KETAAVKRKS------------------------PCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkdERSTSSPAAG 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 691 ELVLH------QLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL----NASAIPEGQFIDSKKASEKLLASIDIDHTQY 760
Cdd:cd01386 600 DELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLapplTKKLGLNSEVADERKAVEELLEELDLEKSSY 679
|
730
....*....|
gi 305632842 761 KFGHTKVFFK 770
Cdd:cd01386 680 RIGLSQVFFR 689
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
101-770 |
6.31e-93 |
|
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: 316.76 E-value: 6.31e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYR---GKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 177
Cdd:cd14878 2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 178 TGESGAGKTVNTKRVIQYFATiavtgekkkeevTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 257
Cdd:cd14878 82 SGERGSGKTEASKQIMKHLTC------------RASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 258 TGK-LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITtNPYDYPFVSQGE----ISVASIDDQEEL 332
Cdd:cd14878 150 RKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLN-NLCAHRYLNQTMredvSTAERSLNREKL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 333 MATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNE 412
Cdd:cd14878 229 AVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 413 FVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARIN----QQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 488
Cdd:cd14878 309 MIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNcclqSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 489 QQFFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQ 567
Cdd:cd14878 389 HHYINEVLFLQEQTECVQEGVTMeTAYSPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLESSNTNAV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 568 KPKVVKGKAE-------AHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFsgtqtaeaegggpkkg 640
Cdd:cd14878 469 YSPMKDGNGNvalkdqgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLF---------------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 641 gkkkGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYA 720
Cdd:cd14878 533 ----QSKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFS 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 305632842 721 DFKQRYKVLnASAIPEGQfidsKKASEKLLASIDIDHTQ---YKFGHTKVFFK 770
Cdd:cd14878 609 DFLSRYKPL-ADTLLGEK----KKQSAEERCRLVLQQCKlqgWQMGVRKVFLK 656
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
101-733 |
9.18e-93 |
|
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: 313.76 E-value: 9.18e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYkwlpvynpEVVTAYRGKKRQE-----APPHIFSISDNAYQFMLTdRENQSI 175
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPY--------ETIYGAGAMKAYLknyshVEPHVYDVAEASVQDLLV-HGNQTI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 176 LITGESGAGKTVNTKRVIQYFatiavtgekkkeeVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 255
Cdd:cd14898 73 VISGESGSGKTENAKLVIKYL-------------VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 256 gtTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpeliemLLITTNPYDYPFVSQGEISVasIDDQEELMAT 335
Cdd:cd14898 140 --DGKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESI--VQLSEKYKMT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 336 DSAIDILGFTNEEkvSIYKLTGAVMHYGNLKFKQkqreeqaepDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVT 415
Cdd:cd14898 210 CSAMKSLGIANFK--SIEDCLLGILYLGSIQFVN---------DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 416 KGQTVE------QVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQyfIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 489
Cdd:cd14898 279 KGETIEvfntlkQARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQ 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 490 QFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKAT--DTSFKNKLYDQHLgksanfq 567
Cdd:cd14898 357 NDFIKKMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNvkNLLVKIKKYLNGF------- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 568 kpkvVKGKAEAHFSLIHYAGVVDYNITGWLEKNKdplnetvvglyQKSAMKTLAHLFSGTQtaeaegggpkkggkkkgSS 647
Cdd:cd14898 429 ----INTKARDKIKVSHYAGDVEYDLRDFLDKNR-----------EKGQLLIFKNLLINDE-----------------GS 476
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 648 FQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 727
Cdd:cd14898 477 KEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYR 556
|
....*.
gi 305632842 728 VLNASA 733
Cdd:cd14898 557 ILGITL 562
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
102-770 |
8.63e-89 |
|
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: 304.25 E-value: 8.63e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYnpevVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 182 GAGKTVNTKRVIQYFatiaVTGEKKKEEVTSgkmqgTLEDqiisANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14937 79 GSGKTEASKLVIKYY----LSGVKEDNEISN-----TLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPyDYPFVSQGEISVASIDDQEELMATDSAIDI 341
Cdd:cd14937 146 VSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDFGNLMISFDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 342 LGFTNEEKVSIYKLTGAVMhYGNLKFKQ-----KQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEFVTK 416
Cdd:cd14937 225 MNMHDMKDDLFLTLSGLLL-LGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 417 GQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14937 304 PLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 497 FVLEQEEYKKEGIEWTFIDFGMDlAACIELIEKPMGIFSILEEECMFPKATDTSfknkLYDQHLGKSANFQKPKVVKGKA 576
Cdd:cd14937 384 YEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDES----IVSVYTNKFSKHEKYASTKKDI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 577 EAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTAEAEGGGpkkggkkkgssfQTVSALFR 656
Cdd:cd14937 459 NKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRK------------NLITFKYL 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 657 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRIcRKGFPSRILYADFKQRYKVLNASAIPE 736
Cdd:cd14937 527 KNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKD 605
|
650 660 670
....*....|....*....|....*....|....
gi 305632842 737 GQFIDSKKASEKLLASIDIDhtQYKFGHTKVFFK 770
Cdd:cd14937 606 SSLTDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
100-770 |
3.72e-88 |
|
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: 305.03 E-value: 3.72e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAA--------WMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRE 171
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 172 NQSILITGESGAGKTVNTKRVIQYFAtiAVTGEKKkeevtsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 251
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLA--AVSDRRH------GADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKML 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 252 RIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITtnpYDYPFVSqgeisvasidDQEE 331
Cdd:cd14887 153 LLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAG---EGDPEST----------DLRR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 332 LMATDSAIDILGFTNEEkvsIYKLTGAVMHYGNLKFKQKQREEQAEPDGT--------EVADK---AAYLQSLNS----- 395
Cdd:cd14887 220 ITAAMKTVGIGGGEQAD---IFKLLAAILHLGNVEFTTDQEPETSKKRKLtsvsvgceETAADrshSSEVKCLSSglkvt 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 396 -------ADLLKALCYPRVKVGNEFV------------TKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPR 456
Cdd:cd14887 297 easrkhlKTVARLLGLPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 457 QY--------------FIGVLDIAGFEIF---DFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFI----D 515
Cdd:cd14887 377 SEsdsdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsafP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 516 FGMDLAAC--------IELIEKP--------------MGIFSILEEE-CMFPKATDTSFKNKLYDQHLGK----SANFQK 568
Cdd:cd14887 457 FSFPLASTltsspsstSPFSPTPsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniinSAKYKN 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 569 PKVVKGKAEAHFSLIHYAGVVDYNITGWLEKNKDPLNEtvvglyqksamkTLAHLFSGTQTAEAEGGGPKKGGKKKGSS- 647
Cdd:cd14887 537 ITPALSRENLEFTVSHFACDVTYDARDFCRANREATSD------------ELERLFLACSTYTRLVGSKKNSGVRAISSr 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 648 FQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 727
Cdd:cd14887 605 RSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYE 684
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 305632842 728 VLNASAIPEgqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 770
Cdd:cd14887 685 TKLPMALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
106-769 |
6.91e-85 |
|
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: 292.92 E-value: 6.91e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 106 LKERYAAWMIYTY---SGLfcVTVNPYKWLPVYNPEVVTAYR-------GKKRQEAPPHIFSISDNAYQFMLTDRENQSI 175
Cdd:cd14879 10 LASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRRRSEDQAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 176 LITGESGAGKTVNTKRVIQYFATIAVTGEKkkeevtsgkmqGT-LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 254
Cdd:cd14879 88 VFLGETGSGKSESRRLLLRQLLRLSSHSKK-----------GTkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 255 FGTTGKLASADIETYLLEKSRVTfQLKA-ERSYHIFYQITSNKKPELIEMLLITTNP-YDYPFVSQG--EISVASIDDQE 330
Cdd:cd14879 157 FNERGRLIGAKVLDYRLERSRVA-SVPTgERNFHVFYYLLAGASPEERQHLGLDDPSdYALLASYGChpLPLGPGSDDAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 331 ---ELMAtdsAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQ--REEQAEPDGTEVADKAAYLQSLNSADLLKALCYP 405
Cdd:cd14879 236 gfqELKT---ALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTYK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 406 RVKVGNEFVTkgqtveqV-TNAVGA------LAKAVYEKMFLWMVARINQQL-DTKQPRQYFIGVLDIAGFEIFD---FN 474
Cdd:cd14879 313 TKLVRKELCT-------VfLDPEGAaaqrdeLARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRSstgGN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 475 SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEEC-MFPKATDTSFK 552
Cdd:cd14879 386 SLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKTDEQML 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 553 NKLYDQHLGKSANFQKPKVVKGKAEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVglyqksamktlaHLFSGTQTaea 632
Cdd:cd14879 465 EALRKRFGNHSSFIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFV------------NLLRGATQ--- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 633 egggpkkggkkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKG 712
Cdd:cd14879 530 ----------------------LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVE 587
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 305632842 713 FPSRILYADFKQRYKvlnasaiPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFF 769
Cdd:cd14879 588 YVVSLEHAEFCERYK-------STLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
100-718 |
6.49e-78 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 273.71 E-value: 6.49e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKRQEA-------PPHIFSISDNAYQFMLTDRE 171
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 172 NQSILITGESGAGKTVNTKRVIQYFATIavtgekkkeevtSGKMQGT-LEDQIISANPLLEAFGNAKTVRNDNSSRFGKF 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI------------QTDSQMTeRIDKLIYINNILESMSNATTIKNNNSSRCGRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 251 IRIHFGT---------TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGE- 320
Cdd:cd14884 149 NLLIFEEventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDEs 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 321 -----------ISVASIDDQEELMATDSA-----IDILGFTNEEKVSI---YKLTGAVMHYGNLKFKQkqreeqaepdgt 381
Cdd:cd14884 229 hqkrsvkgtlrLGSDSLDPSEEEKAKDEKnfvalLHGLHYIKYDERQInefFDIIAGILHLGNRAYKA------------ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 382 evadkAAYLQSLNSADLLKALCYPRVKVGNEFVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARIN---------QQLDT 452
Cdd:cd14884 297 -----AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrnvlkckekDESDN 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 453 KQPRQY---FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDfgmdLAACIELIEK 529
Cdd:cd14884 372 EDIYSIneaIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDV----APSYSDTLIF 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 530 PMGIFSILEEECMFP----KATDTSFKNKLYD----QHLGK--SANFQKPKVVKGKAEAH------FSLIHYAGVVDYNI 593
Cdd:cd14884 448 IAKIFRRLDDITKLKnqgqKKTDDHFFRYLLNnerqQQLEGkvSYGFVLNHDADGTAKKQnikkniFFIRHYAGLVTYRI 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 594 TGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTaeaegggpkkggkkkgSSFQTVSALFRENLNKLMTNLRSTHPHF 673
Cdd:cd14884 528 NNWIDKNSDKIETSIETLISCSSNRFLREANNGGNK----------------GNFLSVSKKYIKELDNLFTQLQSTDMYY 591
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 305632842 674 VRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 718
Cdd:cd14884 592 IRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
101-752 |
1.52e-68 |
|
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: 244.64 E-value: 1.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPvyNPEVVTAYRGKKRQeapPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 181 SGAGKTVNTKRVI-QYFatiavtgekkkeEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTG 259
Cdd:cd14881 77 SGSGKTYASMLLLrQLF------------DVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKP-ELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSA 338
Cdd:cd14881 144 ALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQeERVKLHLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKAC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 339 IDILG--FTNeekvsIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLqSLNSADLLKALcYPRVKVgnefvTK 416
Cdd:cd14881 224 LGILGipFLD-----VVRVLAAVLLLGNVQFIDGGGLEVDVKGETELKSVAALL-GVSGAALFRGL-TTRTHN-----AR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 417 GQTVEQVTNA------VGALAKAVYEKMFLWMVARINQQLD-----TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:cd14881 292 GQLVKSVCDAnmsnmtRDALAKALYCRTVATIVRRANSLKRlgstlGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 486 EKLQQFFNHHMFVLEQEEYKKEGIEwTFIDFG-MDLAACIELIEK-PMGIFSILEEECMfPKATDTSFKNKLYDQHLGkS 563
Cdd:cd14881 372 ETMQHFYNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQ-N 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 564 ANFQKPKVVKGKAeahFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKsamktlahlfsgtQTAEAegggpkkggkk 643
Cdd:cd14881 449 PRLFEAKPQDDRM---FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYK-------------QNCNF----------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 644 kgsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFK 723
Cdd:cd14881 502 ---GFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFN 578
|
650 660
....*....|....*....|....*....
gi 305632842 724 QRYKVLnASAIPEGQFIDSKKASEKLLAS 752
Cdd:cd14881 579 ARYRLL-APFRLLRRVEEKALEDCALILQ 606
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
102-770 |
8.50e-67 |
|
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: 239.64 E-value: 8.50e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 182 GAGKTVNTKRVIQYFATIavtgekkkeevtsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14882 83 YSGKTTNARLLIKHLCYL-------------GDGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQI--TSNKKPELIEMLLITTNPYDY----PFVSQGEISVASIDDQEELMAT 335
Cdd:cd14882 150 SGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFydFIEAQNRLKEYNLKAGRNYRYlripPEVPPSKLKYRRDDPEGNVERY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 336 DSAIDIL---GFTNEEKVSIYKLTGAVMHYGNLKFKQKQREeqAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNE 412
Cdd:cd14882 230 KEFEEILkdlDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 413 FVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTkqPR-----QYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 487
Cdd:cd14882 308 AERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSF--PRavfgdKYSISIHDMFGFECFHRNRLEQLMVNTLNEQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 488 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEecmfpKATDTSFKNKLYDQHLGKSANFQ 567
Cdd:cd14882 386 MQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD-----ASRSCQDQNYIMDRIKEKHSQFV 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 568 KPkvvkgkAEAH-FSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSGTQTaeaegggpkkggkkkgS 646
Cdd:cd14882 461 KK------HSAHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQV----------------R 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 647 SFQTVSALFR----ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADF 722
Cdd:cd14882 519 NMRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEF 598
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 305632842 723 KQRYKVLnasAIPEGQFIDSKKASEKLLAsIDIDHTQYKFGHTKVFFK 770
Cdd:cd14882 599 LRRYQFL---AFDFDETVEMTKDNCRLLL-IRLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
106-713 |
2.56e-66 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 239.22 E-value: 2.56e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYrgKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 184
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 185 KTVNTKRVIQYFATIAVTGEKkkeevtsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASA 264
Cdd:cd14905 85 KSENTKIIIQYLLTTDLSRSK------------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 265 DIETYLLEKSRVTFQLKAERSYHIFYQ----ITSNKKPeliEMLLITTNPYDYpFVSQGEISVASIDDQEELMATDSAID 340
Cdd:cd14905 153 KLYSYFLDENRVTYQNKGERNFHIFYQflkgITDEEKA---AYQLGDINSYHY-LNQGGSISVESIDDNRVFDRLKMSFV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 341 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREeqaepdgTEVADKaAYLQSLNsadllKALCYPRVKVGNEFVT-KGQT 419
Cdd:cd14905 229 FFDFPSEKIDLIFKTLSFIIILGNVTFFQKNGK-------TEVKDR-TLIESLS-----HNITFDSTKLENILISdRSMP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 420 VEQVTNAVGALAKAVYEKMFLWMVARINQQLdtkQPRQY--FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd14905 296 VNEAVENRDSLARSLYSALFHWIIDFLNSKL---KPTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 498 VLEQEEYKKEGIEW-TFIDFgMDLAACIELIEKpmgIFSILEEECMFPKATDTSFKNKLydqhlgksANFQKPKVVKGKA 576
Cdd:cd14905 373 KQEQREYQTERIPWmTPISF-KDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL--------QNFLSRHHLFGKK 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 577 EAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAH---LFSGTQTAEAEGGGPKKGGKKKGSSFQTVSA 653
Cdd:cd14905 441 PNKFGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFSrdgVFNINATVAELNQMFDAKNTAKKSPLSIVKV 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 654 LFR------ENLNK-----------------------LMTNLRSTHP---------HFVRCIIPNETKTPGAMEHELVLH 695
Cdd:cd14905 521 LLScgsnnpNNVNNpnnnsgggggggnsgggsgsggsTYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLTFDVKSVNE 600
|
650
....*....|....*...
gi 305632842 696 QLRCNGVLEGIRICRKGF 713
Cdd:cd14905 601 QIKSLCLLETTRIQRFGY 618
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
101-729 |
4.56e-65 |
|
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: 234.38 E-value: 4.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYrgkkrqeappHIFSISDNAYQFMLTDREN-QSILITG 179
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 180 ESGAGKTVNTKRVIQYFATiavtgeKKKEEVTSgkmqgtleDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14874 72 ESGSGKSYNAFQVFKYLTS------QPKSKVTT--------KHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITtNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14874 138 LTGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIK-GLQKFFYINQGNSTENIQSDVNHFKHLEDAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 340 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKqREEQAEPDGTEVADKA-----AYLQSLNSADLLKALCyPRVKVGNEFv 414
Cdd:cd14874 217 HVLGFSDDHCISIYKIISTILHIGNIYFRTK-RNPNVEQDVVEIGNMSevkwvAFLLEVDFDQLVNFLL-PKSEDGTTI- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 415 tkgqTVEQVTNAVGALAKAVYEKMFLWMVARINQQLdtKQPRQY-FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14874 294 ----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHL--KCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 494 HHMFVLEQEEYKKEGIEwtfIDFGM----DLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSAnFQK 568
Cdd:cd14874 368 KHSFHDQLVDYAKDGIS---VDYKVpnsiENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS-YGK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 569 pkvVKGKAEAHFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAHLFSgTQTAEAEGGGPKKGGKKKGSSF 648
Cdd:cd14874 444 ---ARNKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE-SYSSNTSDMIVSQAQFILRGAQ 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 649 QTVsalfrENLNKlmtnlrsTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 728
Cdd:cd14874 520 EIA-----DKING-------SHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRC 587
|
.
gi 305632842 729 L 729
Cdd:cd14874 588 L 588
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
103-727 |
1.79e-64 |
|
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: 235.25 E-value: 1.79e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQ----------EAPPHIFSISDNAYQFMLTDREN 172
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 173 QSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIR 252
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 253 IHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKK--PELIEMLLITTNPYDYPFVSQG--EISVASID- 327
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQAdpLATNFALDa 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 328 -DQEELMATDSAIDIlgfTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDG--TEVADKAAYL-----QSLNSADLL 399
Cdd:cd14893 244 rDYRDLMSSFSALRI---RKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGAnsTTVSDAQSCAlkdpaQILLAAKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 400 KAlcYPRV------------KVGNEFVT--KGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQL----DTKQPRQYFIG 461
Cdd:cd14893 321 EV--EPVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNIVIN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 462 -----VLDIAGFEIFD--FNSLEQLCINFTNEKLQQFFNHHMFV-----LEQEEYKKEG--IEWTFIDFGMDLAACIELI 527
Cdd:cd14893 399 sqgvhVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 528 E-KPMGIFSILEEECMFPKATDTSFKNKLY--DQHLG------KSANFQKPKVVKGKA-EAHFSLIHYAGVVDYNITGWL 597
Cdd:cd14893 479 EdKPFGIFDLLTENCKVRLPNDEDFVNKLFsgNEAVGglsrpnMGADTTNEYLAPSKDwRLLFIVQHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 598 EKNKDPLNETVVGLYQKSAMKTLaHLFSGTQTAEAEGGG---PKKGGKKKGSSFQTVSALFRENLN-------------- 660
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKNAVL-HAVGAAQMAAASSEKaakQTEERGSTSSKFRKSASSARESKNitdsaatdvynqad 637
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 305632842 661 KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 727
Cdd:cd14893 638 ALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
122-253 |
1.30e-61 |
|
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: 208.35 E-value: 1.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 122 FCVTVNPYKWLPVYNPEVV-TAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIA 200
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 305632842 201 VTGEKKKEE---VTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRI 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 ... |
100-768 |
9.84e-45 |
|
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: 175.02 E-value: 9.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYR-GKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 179 GESGAGKTVNTKRVIQYFA-----------TIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 247
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAyqvkgsrrlptNLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 248 GKFIRIHFGTTgKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASID 327
Cdd:cd14938 161 SKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFL-KNIENYSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 328 DQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGN-------------LKFKQKQREEQAEPDGTEVADKAAYLQSLN 394
Cdd:cd14938 239 YSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNINYETILSELENSEDIGLDEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 395 SADLL---KALCYPRVKVGNEFVT----------KGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYF-- 459
Cdd:cd14938 319 VKNLLlacKLLSFDIETFVKYFTTnyifndsiliKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININtn 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 460 -IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM--GIFSI 536
Cdd:cd14938 399 yINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLFSL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 537 LEEECMfPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAhFSLIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSA 616
Cdd:cd14938 479 LENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 617 MKTLAHLFSGTQTAEAEGGGPKKGGKKKGSSF-----------QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTP 685
Cdd:cd14938 557 NEYMRQFCMFYNYDNSGNIVEEKRRYSIQSALklfkrrydtknQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESKRE 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 686 -GAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAsaipegqfiDSKKASEKLLASIDIDHTQYKFGH 764
Cdd:cd14938 637 lCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMIGN 707
|
....
gi 305632842 765 TKVF 768
Cdd:cd14938 708 NMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1177-1930 |
3.12e-32 |
|
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: 137.50 E-value: 3.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1177 KMRRdlEEATLQHEATAATLrKKHADSVAELGEQIDNLQRVKQKLEKEKsEMKMEIDDLASNVETVSKakgnlekmcRTL 1256
Cdd:TIGR02168 171 KERR--KETERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERYK-ELKAELRELELALLVLRL---------EEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1257 EDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEeikaknalaha 1336
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQI----------- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1337 LQSSRHDcdlLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKK------LAQRLQAAEEHVEA 1410
Cdd:TIGR02168 307 LRERLAN---LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELeaeleeLESRLEELEEQLET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1411 VNAKCASLEKTKQRLQNEVEDLMLDVERtnaacaaLDKKQRNFDKILAEWKQKYEEthAELEASQKEARSLGTELFKMKN 1490
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIERLEARLER-------LEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1491 AYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEA----------SLEHEEG 1560
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlseLISVDEG 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1561 KILRIQLEL------------NQVKSEVD----------RKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRL 1618
Cdd:TIGR02168 535 YEAAIEAALggrlqavvvenlNAAKKAIAflkqnelgrvTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1619 KKKMEGDLNEMEI--QLNHANRMAAEALRNYRNtqgILKDTQLHLDDALRTQEDLKEQLAMVERRAnllqaEIEELRATL 1696
Cdd:TIGR02168 615 RKALSYLLGGVLVvdDLDNALELAKKLRPGYRI---VTLDGDLVRPGGVITGGSAKTNSSILERRR-----EIEELEEKI 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1697 EQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKE 1776
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1777 QDTSAHLERMKKNMEQTVKDLQLRLDEAEQlalkggkkQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTY 1856
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKE--------ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305632842 1857 QTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLRVKSRE 1930
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
844-1593 |
7.34e-29 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 126.72 E-value: 7.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 844 LKSAETEKEMAtmkEEFQKTKDELAKSEAKrkELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKI 923
Cdd:TIGR02169 200 LERLRREREKA---ERYQALLKEKREYEGY--ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 924 KEVTERAED--EEEINA------ELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAK 995
Cdd:TIGR02169 275 EELNKKIKDlgEEEQLRvkekigELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 996 LTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIEN 1075
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1076 EKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLS----------- 1144
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEervrggravee 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1145 -------------RELEEISER----LEEAGGA------------TSAQIEMNKKREA------EFQKMRRDLEEATLQH 1189
Cdd:TIGR02169 515 vlkasiqgvhgtvAQLGSVGERyataIEVAAGNrlnnvvveddavAKEAIELLKRRKAgratflPLNKMRDERRDLSILS 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1190 EATAAtlrkKHADSVAELGEQIDNLQR-------VKQKLEKEKSEM---KM-----EIDDLASNVETVSKAKGNLEKMCR 1254
Cdd:TIGR02169 595 EDGVI----GFAVDLVEFDPKYEPAFKyvfgdtlVVEDIEAARRLMgkyRMvtlegELFEKSGAMTGGSRAPRGGILFSR 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1255 TLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALA 1334
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1335 HALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIqrtEELEEAKKKLAQRLQAAEEHVEAVNAK 1414
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAEL---SKLEEEVSRIEARLREIEQKLNRLTLE 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1415 CASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEE 1494
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1495 SLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIK------KQVEQEKCELQAALEEAE-----ASLEHEEGKIL 1563
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEIRALEpvnmlAIQEYEEVLKR 987
|
810 820 830
....*....|....*....|....*....|.
gi 305632842 1564 RIQLELNQVKSEVDRK-IAEKDEEIDQLKRN 1593
Cdd:TIGR02169 988 LDELKEKRAKLEEERKaILERIEEYEKKKRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1316-1935 |
7.33e-28 |
|
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: 123.24 E-value: 7.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1316 IEELKRQLEE-EIKAKNALA-HALQS--SRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETdAIQRTEELE 1391
Cdd:TIGR02168 195 LNELERQLKSlERQAEKAERyKELKAelRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQE-LEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1392 EAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAEL 1471
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1472 EASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEA 1551
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1552 EASLEHEEGKILRIQLE--------LNQVKSEVDRKIAEKDEEIDQLKRNH------IRIVESMQ--------------- 1602
Cdd:TIGR02168 434 ELKELQAELEELEEELEelqeelerLEEALEELREELEEAEQALDAAERELaqlqarLDSLERLQenlegfsegvkallk 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1603 -------------------------------STLDAEIRSRNDAIR-----LKKKMEGDLNEMEIQLNHANRMAA---EA 1643
Cdd:TIGR02168 514 nqsglsgilgvlselisvdegyeaaieaalgGRLQAVVVENLNAAKkaiafLKQNELGRVTFLPLDSIKGTEIQGndrEI 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1644 LRNYRNTQGILKD-----TQLH---------------LDDALRTQEDLKEQLAMV------------------ERRANLL 1685
Cdd:TIGR02168 594 LKNIEGFLGVAKDlvkfdPKLRkalsyllggvlvvddLDNALELAKKLRPGYRIVtldgdlvrpggvitggsaKTNSSIL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1686 --QAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAI 1763
Cdd:TIGR02168 674 erRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1764 TDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKG 1843
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE-ELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1844 LRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNK 1923
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
730
....*....|..
gi 305632842 1924 LRVKSREVHTKV 1935
Cdd:TIGR02168 913 LRRELEELREKL 924
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
916-1752 |
9.14e-28 |
|
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: 123.24 E-value: 9.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 916 KIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECS------ELKKDIDDLELTLAKVEKEKHatENKVKNLTEEMAGL 989
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEkaerykELKAELRELELALLVLRLEEL--REELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 990 DETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQES 1069
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1070 IMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEE 1149
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1150 ISERLEEAGGATSAQIEmnKKREAEFQKMRRDLEEatlqHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEM- 1228
Cdd:TIGR02168 412 LEDRRERLQQEIEELLK--KLEEAELKELQAELEE----LEEELEELQEELERLEEALEELREELEEAEQALDAAERELa 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1229 -----KMEIDDLASNVETVSKAKGNLEKMCRTLED---QVSELKSKEEEQQRLINdlTAQRGRLQTESGEFSRQLDEKDA 1300
Cdd:TIGR02168 486 qlqarLDSLERLQENLEGFSEGVKALLKNQSGLSGilgVLSELISVDEGYEAAIE--AALGGRLQAVVVENLNAAKKAIA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1301 LVSQLSRGKQAFTqqieELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESK-----------AELQRALSKAN 1369
Cdd:TIGR02168 564 FLKQNELGRVTFL----PLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllggvlvvDDLDNALELAK 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1370 TEVAQWR-------------------TKYETDAIQRTEELEEAKKKLAQrlqaAEEHVEAVNAKCASLEKTKQRLQNEVE 1430
Cdd:TIGR02168 640 KLRPGYRivtldgdlvrpggvitggsAKTNSSILERRREIEELEEKIEE----LEEKIAELEKALAELRKELEELEEELE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1431 DLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQ 1510
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1511 QEISDLTEQIAEG-------GKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDrKIAEK 1583
Cdd:TIGR02168 796 EELKALREALDELraeltllNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-ELESE 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1584 DEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGIL-KDTQLHLD 1662
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLE 954
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1663 DALRTQEDLKEQLAMVERRANLLQAEIEEL-RATLEqtersrkiAEQELLDASERVQLLHTQNTSLINTKKKLETDISQM 1741
Cdd:TIGR02168 955 EAEALENKIEDDEEEARRRLKRLENKIKELgPVNLA--------AIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
890
....*....|.
gi 305632842 1742 QGEMEDILQEA 1752
Cdd:TIGR02168 1027 DREARERFKDT 1037
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
980-1798 |
1.80e-27 |
|
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: 122.09 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 980 KNLTEEMAGldetIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLR--------MD 1051
Cdd:TIGR02168 158 RAIFEEAAG----ISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRelelallvLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1052 LERAKRKLE---GDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEA 1128
Cdd:TIGR02168 234 LEELREELEelqEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1129 ERASRAKAEKQRSDLSR---ELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKhadsVA 1205
Cdd:TIGR02168 314 LERQLEELEAQLEELESkldELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK----VA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1206 ELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKmcRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQ 1285
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEEALEELR 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1286 TESGEFSRQLDEKDALVSQLsRGKQAFTQQIEELKRQLEEEIKakNALAHALQSSRHDcDLLREQYEEEQESKAELQRAL 1365
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQL-QARLDSLERLQENLEGFSEGVK--ALLKNQSGLSGIL-GVLSELISVDEGYEAAIEAAL 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1366 SKANTEVAqwrTKYETDAIQRTEELEEAKK--------------KLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVED 1431
Cdd:TIGR02168 544 GGRLQAVV---VENLNAAKKAIAFLKQNELgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSY 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1432 LMLDV----------------------------------------ERTNAACAALDKKQRNFDKILAEWKQKYEETHAEL 1471
Cdd:TIGR02168 621 LLGGVlvvddldnalelakklrpgyrivtldgdlvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKAL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1472 EASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEA 1551
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1552 EASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRiVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEI 1631
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER-LESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1632 QLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELL 1711
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1712 DASERVQLLHTQNTSLINTKK-KLETDISQMQGEMEDIlqearnaeEKAKKAITDAAMMA-EELKKEQDTSAHLERMKKN 1789
Cdd:TIGR02168 940 NLQERLSEEYSLTLEEAEALEnKIEDDEEEARRRLKRL--------ENKIKELGPVNLAAiEEYEELKERYDFLTAQKED 1011
|
....*....
gi 305632842 1790 MEQTVKDLQ 1798
Cdd:TIGR02168 1012 LTEAKETLE 1020
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
852-1433 |
1.02e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 112.72 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 852 EMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAE 931
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 932 DEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTL 1011
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1012 DDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEI 1091
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1092 SNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQR---------SDLSRELEEISERLEEAGGATS 1162
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavavliGVEAAYEAALEAALAAALQNIV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1163 AQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDnlqRVKQKLEKEKSEMKMEIDDLASNVETV 1242
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD---LVASDLREADARYYVLGDTLLGRTLVA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1243 SKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQ 1322
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1323 LEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVaqwrtkYETDAIQRteELEEAKKKLaQRL- 1401
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP------PDLEELER--ELERLEREI-EALg 780
|
570 580 590
....*....|....*....|....*....|....*
gi 305632842 1402 ---QAAEEHVEAVNAKCASLEKTKQRLQNEVEDLM 1433
Cdd:COG1196 781 pvnLLAIEEYEELEERYDFLSEQREDLEEARETLE 815
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
921-1807 |
2.55e-24 |
|
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: 111.70 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 921 AKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKdIDDLELTLAKVE-----KEKHATENKVKNLTEEMAGLDETIAK 995
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 996 LTKEKKALQEAHQQTLDDLQAEEDKVNTLTKaktkleqqvddlEGSLEQEKKLRmDLERAKRKLEGDLKLAQESIMDIEN 1075
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGE------------EEQLRVKEKIG-ELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1076 EKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLE 1155
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1156 EAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRkkhaDSVAELGEQIDNLQRVKQKLEKEKSEMkmeiddl 1235
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE----DKALEIKKQEWKLEQLAADLSKYEQEL------- 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1236 asnvetvskakgnlekmcRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDA-------LVSQLSRG 1308
Cdd:TIGR02169 472 ------------------YDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGSV 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1309 KQAFTQQIEELKRQ------LEEEIKAKNA--LAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYE 1380
Cdd:TIGR02169 534 GERYATAIEVAAGNrlnnvvVEDDAVAKEAieLLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1381 TD---AIQRT---EELEEAKKKLAQ-RLQAAE-EHVEAVNA------KCASLEKTKQRLQNEVEDLMLDVERTNAACAAL 1446
Cdd:TIGR02169 614 PAfkyVFGDTlvvEDIEAARRLMGKyRMVTLEgELFEKSGAmtggsrAPRGGILFSRSEPAELQRLRERLEGLKRELSSL 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1447 DKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGtelfkmknayeeslDQLETLKRENKNLQQEISDLTEQIAEGGKR 1526
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE--------------QEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1527 IHELEKIKKQVEQEKCELQAALEEAEASLEHEegKILRIQLELNQVKSEVdRKIAEKDEEIDQ-LKRNHIRivESMQSTL 1605
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLEARLSHS--RIPEIQAELSKLEEEV-SRIEARLREIEQkLNRLTLE--KEYLEKE 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1606 DAEIRSRNDAIRLKKKMEGDlnemeiQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRTQEDLKEQLAMVERRANLL 1685
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEK------EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1686 QAEIEELRATLEQTERSRKIAEQELldaservqllhtqntSLINTKKKLETDISQMQGEMEDIlQEARNAEEKAKKAITD 1765
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLEALEEEL---------------SEIEDPKGEDEEIPEEELSLEDV-QAELQRVEEEIRALEP 972
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 305632842 1766 AAMMA-EELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQL 1807
Cdd:TIGR02169 973 VNMLAiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1314-1915 |
2.69e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.57 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1314 QQIEELKRQ---------LEEEIKAKNALAHALQSsrhdcDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYEtdai 1384
Cdd:COG1196 200 RQLEPLERQaekaeryreLKEELKELEAELLLLKL-----RELEAELEELEAELEELEAELEELEAELAELEAELE---- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1385 qrteELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKY 1464
Cdd:COG1196 271 ----ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1465 EETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCEL 1544
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1545 QAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRsRNDAIRLKKKMEG 1624
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR-LLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1625 DLNE------------------MEIQLNHANRMAAEALRNYRNTQGILKDTQlhldDALRTQEDLKEQLAmveRRANLLQ 1686
Cdd:COG1196 506 FLEGvkaalllaglrglagavaVLIGVEAAYEAALEAALAAALQNIVVEDDE----VAAAAIEYLKAAKA---GRATFLP 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1687 AEIEELRATLEQTERSRKIAEQELLDASERVQLLHT----QNTSLINTkkkLETDISQMQGEMEDILQEARNAEEKAKKA 1762
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARyyvlGDTLLGRT---LVAARLEAALRRAVTLAGRLREVTLEGEG 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1763 ITDAAMMAEELKKEQDTSahLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVK 1842
Cdd:COG1196 656 GSAGGSLTGGSRRELLAA--LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1843 GLRKHERRVKELTYQTEEDRKNILRLQDLvDKLQAKVKSYKRQAEE-------AEEqsntnlakfrklqhELEEAEERAD 1915
Cdd:COG1196 734 REELLEELLEEEELLEEEALEELPEPPDL-EELERELERLEREIEAlgpvnllAIE--------------EYEELEERYD 798
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1145-1934 |
3.86e-24 |
|
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: 111.31 E-value: 3.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1145 RELEEISERLEEAggatsaQIEMNKKREaEFQKMRRDLEEAtlqhEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKE 1224
Cdd:TIGR02169 177 EELEEVEENIERL------DLIIDEKRQ-QLERLRREREKA----ERYQALLKEKREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1225 KSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQ-QRLINDLTAQRGRLQTESGEFSRQLDEKDALVS 1303
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1304 QLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVaqwrtkyeTDA 1383
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL--------EKL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1384 IQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVErtnaacaALDKKQRNFDKILAEWKQK 1463
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK-------KQEWKLEQLAADLSKYEQE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1464 YEETHAELEASQKEARSLgtelfkmknayEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELekiKKQVEQEKCE 1543
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKL-----------QRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGT---VAQLGSVGER 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1544 LQAALEEAEAS------LEHEEGKILRIQ------------LELNQVKSE-VDRKIAEKDE---------EIDQLKRNHI 1595
Cdd:TIGR02169 537 YATAIEVAAGNrlnnvvVEDDAVAKEAIEllkrrkagratfLPLNKMRDErRDLSILSEDGvigfavdlvEFDPKYEPAF 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1596 R-------IVESMQSTldaeiRSRNDAIRLKKkMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRTQ 1668
Cdd:TIGR02169 617 KyvfgdtlVVEDIEAA-----RRLMGKYRMVT-LEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKREL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1669 EDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVqllhtqntslintkKKLETDISQMQGEMEdi 1748
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL--------------EELEEDLSSLEQEIE-- 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1749 lqearNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKnmEQTVKDLQLRLDEAEqlalkggkKQIQKLEARVRELEG 1828
Cdd:TIGR02169 755 -----NVKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLE--------EEVSRIEARLREIEQ 819
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1829 EVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELE 1908
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
810 820
....*....|....*....|....*.
gi 305632842 1909 EAEERADIAESQVNKLRVKSREVHTK 1934
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1123-1913 |
1.09e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 109.77 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1123 EeeieaerasrAKAEKQRsdlsRELEEISERLEEaggatsAQIEMNKKREaEFQKMRRDLEEAtlqhEATAATLRKKHAD 1202
Cdd:TIGR02169 169 D----------RKKEKAL----EELEEVEENIER------LDLIIDEKRQ-QLERLRREREKA----ERYQALLKEKREY 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1203 SVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQ-QRLINDLTAQR 1281
Cdd:TIGR02169 224 EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1282 GRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAEL 1361
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1362 QRALSKANTEVaqwrtkyeTDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVErtna 1441
Cdd:TIGR02169 384 RDELKDYREKL--------EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK---- 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1442 acaALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLgtelfkmknayEESLDQLETLKRENKNLQQEISDLTEQIA 1521
Cdd:TIGR02169 452 ---KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL-----------QRELAEAEAQARASEERVRGGRAVEEVLK 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1522 EGGKRIHELekiKKQVEQEKCELQAALEEAEAS------LEHEEGKILRIQ------------LELNQVKSE-VDRKIAE 1582
Cdd:TIGR02169 518 ASIQGVHGT---VAQLGSVGERYATAIEVAAGNrlnnvvVEDDAVAKEAIEllkrrkagratfLPLNKMRDErRDLSILS 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1583 KDE---------EIDQLKRNHIR-------IVESMQS-----------TLDAEI-----------RSRNDAIRLKKKMEG 1624
Cdd:TIGR02169 595 EDGvigfavdlvEFDPKYEPAFKyvfgdtlVVEDIEAarrlmgkyrmvTLEGELfeksgamtggsRAPRGGILFSRSEPA 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1625 DLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRK 1704
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1705 IAEQELLDASERVQLLHTQNTSLINTKKKLETDIS-----QMQGEMEDILQE-------ARNAEEKAKKAITDAAMMAEE 1772
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEvsriearLREIEQKLNRLTLEKEYLEKE 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1773 LKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlalkggkkQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVK 1852
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE--------ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305632842 1853 ELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSnTNLAKFRKLQHELEEAEER 1913
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP-EEELSLEDVQAELQRVEEE 966
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1249-1832 |
2.81e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.10 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1249 LEKMCRTLEDQVS------ELKSKEEEQQRL-----INDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIE 1317
Cdd:COG1196 198 LERQLEPLERQAEkaeryrELKEELKELEAEllllkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1318 ELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQwrtkyetdAIQRTEELEEAKKKL 1397
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE--------LEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1398 AQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKE 1477
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1478 ARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKcelqAALEEAEASLEH 1557
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL----LLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1558 EEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHAN 1637
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1638 RMAAEALRNYRNTQGILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAeiEELRATLEQTERSRKIAEQELLDASERV 1717
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA--LRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1718 QLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDL 1797
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
570 580 590
....*....|....*....|....*....|....*
gi 305632842 1798 QLRLDEAEQLALKGGKKQIQKLEARVRELEGEVES 1832
Cdd:COG1196 744 EEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1139-1752 |
1.25e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.17 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1139 QRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHAdSVAELGEQIDNLQRVK 1218
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA-ELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1219 QKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEK 1298
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1299 DALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTK 1378
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1379 YETDA---IQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVE---------RTNAACAAL 1446
Cdd:COG1196 472 AALLEaalAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEaayeaaleaALAAALQNI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1447 DKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKR 1526
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1527 IHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLD 1606
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1607 AEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEalrnyrntqgilkdtqlhLDDALRTQEDLKEQLAMVERRANLLQ 1686
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEEL------------------LEEEALEELPEPPDLEELERELERLE 773
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305632842 1687 AEIEEL-----RAtleqtersrkiaEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEA 1752
Cdd:COG1196 774 REIEALgpvnlLA------------IEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLET 832
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
858-1600 |
1.50e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 106.38 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 858 EEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEIN 937
Cdd:PTZ00121 1191 EELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA 1270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 938 AELTAKKRKLED-ECSELKKDIDDLEltlaKVEKEKHATENKVKnlTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQA 1016
Cdd:PTZ00121 1271 AIKAEEARKADElKKAEEKKKADEAK----KAEEKKKADEAKKK--AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1017 EEdkvntltKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQS 1096
Cdd:PTZ00121 1345 AE-------AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK 1417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1097 KIEDEQALGIQLQKKIKELQARIEELEeeieaerasRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEfq 1176
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKADEAKKKAEEAK---------KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD-- 1486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1177 KMRRDLEEATLQ-HEATAATLRKKHADSVAELGEQidnlqrvKQKLEKEKSEMKMEIDDlASNVETVSKAkgnlEKMCRT 1255
Cdd:PTZ00121 1487 EAKKKAEEAKKKaDEAKKAAEAKKKADEAKKAEEA-------KKADEAKKAEEAKKADE-AKKAEEKKKA----DELKKA 1554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1256 LEDQVSELKSKEEEQQRlindlTAQRGRLQTESGEFSRQLDEKdALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNalAH 1335
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKK-----AEEDKNMALRKAEEAKKAEEA-RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE--LK 1626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1336 ALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAiQRTEEL---EEAKKKLAQRLQAAEEH---VE 1409
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAkkaEEDEKKAAEALKKEAEEakkAE 1705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1410 AVNAKCASLEKTKQRLQNEVEDLMLDVERTnaacaaldKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMK 1489
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEA--------KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1490 NAY-EESLDQLETLKR-ENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQA-----ALEEAEASLEHEEGKi 1562
Cdd:PTZ00121 1778 EAViEEELDEEDEKRRmEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVAdsknmQLEEADAFEKHKFNK- 1856
|
730 740 750
....*....|....*....|....*....|....*...
gi 305632842 1563 lriqlelNQVKSEVDRKIAEKDEEIDQLKRNHIRIVES 1600
Cdd:PTZ00121 1857 -------NNENGEDGNKEADFNKEKDLKEDDEEEIEEA 1887
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
223-715 |
2.92e-22 |
|
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: 104.82 E-value: 2.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 223 IISANPLLEAFGNAKTVRNDNSSRFGKF--IRIHFGTTG---KLASADIETYLLEKSRVTFQL------KAERSYHIFYQ 291
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 292 ITS--NKKPEL----IEMLLITTNPYDYPFVSQGEISVASIDDQEELMATD--------SAIDILGFTNEEKVSIYKLTG 357
Cdd:cd14894 329 MVAgvNAFPFMrllaKELHLDGIDCSALTYLGRSDHKLAGFVSKEDTWKKDverwqqviDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 358 AVMHYGNLKFKQKQREEQAEPDGT---EVADKAAYLQSLNSADLL-KALCYPRVKVGNEFVTKGQTVE--QVTNAVGALA 431
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLeRMLMTKSVSLQSTSETFEVTLEkgQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 432 KAVYEKMFLWMVARINQ--------------QLDTKQPRQYFIGVL---DIAGFEIFDFNSLEQLCINFTNEKLqqFFNH 494
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEatkmsalstdgnkhQMDSNASAPEAVSLLkivDVFGFEDLTHNSLDQLCINYLSEKL--YARE 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 495 HMFVLEQEEYKKEGIEWtfiDFGMDLaacIELIEKPMGIFSILEEECMFPKATDTSF-----KNKLYDQHL--GKSANFQ 567
Cdd:cd14894 567 EQVIAVAYSSRPHLTAR---DSEKDV---LFIYEHPLGVFASLEELTILHQSENMNAqqeekRNKLFVRNIydRNSSRLP 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 568 KPKVVKGKAEAH---------FSLIHYAGVVDYNITGWLEKNKDPL-NETVVGLYQKSAMKTLAHLFSGTQTAEAEGGGP 637
Cdd:cd14894 641 EPPRVLSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVyANLLVGLKTSNSSHFCRMLNESSQLGWSPNTNR 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 638 KK--GGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPS 715
Cdd:cd14894 721 SMlgSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICRNSSSS 800
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
847-1536 |
1.34e-21 |
|
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: 102.83 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 847 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMvtllkekNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEV 926
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRL-------EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 927 TERAEDEEEINAELtaKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKE---KKAL 1003
Cdd:TIGR02168 413 EDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERElaqLQAR 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1004 QEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAkrkLEGDLklaQESIMDIENEKQQLDEK 1083
Cdd:TIGR02168 491 LDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAA---LGGRL---QAVVVENLNAAKKAIAF 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1084 LKKKEFEISNLqskIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSD-LSRELeeISERLEEA----- 1157
Cdd:TIGR02168 565 LKQNELGRVTF---LPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYlLGGVL--VVDDLDNAlelak 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1158 ------------------GGATSAQIEmnkKREAEFQKMRRDLEEATLQHEATAATLRKKHAdSVAELGEQIDNLQRVKQ 1219
Cdd:TIGR02168 640 klrpgyrivtldgdlvrpGGVITGGSA---KTNSSILERRREIEELEEKIEELEEKIAELEK-ALAELRKELEELEEELE 715
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1220 KLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQrlindltAQRGRLQTESGEFSRQLDEKD 1299
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE-------ERLEEAEEELAEAEAEIEELE 788
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1300 ALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKY 1379
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1380 ETdAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKK-QRNFDKILA 1458
Cdd:TIGR02168 869 EE-LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRiDNLQERLSE 947
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1459 EWK-------QKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELE 1531
Cdd:TIGR02168 948 EYSltleeaeALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID 1027
|
....*
gi 305632842 1532 KIKKQ 1536
Cdd:TIGR02168 1028 REARE 1032
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1005-1828 |
6.53e-21 |
|
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: 100.58 E-value: 6.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1005 EAHQQTLDDLQAEEDKVNTL-TKAKTKLEQQVDDLEGSLEQ---EKKLRMDLERAKRKLEGDLK-LAQESIMDIENEKQQ 1079
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELhEKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQEDLRnQLQNTVHELEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1080 LDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAEraSRAKAEKQRSDLSRELEEISERLEEAGG 1159
Cdd:pfam15921 161 KEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSM--STMHFRSLGSAISKILRELDTEISYLKG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1160 AT--------SAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKME 1231
Cdd:pfam15921 239 RIfpvedqleALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQ 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1232 IDDLASnveTVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEkdaLVSQLSRGKQA 1311
Cdd:pfam15921 319 LSDLES---TVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQK---LLADLHKREKE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1312 FTQQIEELKRQLEEEIKAKNALAHalqssrhdcdllreqyeeeqeskaeLQRALSKANTEVaqwrtkyetdaiQRTEELE 1391
Cdd:pfam15921 393 LSLEKEQNKRLWDRDTGNSITIDH-------------------------LRRELDDRNMEV------------QRLEALL 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1392 EAKKKLAQ--------RLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLmldvertNAACAALDKKQRNFDKILAEWKQK 1463
Cdd:pfam15921 436 KAMKSECQgqmerqmaAIQGKNESLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTVSDLTASLQEK 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1464 yeethaeleasQKEARSLGTELFKMKNAYEESLDQLETLKREN---KNLQQEISDLTEQIAEGGKRIhelEKIKKQVEQ- 1539
Cdd:pfam15921 509 -----------ERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTECEALKLQMAEKDKVI---EILRQQIENm 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1540 -----EKCELQAALEEAEASLEHE-EGKILRIQlELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLdaeiRSRN 1613
Cdd:pfam15921 575 tqlvgQHGRTAGAMQVEKAQLEKEiNDRRLELQ-EFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERL----RAVK 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1614 DairLKKKMEGDLNEMEIQLNHANRMAAE---ALRNYRNTQgilkdtqlhlDDALRTQEDLKEQLAMVerranllQAEIE 1690
Cdd:pfam15921 650 D---IKQERDQLLNEVKTSRNELNSLSEDyevLKRNFRNKS----------EEMETTTNKLKMQLKSA-------QSELE 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1691 ELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMA 1770
Cdd:pfam15921 710 QTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMA 789
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305632842 1771 EELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQ-KLEAR--VRELEG 1828
Cdd:pfam15921 790 GELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRlKLQHTldVKELQG 850
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
845-1432 |
1.47e-20 |
|
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: 99.36 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 845 KSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQ----------AEAEGLADAEERCDQLIK 914
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAslnneierleARLERLEDRRERLQQEIE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 915 T--KIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKV---KNLTEEMAGL 989
Cdd:TIGR02168 425 EllKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdslERLQENLEGF 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 990 DETIAKLTKEKK-------------------------ALQEAHQQTL-DDLQAEEDKVNTLTKAKTKL------------ 1031
Cdd:TIGR02168 505 SEGVKALLKNQSglsgilgvlselisvdegyeaaieaALGGRLQAVVvENLNAAKKAIAFLKQNELGRvtflpldsikgt 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1032 EQQVDDLEGSLEQEKKLRM--DLERAKRKLEGDLK--LAQESIMDIENEKQQLDEKLKKKE---------FEISNLQSKI 1098
Cdd:TIGR02168 585 EIQGNDREILKNIEGFLGVakDLVKFDPKLRKALSylLGGVLVVDDLDNALELAKKLRPGYrivtldgdlVRPGGVITGG 664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1099 EDEQALGIQ-LQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatsaqiemnkkrEAEFQK 1177
Cdd:TIGR02168 665 SAKTNSSILeRRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL--------------SRQISA 730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1178 MRRDLEEATLQHEATAATLRKKHADsVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLE 1257
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKE-LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1258 DQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHAL 1337
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1338 QSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCAS 1417
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEE 969
|
650
....*....|....*
gi 305632842 1418 LEKTKQRLQNEVEDL 1432
Cdd:TIGR02168 970 ARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
848-1537 |
4.47e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 97.70 E-value: 4.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 848 ETEKEMAtmkeefqKTKDELAKSEAKRKELEEKMVTLLKEKNDLQ--LQVQAEAEgLADAEERCDQLIktkiQLEAKIKE 925
Cdd:COG1196 176 EAERKLE-------ATEENLERLEDILGELERQLEPLERQAEKAEryRELKEELK-ELEAELLLLKLR----ELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 926 VTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQE 1005
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1006 AHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLK 1085
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1086 kkefeisNLQSKIEDEQALGIQLQKKIKELqarieeleeeIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQI 1165
Cdd:COG1196 404 -------ELEEAEEALLERLERLEEELEEL----------EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1166 EMNKKR---EAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETV 1242
Cdd:COG1196 467 ELLEEAallEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1243 SKAKGNLEKMcRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELkrq 1322
Cdd:COG1196 547 ALQNIVVEDD-EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL--- 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1323 LEEEIKAKNALAHALQSSRHDcdllreqyeeeqeskaELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQ 1402
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLA----------------GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1403 AAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLG 1482
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 305632842 1483 TELFKMKNAYEE-------SLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQV 1537
Cdd:COG1196 767 RELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
834-1439 |
4.80e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 98.29 E-value: 4.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 834 MKLFFKIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAeercdqlI 913
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA-------A 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 914 KTKIQLEAKIKEVTERAEDEEEINAELTAKKRKL-EDECSELKKDIDDLEltlAKVEKEKHATENKVKnlTEEMAGLDET 992
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaEKKKEEAKKKADAAK---KKAEEKKKADEAKKK--AEEDKKKADE 1409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 993 IAKLTKEKKALQEAHQqtlddlQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKlrmdLERAKRKLEgdlklaqesimd 1072
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKK------KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK----AEEAKKKAE------------ 1467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1073 ienEKQQLDEKLKKKEFEISNLQSKIEDEQAlgiqlQKKIKELQarieeleeeieAERASRAKAEKQRSDLSRELEEISE 1152
Cdd:PTZ00121 1468 ---EAKKADEAKKKAEEAKKADEAKKKAEEA-----KKKADEAK-----------KAAEAKKKADEAKKAEEAKKADEAK 1528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1153 RLEEAGGATSAQIEMNKKREAEFQKMR--RDLEEATLQHEATAATLRKKHADSVAELGEQIDNlQRVKQKLEKEKSEMKM 1230
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELKKAEelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE-ARIEEVMKLYEEEKKM 1607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1231 EIDDLASNVETVSKAKgnlekmcrtledqvsELKsKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQ 1310
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAE---------------ELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1311 AFTQQIEELKRQLEEEIKAKNALAHALQSSRhDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAiQRTEEL 1390
Cdd:PTZ00121 1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEAK-KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK-KKAEEA 1749
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 305632842 1391 ---EEAKKKLAQRLQAAEEHVEAVNAKCASLekTKQRLQNEVEDLMLDVERT 1439
Cdd:PTZ00121 1750 kkdEEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVDKK 1799
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
841-1378 |
4.03e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 94.36 E-value: 4.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 841 KPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQlqvqAEAEGLADAEERCDQLIKTKIQLE 920
Cdd:PRK03918 183 KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 921 AKIKEVTERAEDEEEINAELTAKKRKLE------DECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIA 994
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 995 KLTKEKKALQEahqqTLDDLQAEEDKVNTLTKAKTKLEQ--QVDDLEGSLEQEKKLRM--DLERAKRKLEGDLKLAQESI 1070
Cdd:PRK03918 339 RLEELKKKLKE----LEKRLEELEERHELYEEAKAKKEEleRLKKRLTGLTPEKLEKEleELEKAKEEIEEEISKITARI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1071 MDIENEKQQLD---EKLKKKEFEISNLQSKIEDEQALGIqLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRE- 1146
Cdd:PRK03918 415 GELKKEIKELKkaiEELKKAKGKCPVCGRELTEEHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEs 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1147 ----LEEISERLEEAGGATSA-QIEMNKKREAEFQKMRRDLEEATLQHEATaatlrKKHADSVAELGEQIDNLQRVKQKL 1221
Cdd:PRK03918 494 elikLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSL-----KKELEKLEELKKKLAELEKKLDEL 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1222 EKEKSEMKMEIDDLA-SNVETVSKAKGNLEKMCR---TLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDE 1297
Cdd:PRK03918 569 EEELAELLKELEELGfESVEELEERLKELEPFYNeylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1298 KDALVSQLSRGKQaftQQIEELKRQLEEEIKAKNALAHALQSSRH----DCDLLREQYEEEQESKAELQRaLSKANTEVA 1373
Cdd:PRK03918 649 LEELEKKYSEEEY---EELREEYLELSRELAGLRAELEELEKRREeikkTLEKLKEELEEREKAKKELEK-LEKALERVE 724
|
....*
gi 305632842 1374 QWRTK 1378
Cdd:PRK03918 725 ELREK 729
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
967-1867 |
4.54e-19 |
|
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: 94.65 E-value: 4.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 967 KVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAhqqtlDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEK 1046
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEET-----ENLAELIIDLEELKLQELKLKEQAKKALEYYQLKE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1047 KLRmdLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEI 1126
Cdd:pfam02463 218 KLE--LEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1127 EAERASRAKAEKQRSDLSRELEEISERLEEAggatSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAE 1206
Cdd:pfam02463 296 EELKSELLKLERRKVDDEEKLKESEKEKKKA----EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQL 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1207 LGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQT 1286
Cdd:pfam02463 372 EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1287 ESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALS 1366
Cdd:pfam02463 452 ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRL 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1367 KANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEhVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAAL 1446
Cdd:pfam02463 532 GDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT-ELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDK 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1447 DKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNA-----YEESLDQLETLKRENKNLQQEISDLTEQIA 1521
Cdd:pfam02463 611 ATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEeglaeKSEVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1522 EGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESM 1601
Cdd:pfam02463 691 KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELS 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1602 QstldaeirsrnDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRTQEDLKEQLAMVERR 1681
Cdd:pfam02463 771 L-----------KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELA 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1682 ANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDisqmQGEMEDILQEARNAEEKAKK 1761
Cdd:pfam02463 840 LELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKE----KEEKKELEEESQKLNLLEEK 915
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1762 AITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNAEAV 1841
Cdd:pfam02463 916 ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDEL 995
|
890 900
....*....|....*....|....*.
gi 305632842 1842 KGLRKHERRVKELTYQTEEDRKNILR 1867
Cdd:pfam02463 996 EKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1626-1927 |
1.93e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.31 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1626 LNEMEIQLNHANRMAAEALRnYRNTQGILKDTQLHLddALRTQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKI 1705
Cdd:COG1196 195 LGELERQLEPLERQAEKAER-YRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1706 AEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLER 1785
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1786 MKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEgEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNI 1865
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR-AAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 305632842 1866 LRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLRVK 1927
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1171-1915 |
2.35e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.51 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1171 REAEFQKMRRDLEEATLQHEATAATLRKKHADSVAElgeqidnlqrvkqklEKEKSEMKMEIDDLASNVETVSKAKG--N 1248
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAE---------------EARKAEEAKKKAEDARKAEEARKAEDarK 1141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1249 LEKMCRTLEDQVSELKSKEEEQQRLINDLTAQRGRlqteSGEFSRQLDEkdalVSQLSRGKQAFTQQIEELKRQLEEEIK 1328
Cdd:PTZ00121 1142 AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAK----KAEAARKAEE----VRKAEELRKAEDARKAEAARKAEEERK 1213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1329 AKNALAHALQSSRHDCDLLREQYEEEQESK-AELQRAlskaNTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEH 1407
Cdd:PTZ00121 1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKkAEEERN----NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEK 1289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1408 VEAVNAKCASLEKTKQRLQNEVEDLMLDVErtnaacaaLDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELfk 1487
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEAKKKAEEAKKADE--------AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEA-- 1359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1488 mkNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKilriql 1567
Cdd:PTZ00121 1360 --EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK------ 1431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1568 elnqvKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNY 1647
Cdd:PTZ00121 1432 -----KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA 1506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1648 RNTQgilKDTQLHLDDALRTQEDLKEqlAMVERRANLLQAEIEELRA-TLEQTERSRKIAEQELLDASERVQllHTQNTS 1726
Cdd:PTZ00121 1507 EAKK---KADEAKKAEEAKKADEAKK--AEEAKKADEAKKAEEKKKAdELKKAEELKKAEEKKKAEEAKKAE--EDKNMA 1579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1727 LINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAiTDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDL-QLRLDEAE 1805
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA-EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeELKKAEEE 1658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1806 QLALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQ 1885
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
|
730 740 750
....*....|....*....|....*....|...
gi 305632842 1886 AEEAE---EQSNTNLAKFRKLQHELEEAEERAD 1915
Cdd:PTZ00121 1739 AEEDKkkaEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
848-1328 |
3.79e-18 |
|
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: 91.24 E-value: 3.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 848 ETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQL------IKTKIQ--- 918
Cdd:TIGR04523 135 ENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLelllsnLKKKIQknk 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 919 -LEAKI-----------KEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKekhaTENKVKNLTEEM 986
Cdd:TIGR04523 215 sLESQIselkkqnnqlkDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ----NNKKIKELEKQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 987 AGLDETIAKLTKEKKalQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLA 1066
Cdd:TIGR04523 291 NQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEK 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1067 QESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRE 1146
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1147 LEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATL------RKKHADSVAELGEQIDNLQRVKQK 1220
Cdd:TIGR04523 449 DSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELkklneeKKELEEKVKDLTKKISSLKEKIEK 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1221 LEKEKSEMKMEIDDLASNVETV--SKAKGNLEKMCRTLEDQVSELK-------SKEEEQQRLINDLTAQRGRLqtesgef 1291
Cdd:TIGR04523 529 LESEKKEKESKISDLEDELNKDdfELKKENLEKEIDEKNKEIEELKqtqkslkKKQEEKQELIDQKEKEKKDL------- 601
|
490 500 510
....*....|....*....|....*....|....*..
gi 305632842 1292 SRQLDEKDALVSQLSRGkqafTQQIEELKRQLEEEIK 1328
Cdd:TIGR04523 602 IKEIEEKEKKISSLEKE----LEKAKKENEKLSSIIK 634
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1013-1797 |
4.76e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 91.74 E-value: 4.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1013 DLQAEEDKVNTLT--KAKTKLEQQVDDLEGSLEQEKKLrmdlERAKRKLEgDLKLAQESIMdiENEKQQLDEKLKKKEFE 1090
Cdd:PTZ00121 1080 DFDAKEDNRADEAteEAFGKAEEAKKTETGKAEEARKA----EEAKKKAE-DARKAEEARK--AEDARKAEEARKAEDAK 1152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1091 ISNLQSKIED----EQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEK-QRSDLSRELEEISERLEEAGGATSAQI 1165
Cdd:PTZ00121 1153 RVEIARKAEDarkaEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAaRKAEEERKAEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1166 EMNKKREAEFQKMR--RDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQR---VKQKLEKEKSEMKMEIDDLASNVE 1240
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEeeRNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeeKKKADEAKKAEEKKKADEAKKKAE 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1241 TVSKAKgNLEKMCRTLEDQVSELKSKEEEQQRlindlTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQafTQQIEELK 1320
Cdd:PTZ00121 1313 EAKKAD-EAKKKAEEAKKKADAAKKKAEEAKK-----AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA--KKKADAAK 1384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1321 RQLEEEIKAKNALAHAlQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAiqrteelEEAKKKLAQR 1400
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKA-EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA-------DEAKKKAEEA 1456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1401 LQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKilAEWKQKYEETHAELEASQKEARS 1480
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK--ADEAKKAEEAKKADEAKKAEEAK 1534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1481 LGTELFKMknayEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEK--IKKQVEQEKCELQAALEEAEASLEHE 1558
Cdd:PTZ00121 1535 KADEAKKA----EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaeEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1559 EGKilriQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDlnemeiqlnhanR 1638
Cdd:PTZ00121 1611 EAK----KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED------------K 1674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1639 MAAEALRNYRNTQGILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSrkiAEQElldaservq 1718
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE---AEED--------- 1742
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305632842 1719 llhtqntslintKKKLEtDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLErmkknMEQTVKDL 1797
Cdd:PTZ00121 1743 ------------KKKAE-EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME-----VDKKIKDI 1803
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
848-1637 |
8.87e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.59 E-value: 8.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 848 ETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQlEAKIKEVT 927
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAE-DARKAEEA 1169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 928 ERAEDEEEINAeltAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAgldETIAKLTKEKKALQEAH 1007
Cdd:PTZ00121 1170 RKAEDAKKAEA---ARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKA---EAVKKAEEAKKDAEEAK 1243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1008 QQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEgsleqEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKK 1087
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAE-----EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD 1318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1088 EfeisnLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatSAQIEM 1167
Cdd:PTZ00121 1319 E-----AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA----KKKAEE 1389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1168 NKKREAEFQKMRRDLEEATLQHEATAAtlrKKHADSVAELGEQIDNLQRVKQKLEKEKsemkmEIDDLASNVETVSKAKg 1247
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAA---KKKADEAKKKAEEKKKADEAKKKAEEAK-----KADEAKKKAEEAKKAE- 1460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1248 NLEKMCRTlEDQVSELKSKEEEQQRlindltaqRGRLQTESGEFSRQLDEkdalvsqlSRGKQAFTQQIEELKRQlEEEI 1327
Cdd:PTZ00121 1461 EAKKKAEE-AKKADEAKKKAEEAKK--------ADEAKKKAEEAKKKADE--------AKKAAEAKKKADEAKKA-EEAK 1522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1328 KAKNALAHALQSSRHDCDLLREQYEEEQESKAE-LQRALSKANTEVAQWRTKYETDAIQRTEEL---EEAKKKLAQRLQA 1403
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEeLKKAEEKKKAEEAKKAEEDKNMALRKAEEAkkaEEARIEEVMKLYE 1602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1404 AEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLgt 1483
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA-- 1680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1484 elfkmKNAYEESLDQLETLKREnknlqqeisdlteqiAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHeegkiL 1563
Cdd:PTZ00121 1681 -----KKAEEDEKKAAEALKKE---------------AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE-----A 1735
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305632842 1564 RIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHAN 1637
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFAN 1809
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
847-1459 |
1.00e-17 |
|
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: 90.13 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 847 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEV 926
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 927 TERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKN-------LTEEMAGLDETIAKLTKE 999
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGgraveevLKASIQGVHGTVAQLGSV 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1000 K----KALQEAHQQTLDDLQAEEDKVNT----LTKAK----------TKLEQQVDDLEGSLEQ------------EKKLR 1049
Cdd:TIGR02169 534 GeryaTAIEVAAGNRLNNVVVEDDAVAKeaieLLKRRkagratflplNKMRDERRDLSILSEDgvigfavdlvefDPKYE 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1050 -------------MDLERAKR--------KLEGDL--------------KLAQESIMDIENEKQQLDEKLKKKEFEISNL 1094
Cdd:TIGR02169 614 pafkyvfgdtlvvEDIEAARRlmgkyrmvTLEGELfeksgamtggsrapRGGILFSRSEPAELQRLRERLEGLKRELSSL 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1095 QSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatsaqIEMNKKREAE 1174
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV-------KSELKELEAR 766
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1175 FQKMRRDLEEATLQHEATAATLRkkhadsvaelGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCR 1254
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLS----------HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1255 TLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEeikaknala 1334
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE--------- 907
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1335 halqssrhdcdlLREQYEEEQESKAELQRALSKANTEVAQ-----WRTKYETDAIQRTEELEEAKKKLAQRLQA------ 1403
Cdd:TIGR02169 908 ------------LEAQIEKKRKRLSELKAKLEALEEELSEiedpkGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnm 975
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 305632842 1404 -AEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTN-----AACAALDKKQRNFDKILAE 1459
Cdd:TIGR02169 976 lAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEkkkreVFMEAFEAINENFNEIFAE 1037
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
883-1429 |
1.00e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 90.10 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 883 TLLKEKNDLQLQVQAEAEGLADAEercdqLIKTKIQLEAKIKEVTERAE--DEEEINAELT--------AKKRKLEDECS 952
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEKEEKD-----LHERLNGLESELAELDEEIEryEEQREQARETrdeadevlEEHEERREELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 953 ELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKkALQEAHQQTLDDLQAEedkvntltkaktkLE 1032
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA-GLDDADAEAVEARREE-------------LE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1033 QQVDDLEGSLEQEkklRMDLERAKRKLEGdlklAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKI 1112
Cdd:PRK02224 321 DRDEELRDRLEEC---RVAAQAHNEEAES----LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1113 KELqarieeleeeieaerasrakaEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEA-TLQHEA 1191
Cdd:PRK02224 394 EEL---------------------RERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAeALLEAG 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1192 TAATLRKK-----HADSVAELGEQIDnlqrvkqKLEKEKSEMKMEIDDLASNVETVSKAKgNLEKMCRTLEDQVSELKSK 1266
Cdd:PRK02224 453 KCPECGQPvegspHVETIEEDRERVE-------ELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEEL 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1267 EEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEE---EIKAKNALAHALQssrhd 1343
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAElkeRIESLERIRTLLA----- 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1344 cdlLREQYEEEQESKAELQRALSKANTEvaqwRTKYETDAIQRTEELEE-----AKKKLAQRLQAAEEHVEAVNAKCASL 1418
Cdd:PRK02224 600 ---AIADAEDEIERLREKREALAELNDE----RRERLAEKRERKRELEAefdeaRIEEAREDKERAEEYLEQVEEKLDEL 672
|
570
....*....|.
gi 305632842 1419 EKTKQRLQNEV 1429
Cdd:PRK02224 673 REERDDLQAEI 683
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
841-1704 |
1.80e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 89.26 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 841 KPLLKSAETEKEMATMKEefqktKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERcdQLIKTKIQLE 920
Cdd:pfam02463 150 MKPERRLEIEEEAAGSRL-----KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEY--YQLKEKLELE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 921 AKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEK 1000
Cdd:pfam02463 223 EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSEL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1001 KALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAK---RKLEGDLKLAQESIMDIENEK 1077
Cdd:pfam02463 303 LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEeelEKLQEKLEQLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1078 QQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEA 1157
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1158 GGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLAS 1237
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1238 NVETVSKAKGNLEKMCRTLEDQVSEL-----------------KSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDA 1300
Cdd:pfam02463 543 VAISTAVIVEVSATADEVEERQKLVRaltelplgarklrllipKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRA 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1301 LVSQLSRGKQAFTQQIEELKRQLEEEIKAKnALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYE 1380
Cdd:pfam02463 623 KVVEGILKDTELTKLKESAKAKESGLRKGV-SLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEI 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1381 TDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVErtnaacaALDKKQRNFDKILAEW 1460
Cdd:pfam02463 702 KKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK-------KEEKEEEKSELSLKEK 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1461 KQKYEETHAELEASQKEARSLGTEL-FKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQ 1539
Cdd:pfam02463 775 ELAEEREKTEKLKVEEEKEEKLKAQeEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1540 EKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKR--NHIRIVESMQSTLDAEIRSRNDAIR 1617
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQklNLLEEKENEIEERIKEEAEILLKYE 934
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1618 LKKKMEGDLNEMEIQLNHANRMAAEaLRNYRNTQGILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEELRATLE 1697
Cdd:pfam02463 935 EEPEELLLEEADEKEKEENNKEEEE-ERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIE 1013
|
....*..
gi 305632842 1698 QTERSRK 1704
Cdd:pfam02463 1014 ETCQRLK 1020
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1390-1930 |
2.55e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.84 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1390 LEEA--------KKKLA-QRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDlmldvertnAACA-ALDKKQRNFDKILae 1459
Cdd:COG1196 161 IEEAagiskykeRKEEAeRKLEATEENLERLEDILGELERQLEPLERQAEK---------AERYrELKEELKELEAEL-- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1460 WKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQ 1539
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1540 EKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDR---KIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAI 1616
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEaeeELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1617 RLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEELRATL 1696
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1697 EQTERSRKIAEQELLDASERVQLLHTQ-----NTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAIT------- 1764
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLleaeaDYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAalaaalq 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1765 --------DAAMMAEELKKEQD---TSAHLERMKKNMEQTVKDLQLRLDEA---------------------------EQ 1806
Cdd:COG1196 550 nivveddeVAAAAIEYLKAAKAgraTFLPLDKIRARAALAAALARGAIGAAvdlvasdlreadaryyvlgdtllgrtlVA 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1807 LALKGGKKQIQKLEARVRELEGEVESEQKRNAEAvkglrkhERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQA 1886
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT-------GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 305632842 1887 EEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLRVKSRE 1930
Cdd:COG1196 703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
869-1588 |
3.00e-17 |
|
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: 88.15 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 869 KSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLE 948
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 949 DECSELKKDIDDLELTLAKVEKEKHATE-------NKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKV 1021
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKknidkflTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1022 NTLTKAKTKLEQQVDDLEGSLEQEKKLR---MDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKkkefEISNLQSKI 1098
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQKNKSLEsqiSELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN----QLKDEQNKI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1099 EDeqalgiQLQKKIKELQarieeleeeieaerasraKAEKQRSDLSRELEEISERLEEAGgaTSAQIEMNKKREAEFQKM 1178
Cdd:TIGR04523 266 KK------QLSEKQKELE------------------QNNKKIKELEKQLNQLKSEISDLN--NQKEQDWNKELKSELKNQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1179 RRDLEEATLQheataatlRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLED 1258
Cdd:TIGR04523 320 EKKLEEIQNQ--------ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLES 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1259 QVSELKSKEEEQQRLINDLTAQRGRLQTesgefsrqldEKDALVSQLSRGKQAFTQQIEELKRqLEEEIKAKNALAHALQ 1338
Cdd:TIGR04523 392 QINDLESKIQNQEKLNQQKDEQIKKLQQ----------EKELLEKEIERLKETIIKNNSEIKD-LTNQDSVKELIIKNLD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1339 SSRhdcdllreqyeEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASL 1418
Cdd:TIGR04523 461 NTR-----------ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1419 EKTKQRLQNEVEDLMLDVErtnaacaaldkkqrnfdkilaewKQKYEETHAELEasqKEARSLGTELFKMKNAYEESLDQ 1498
Cdd:TIGR04523 530 ESEKKEKESKISDLEDELN-----------------------KDDFELKKENLE---KEIDEKNKEIEELKQTQKSLKKK 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1499 LETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVK---SE 1575
Cdd:TIGR04523 584 QEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRnkwPE 663
|
730
....*....|...
gi 305632842 1576 VDRKIAEKDEEID 1588
Cdd:TIGR04523 664 IIKKIKESKTKID 676
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1077-1853 |
3.49e-17 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 88.25 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1077 KQQLDEKLKKKEFEISNLQSKIEDEQALG-----------IQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSR 1145
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHekqkfylrqsvIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1146 ELEEISERLEEAGGATSAQIEMNKK----REAEFQKMRR---DLEEATLQHEATAATLRKKHADSvaeLGEQIDNLQRvk 1218
Cdd:pfam15921 153 ELEAAKCLKEDMLEDSNTQIEQLRKmmlsHEGVLQEIRSilvDFEEASGKKIYEHDSMSTMHFRS---LGSAISKILR-- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1219 qKLEKEKSEMKMEIDDLASNVETV-SKAKGNLEKMCRTLEDQVSELKSKEEEQqrlINDLTAQRGRLQTESGEFSRQLDe 1297
Cdd:pfam15921 228 -ELDTEISYLKGRIFPVEDQLEALkSESQNKIELLLQQHQDRIEQLISEHEVE---ITGLTEKASSARSQANSIQSQLE- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1298 kdaLVSQLSRGKQA-FTQQIEELKRQLEEeikaknalahaLQSSrhdcdlLREQYEEEQESKAELQRALSKANTEVAQWR 1376
Cdd:pfam15921 303 ---IIQEQARNQNSmYMRQLSDLESTVSQ-----------LRSE------LREAKRMYEDKIEELEKQLVLANSELTEAR 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1377 TKYETDAiQRTEELEEAKKKLAQRLQAAEEHVeavnakcaSLEKTKQR---------------LQNEVEDLMLDVERTNA 1441
Cdd:pfam15921 363 TERDQFS-QESGNLDDQLQKLLADLHKREKEL--------SLEKEQNKrlwdrdtgnsitidhLRRELDDRNMEVQRLEA 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1442 ACAALDKK-QRNFDKILAEWKQKYEethaeleaSQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQI 1520
Cdd:pfam15921 434 LLKAMKSEcQGQMERQMAAIQGKNE--------SLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASL 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1521 AEGGKRIH----ELEKIKKQVEQEKCELQaaleeaeaSLEHEEGKILRIQLELNQVKSEvdrkIAEKDEEIDQLKRNhir 1596
Cdd:pfam15921 506 QEKERAIEatnaEITKLRSRVDLKLQELQ--------HLKNEGDHLRNVQTECEALKLQ----MAEKDKVIEILRQQ--- 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1597 iVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHL-------DDALRTQE 1669
Cdd:pfam15921 571 -IENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKvklvnagSERLRAVK 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1670 DLKEQlamverRANLLQaEIEELRATLEQTERSRKIAEQELLDASERVQLlhtqntslinTKKKLETDISQMQGEMEDIL 1749
Cdd:pfam15921 650 DIKQE------RDQLLN-EVKTSRNELNSLSEDYEVLKRNFRNKSEEMET----------TTNKLKMQLKSAQSELEQTR 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1750 QEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQlrldeAEQLALKGGKKQIQKlearvrELEgE 1829
Cdd:pfam15921 713 NTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNAN-----KEKHFLKEEKNKLSQ------ELS-T 780
|
810 820
....*....|....*....|....
gi 305632842 1830 VESEQKRNAEAVKGLRKHERRVKE 1853
Cdd:pfam15921 781 VATEKNKMAGELEVLRSQERRLKE 804
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1074-1634 |
3.59e-17 |
|
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: 87.77 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1074 ENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISER 1153
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1154 LEeaggatsAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADsVAELGEQIDNLQRVKQKLEKEKSEMKMEID 1233
Cdd:TIGR04523 112 IK-------NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1234 DLASNVETVSKAKGNLEKMC----------RTLEDQVSELKSK--------EEEQQRL-------------INDLTAQRG 1282
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELLLsnlkkkiqknKSLESQISELKKQnnqlkdniEKKQQEInektteisntqtqLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1283 RLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKakNALAHALQSSRHDCDLLREQYEEEQESKAELQ 1362
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWN--KELKSELKNQEKKLEEIQNQISQNNKIISQLN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1363 RALSKANTEvaqwRTKYETDAIQRTEELEEAKKK------------------------LAQRLQAAEEHVEAVNAKCASL 1418
Cdd:TIGR04523 342 EQISQLKKE----LTNSESENSEKQRELEEKQNEieklkkenqsykqeiknlesqindLESKIQNQEKLNQQKDEQIKKL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1419 EKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQ 1498
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1499 LETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHE--EGKILRIQLELNQVKSE- 1575
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTq 577
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305632842 1576 --VDRKIAEKDEEIDQLKRNhIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLN 1634
Cdd:TIGR04523 578 ksLKKKQEEKQELIDQKEKE-KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
901-1538 |
9.46e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 86.66 E-value: 9.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 901 GLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLED---ECSELKKDIDDLELTLAKVEKEKhateN 977
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlrEINEISSELPELREELEKLEKEV----K 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 978 KVKNLTEEMAGLDETIAKLTKEKKALQEahqqtldDLQAEEDKVNTLTKAKTKLEQQVDDLEgSLEQEKKLRMDLERAKR 1057
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEE-------KIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1058 KLEgdlklaqesimdienekqqldEKLKKKEFEISNLQSKIEDeqalgiqLQKKIKELqarieeleeeieaerasrakae 1137
Cdd:PRK03918 304 EYL---------------------DELREIEKRLSRLEEEING-------IEERIKEL---------------------- 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1138 kqrSDLSRELEEISERLEEAggatsaqiemnKKREAEFQKMRRDLEEAtLQHEATAATLRKKHAD-SVAELGEQIDNLQR 1216
Cdd:PRK03918 334 ---EEKEERLEELKKKLKEL-----------EKRLEELEERHELYEEA-KAKKEELERLKKRLTGlTPEKLEKELEELEK 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1217 VKQKLEKE-------KSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEdqvselkskEEEQQRLINDLTAQRGRLQTESG 1289
Cdd:PRK03918 399 AKEEIEEEiskitarIGELKKEIKELKKAIEELKKAKGKCPVCGRELT---------EEHRKELLEEYTAELKRIEKELK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1290 EFSRQLD----EKDALVSQLSRGKQAFTQ-----QIEELKRQLE----EEIKAKNALAHALQSS----RHDCDLLREQYE 1352
Cdd:PRK03918 470 EIEEKERklrkELRELEKVLKKESELIKLkelaeQLKELEEKLKkynlEELEKKAEEYEKLKEKliklKGEIKSLKKELE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1353 EEQE---SKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAqrlQAAEEHVEAVNAkcaslEKTKQRLQNEV 1429
Cdd:PRK03918 550 KLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELE---PFYNEYLELKDA-----EKELEREEKEL 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1430 EDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYeethaeleaSQKEARSLGTELFKMKNAYEESLDQLETLKRENKNL 1509
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKY---------SEEEYEELREEYLELSRELAGLRAELEELEKRREEI 692
|
650 660
....*....|....*....|....*....
gi 305632842 1510 QQEISDLTEQIAEGGKRIHELEKIKKQVE 1538
Cdd:PRK03918 693 KKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1204-1698 |
1.32e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 83.17 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1204 VAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKmcrtLEDQVSELKSKEEEQQRLINDLTAQRGR 1283
Cdd:PRK02224 215 LAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIED----LRETIAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1284 LQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQR 1363
Cdd:PRK02224 291 LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1364 ALSKANTEVAQWRTKYE------TDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQN---EVEDLM- 1433
Cdd:PRK02224 371 ELEEAREAVEDRREEIEeleeeiEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARErveEAEALLe 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1434 --------LDVERTNAACAALDKKQRNFDkiLAEWKQKYEETHAELEASQKEARSLgtelfkmknayEESLDQLETLKRE 1505
Cdd:PRK02224 451 agkcpecgQPVEGSPHVETIEEDRERVEE--LEAELEDLEEEVEEVEERLERAEDL-----------VEAEDRIERLEER 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1506 NKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDR------- 1578
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESlerirtl 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1579 --KIAEKDEEIDQL--KRNHIRIVESMQSTLDAEIRSRndairlKKKMEGDLNEMEIQLNHANRMAAEA--------LRN 1646
Cdd:PRK02224 598 laAIADAEDEIERLreKREALAELNDERRERLAEKRER------KRELEAEFDEARIEEAREDKERAEEyleqveekLDE 671
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 305632842 1647 YRNTQGILKDTQLHLDDALRTQEDLKEQLAMVERR----------ANLLQAEIEELRATLEQ 1698
Cdd:PRK02224 672 LREERDDLQAEIGAVENELEELEELRERREALENRvealealydeAEELESMYGDLRAELRQ 733
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1027-1629 |
3.78e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.62 E-value: 3.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1027 AKTKLEQQVDDLEGSLEQ-----EKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDE 1101
Cdd:PRK02224 174 ARLGVERVLSDQRGSLDQlkaqiEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1102 QalgiQLQKKIKELQARIeeleeeieaerasrAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRD 1181
Cdd:PRK02224 254 E----TLEAEIEDLRETI--------------AETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEAR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1182 LEEATLQHEATAATLRKKHADsVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAkgnlekmCRTLEDQVS 1261
Cdd:PRK02224 316 REELEDRDEELRDRLEECRVA-AQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREA-------VEDRREEIE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1262 ELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEElKRQLEEEIKAKNAlAHALQSSR 1341
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE-AEALLEAGKCPEC-GQPVEGSP 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1342 HDCDLlreqyEEEQESKAELQRALSKANTEVAQWRTKYET-----DAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCA 1416
Cdd:PRK02224 466 HVETI-----EEDRERVEELEAELEDLEEEVEEVEERLERaedlvEAEDRIERLEERREDLEELIAERRETIEEKRERAE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1417 SLEKTKQRLQNEVEdlmldvERTNAACAALDKKQRNFDKIlAEWKQKYEETHAELEASQKEARSLgtelfkmkNAYEESL 1496
Cdd:PRK02224 541 ELRERAAELEAEAE------EKREAAAEAEEEAEEAREEV-AELNSKLAELKERIESLERIRTLL--------AAIADAE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1497 DQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKikkQVEQEKCE-LQAALEEAEASLEHEEGKILR-------IQLE 1568
Cdd:PRK02224 606 DEIERLREKREALAELNDERRERLAEKRERKRELEA---EFDEARIEeAREDKERAEEYLEQVEEKLDElreerddLQAE 682
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1569 LNQVKSEVDRkIAEKDEEIDQLKRNHIRI---------VESMQSTLDAEIRSRNDAirlkkKMEGDLNEM 1629
Cdd:PRK02224 683 IGAVENELEE-LEELRERREALENRVEALealydeaeeLESMYGDLRAELRQRNVE-----TLERMLNET 746
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
900-1837 |
9.30e-15 |
|
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: 80.40 E-value: 9.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 900 EGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAEL-TAKKRKLEDECSELKKDIDDLELTLAKVEKEKHatenk 978
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELkLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL----- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 979 vknlteemagLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRK 1058
Cdd:pfam02463 235 ----------NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1059 LEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEK 1138
Cdd:pfam02463 305 LERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1139 QRSDLSRELEEISERLEEaggatsaqiemnKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVK 1218
Cdd:pfam02463 385 RLSSAAKLKEEELELKSE------------EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1219 QKLEKEKSEMKmeiddlasnvetvskakgnlekmCRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEK 1298
Cdd:pfam02463 453 LEKQELKLLKD-----------------------ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGL 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1299 DALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALqssrhdCDLLREQYEEEQESKAELQRALSKANTEVAQWRTK 1378
Cdd:pfam02463 510 KVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTA------VIVEVSATADEVEERQKLVRALTELPLGARKLRLL 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1379 YETDaiqRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILA 1458
Cdd:pfam02463 584 IPKL---KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAE 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1459 EWKQKYEETHAELEASQKEARslgtelfkmKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVE 1538
Cdd:pfam02463 661 KSEVKASLSELTKELLEIQEL---------QEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ 731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1539 QEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRsRNDAIRL 1618
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL-RALEEEL 810
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1619 KKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEELRATLEQ 1698
Cdd:pfam02463 811 KEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELES 890
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1699 TERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAItdaamMAEELKKEQD 1778
Cdd:pfam02463 891 KEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK-----EEEEERNKRL 965
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 305632842 1779 TSAHLERMKKNMEQtvkDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRN 1837
Cdd:pfam02463 966 LLAKEELGKVNLMA---IEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
839-1275 |
2.06e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.41 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 839 KIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQlqvqaEAEGLADAEERCDQLIKTKIQ 918
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK-----KAEEAKKAEEDKNMALRKAEE 1585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 919 L----EAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDiddlELTLAKVEKEKHATENKVKNLTEEMAGLDETIA 994
Cdd:PTZ00121 1586 AkkaeEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA----EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 995 KLTKEKKALQEAHQQTLDDLQAEEDkvntltkaKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIE 1074
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEED--------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1075 NEKQQLDEKLKKKEfeisnlQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEI---S 1151
Cdd:PTZ00121 1734 EAKKEAEEDKKKAE------EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIfdnF 1807
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1152 ERLEEAGGATSAQIEMNKKRE-------AEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKE 1224
Cdd:PTZ00121 1808 ANIIEGGKEGNLVINDSKEMEdsaikevADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEA 1887
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 305632842 1225 KSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLIN 1275
Cdd:PTZ00121 1888 DEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEIIK 1938
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
848-1405 |
2.13e-14 |
|
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: 79.39 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 848 ETEKEMATMKEEFQKTKDELaksEAKRKELEEKMVTLLKEKNDLQLQVQAEAE-GLADAEERCDQLIKTKIQLEAKIKEV 926
Cdd:pfam15921 228 ELDTEISYLKGRIFPVEDQL---EALKSESQNKIELLLQQHQDRIEQLISEHEvEITGLTEKASSARSQANSIQSQLEII 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 927 TERAEDE---------------EEINAELTAKKRKLEDECSELKKD--IDDLELTLAKVEKEKHATENkvKNLTEEMAGL 989
Cdd:pfam15921 305 QEQARNQnsmymrqlsdlestvSQLRSELREAKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQLQKL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 990 detIAKLTKEKKALQEAHQQT--------------------LDDLQAEEDKVNTLTKA-----KTKLEQQVDDLEG---S 1041
Cdd:pfam15921 383 ---LADLHKREKELSLEKEQNkrlwdrdtgnsitidhlrreLDDRNMEVQRLEALLKAmksecQGQMERQMAAIQGkneS 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1042 LEQEKKLRMDLERAKRKLEG----------DLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEdeqaLGIQLQKK 1111
Cdd:pfam15921 460 LEKVSSLTAQLESTKEMLRKvveeltakkmTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVD----LKLQELQH 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1112 IKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEA 1191
Cdd:pfam15921 536 LKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDK 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1192 TAATLRKKHAdSVAEL-----------GEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNL----EKMCRTL 1256
Cdd:pfam15921 616 KDAKIRELEA-RVSDLelekvklvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFrnksEEMETTT 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1257 EDQVSELKSKEEEQQRLINDLTAQRGR----LQTESGeFSRQLDEK----DALVSQLSRGKQAFTQQ------IEELKRQ 1322
Cdd:pfam15921 695 NKLKMQLKSAQSELEQTRNTLKSMEGSdghaMKVAMG-MQKQITAKrgqiDALQSKIQFLEEAMTNAnkekhfLKEEKNK 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1323 LEEEIKA----KNALAHALQssrhdcdLLREQYEEEQESKAELQRALSKANTEVAQWRtkyetDAIQRTEElEEAKKKLA 1398
Cdd:pfam15921 774 LSQELSTvateKNKMAGELE-------VLRSQERRLKEKVANMEVALDKASLQFAECQ-----DIIQRQEQ-ESVRLKLQ 840
|
....*..
gi 305632842 1399 QRLQAAE 1405
Cdd:pfam15921 841 HTLDVKE 847
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
908-1599 |
2.14e-14 |
|
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: 79.24 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 908 RCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHAT----ENKVKNLT 983
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERkqvlEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 984 EEMAGLDETIAKLTKEKKALQEAH--QQTLDDLQAEEDKVNTLTKAKTKLEQqvddlegsleqekklRMDLERAKRKLEG 1061
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRAQEAVLEETQE---------------RINRARKAAPLAA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1062 DLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQlQKKIKELQARIEELEEEIEAERASRAKAEKQRS 1141
Cdd:TIGR00618 298 HIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ-RRLLQTLHSQEIHIRDAHEVATSIREISCQQHT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1142 DLS--RELEEISERLEEAGGATSAQIE-----------------------MNKKREAEFQKMRRDLEEATLQHEATAATL 1196
Cdd:TIGR00618 377 LTQhiHTLQQQKTTLTQKLQSLCKELDilqreqatidtrtsafrdlqgqlAHAKKQQELQQRYAELCAAAITCTAQCEKL 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1197 RKKHADSVA----ELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSK----------AKGNLEKMCRTLEDQVSE 1262
Cdd:TIGR00618 457 EKIHLQESAqslkEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGscihpnparqDIDNPGPLTRRMQRGEQT 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1263 LKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQA---FTQQIEELKRQLEEEIKAKNALAhalqs 1339
Cdd:TIGR00618 537 YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDipnLQNITVRLQDLTEKLSEAEDMLA----- 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1340 srhdcDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLE 1419
Cdd:TIGR00618 612 -----CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQ 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1420 KTKQRLQNEVEDLmldvERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEA-------SQKEARSLG-TELFKMKNA 1491
Cdd:TIGR00618 687 SEKEQLTYWKEML----AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAredalnqSLKELMHQArTVLKARTEA 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1492 YEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQ 1571
Cdd:TIGR00618 763 HFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSA 842
|
730 740 750
....*....|....*....|....*....|.
gi 305632842 1572 VKSEVDR---KIAEKDEEIDQLKRNHIRIVE 1599
Cdd:TIGR00618 843 TLGEITHqllKYEECSKQLAQLTQEQAKIIQ 873
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
847-1613 |
3.33e-14 |
|
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: 78.86 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 847 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEV 926
Cdd:pfam02463 275 KEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 927 TERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEA 1006
Cdd:pfam02463 355 EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1007 HQ--QTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKL 1084
Cdd:pfam02463 435 EEesIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1085 KKKEFEISNLQSKIEDEQALGIQLQKkiKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQ 1164
Cdd:pfam02463 515 LIKDGVGGRIISAHGRLGDLGVAVEN--YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLK 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1165 IEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIdnLQRVKQKLEKEKSEMKMEIDDLASNVETVSK 1244
Cdd:pfam02463 593 SIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKE--SAKAKESGLRKGVSLEEGLAEKSEVKASLSE 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1245 AKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTAQR--GRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQ 1322
Cdd:pfam02463 671 LTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRekEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEE 750
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1323 LEEEIKAKNALAHALQSSRHDCDLLREQYEEEQE--SKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQR 1400
Cdd:pfam02463 751 EEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEklKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKI 830
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1401 LQAAEEHVEAVnakcaSLEKTKQRLQNEVEDLMLDVERTNAACAA---LDKKQRNFDKILAEWKQKYEETHAELEASQKE 1477
Cdd:pfam02463 831 KEEELEELALE-----LKEEQKLEKLAEEELERLEEEITKEELLQellLKEEELEEQKLKDELESKEEKEKEEKKELEEE 905
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1478 ARSLGTELFKMKnaYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIH--ELEKIKKQVEQEKCELQAALEEAEASL 1555
Cdd:pfam02463 906 SQKLNLLEEKEN--EIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNkeEEEERNKRLLLAKEELGKVNLMAIEEF 983
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 305632842 1556 EHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRN 1613
Cdd:pfam02463 984 EEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLE 1041
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
33-77 |
3.53e-14 |
|
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: 68.23 E-value: 3.53e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 305632842 33 DAKTSVFVAEPKESFVKGTIQSREGGKVTVKTEGGATLTVKDDQV 77
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1070-1592 |
4.39e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.18 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1070 IMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQalgiQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEE 1149
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIKRTE----NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1150 ISERLEEAGGATSAQIEMNKKREA------EFQKMRRDLEEATLQHEATAATLR--KKHADSVAELGEQIDNLQRVKQKL 1221
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKleekirELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1222 EKEKSEMKMEIDDLASNVETVSKAK---GNLEKMCRTLEDQVSELKSKEEEQQRlINDLTAQRGRLQTESGEFSrqLDEK 1298
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEE-AKAKKEELERLKKRLTGLT--PEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1299 DALVSQLSRGKQAFTQQIEEL---KRQLEEEIKAKNALAHALQSSRHDC-------------DLLREQYEEEQESKAELQ 1362
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKItarIGELKKEIKELKKAIEELKKAKGKCpvcgrelteehrkELLEEYTAELKRIEKELK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1363 RA------LSKANTEVAQWRTKYETDAIQRT--EELEEAKKKL----AQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVE 1430
Cdd:PRK03918 470 EIeekerkLRKELRELEKVLKKESELIKLKElaEQLKELEEKLkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1431 DLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNA---YEESLDQLETLKRENK 1507
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAekeLEREEKELKKLEEELD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1508 NLQQEISDLTEQIAEGGKRIHELEKI-----KKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDrKIAE 1582
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREK 708
|
570
....*....|
gi 305632842 1583 KDEEIDQLKR 1592
Cdd:PRK03918 709 AKKELEKLEK 718
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1386-1922 |
4.84e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.03 E-value: 4.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1386 RTEELEEakKKLAQRLQAAEEHVEAVNAKCASLEKTKQRlqneVEDLmldvERTNAACAALDKKQRNFDKilaewkQKYE 1465
Cdd:COG4913 214 REYMLEE--PDTFEAADALVEHFDDLERAHEALEDAREQ----IELL----EPIRELAERYAAARERLAE------LEYL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1466 ETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAE-GGKRIHELEKIKKQVEQEKCE- 1543
Cdd:COG4913 278 RAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEEr 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1544 ------LQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNH-------------IRIVESMQST 1604
Cdd:COG4913 358 errrarLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALrdlrrelreleaeIASLERRKSN 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1605 LDAEIRSRNDAIR--LKKKME-----GDLneMEIQLNHAN-RMAAE-ALRNYRNTqgILKDTQlHLDDALRTQEDLKeql 1675
Cdd:COG4913 438 IPARLLALRDALAeaLGLDEAelpfvGEL--IEVRPEEERwRGAIErVLGGFALT--LLVPPE-HYAAALRWVNRLH--- 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1676 amverranllqaeieeLRATLeQTERSRKIAEQELLDASERVQLLHtqntslintkkKLETDISQMQGEMEDILQE---- 1751
Cdd:COG4913 510 ----------------LRGRL-VYERVRTGLPDPERPRLDPDSLAG-----------KLDFKPHPFRAWLEAELGRrfdy 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1752 --ARNAEE--KAKKAITDAAMMAeelkkeQDTSAHlermKKNMEQTVK-DLQLRLDEAEQLALKggKKQIQKLEARVREL 1826
Cdd:COG4913 562 vcVDSPEElrRHPRAITRAGQVK------GNGTRH----EKDDRRRIRsRYVLGFDNRAKLAAL--EAELAELEEELAEA 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1827 EGEVE---------SEQKRNAEAVKGLRKHERRVKELTY---QTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSN 1894
Cdd:COG4913 630 EERLEaleaeldalQERREALQRLAEYSWDEIDVASAEReiaELEAELERLDASSDDLAALEEQLEELEAELEELEEELD 709
|
570 580
....*....|....*....|....*...
gi 305632842 1895 TNLAKFRKLQHELEEAEERADIAESQVN 1922
Cdd:COG4913 710 ELKGEIGRLEKELEQAEEELDELQDRLE 737
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1299-1913 |
5.31e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.03 E-value: 5.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1299 DALVSQLSRGKQAFtQQIEELKRQLE--EEIKAKNALAHALQSSRHDCDLLRE--QYEEEQESKAELQRALSKANTEVAQ 1374
Cdd:COG4913 228 DALVEHFDDLERAH-EALEDAREQIEllEPIRELAERYAAARERLAELEYLRAalRLWFAQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1375 WRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMldvERTNAACAALDKKQRNFD 1454
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE---ALLAALGLPLPASAEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1455 KILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEG-GKRIHEL--- 1530
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAlGLDEAELpfv 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1531 -EKIkkQVEQEKCELQAALEEAEASLEheegkiLRIQLElnqvksevDRKIAEKDEEIDQLK-RNHIRIvESMQSTLDAE 1608
Cdd:COG4913 464 gELI--EVRPEEERWRGAIERVLGGFA------LTLLVP--------PEHYAAALRWVNRLHlRGRLVY-ERVRTGLPDP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1609 IRSRNDAIRLKKKMEGDLNEMEIQLNH--ANRMA------AEALRNYRntQGILKDTQLH-------LDDALRTQEDL-- 1671
Cdd:COG4913 527 ERPRLDPDSLAGKLDFKPHPFRAWLEAelGRRFDyvcvdsPEELRRHP--RAITRAGQVKgngtrheKDDRRRIRSRYvl 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1672 ----KEQLAMVERRANLLQAEIEELRATLEQTERSRKiAEQELLDASERVQLLHTQntslintkkklETDISQMQGEMED 1747
Cdd:COG4913 605 gfdnRAKLAALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLAEYSWD-----------EIDVASAEREIAE 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1748 iLQEARNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTVKDLQLRLDEAEQlalkggkkQIQKLEARVRELE 1827
Cdd:COG4913 673 -LEAELERLDASSDDLAALEEQLEELEAELEE---LEEELDELKGEIGRLEKELEQAEE--------ELDELQDRLEAAE 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1828 GEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNIL-RLQDLVDKLQAKVKSYKRQAEEAEEQSNTNL-------AK 1899
Cdd:COG4913 741 DLARLELRALLEERFAAALGDAVERELRENLEERIDALRaRLNRAEEELERAMRAFNREWPAETADLDADLeslpeylAL 820
|
650
....*....|....*
gi 305632842 1900 FRKLQHE-LEEAEER 1913
Cdd:COG4913 821 LDRLEEDgLPEYEER 835
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1212-1935 |
6.94e-14 |
|
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: 77.70 E-value: 6.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1212 DNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLiNDLTAQRGRLQTESGEF 1291
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1292 SRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEikaknALAHALQSSRhdcdllrEQYEEEQESKAELQRALSKANTE 1371
Cdd:TIGR00618 266 RARIEELRAQEAVLEETQERINRARKAAPLAAHIK-----AVTQIEQQAQ-------RIHTELQSKMRSRAKLLMKRAAH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1372 VAQwrtkyetdaiqrtEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTK-------QRLQNEVEDLMLDVERTNAACA 1444
Cdd:TIGR00618 334 VKQ-------------QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIScqqhtltQHIHTLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1445 ALDKKQRNFDKILAE------WKQKYEETHAELEASQKEARSLgtelfkmKNAYEESLDQLETLKRENKNLQQEISDLTE 1518
Cdd:TIGR00618 401 ELDILQREQATIDTRtsafrdLQGQLAHAKKQQELQQRYAELC-------AAAITCTAQCEKLEKIHLQESAQSLKEREQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1519 QIAEGgKRIHELEKIKKQVEQEKCELQAALE-EAEASLEHEEGK-------------ILRIQLELNQVKSEVDRKIAEKD 1584
Cdd:TIGR00618 474 QLQTK-EQIHLQETRKKAVVLARLLELQEEPcPLCGSCIHPNPArqdidnpgpltrrMQRGEQTYAQLETSEEDVYHQLT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1585 EEIDQLKRNHIRIVESMQSTLDAEI---RSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHL 1661
Cdd:TIGR00618 553 SERKQRASLKEQMQEIQQSFSILTQcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1662 DDALRTQEDLKEQLAMVERRANLLQAEIEE-LRATLEQTERSRKIAEQELLDASERVQllhtqntSLINTKKKLETDISQ 1740
Cdd:TIGR00618 633 HLQQCSQELALKLTALHALQLTLTQERVREhALSIRVLPKELLASRQLALQKMQSEKE-------QLTYWKEMLAQCQTL 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1741 MQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKqiqkle 1820
Cdd:TIGR00618 706 LRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAE------ 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1821 arVRELEGEVESEQKRNAEAVKGLrkherrvKELTYQTEEDRKNILRLQDLVDKLQAKvksykrqaeeAEEQSNTNLAKF 1900
Cdd:TIGR00618 780 --LSHLAAEIQFFNRLREEDTHLL-------KTLEAEIGQEIPSDEDILNLQCETLVQ----------EEEQFLSRLEEK 840
|
730 740 750
....*....|....*....|....*....|....*
gi 305632842 1901 RKLQHELEEAEERADIAESQVNKLRVKSREVHTKV 1935
Cdd:TIGR00618 841 SATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1028-1611 |
9.20e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.26 E-value: 9.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1028 KTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLE--GDLKLAQESIMDIENEKQQLDEklkkkefeisnLQSKIEDEQAlg 1105
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEY-----------LRAALRLWFA-- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1106 iqlQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIE-----MNKKRE------AE 1174
Cdd:COG4913 287 ---QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEreierLERELEererrrAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1175 FQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNL----- 1249
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparll 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1250 ---EKMCRTLEDQVSEL---------KSKEEEQQ----RLINDltaQRGRLQTESGEFSRQLdekdALVSQLSRGKQAFT 1313
Cdd:COG4913 444 alrDALAEALGLDEAELpfvgelievRPEEERWRgaieRVLGG---FALTLLVPPEHYAAAL----RWVNRLHLRGRLVY 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1314 QQIEELKRQLEEEIKAKNALAHALQSSRHDC-DLLREQYEEEQ-----ESKAELQRAlSKANTE---VAQWRTKYE---- 1380
Cdd:COG4913 517 ERVRTGLPDPERPRLDPDSLAGKLDFKPHPFrAWLEAELGRRFdyvcvDSPEELRRH-PRAITRagqVKGNGTRHEkddr 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1381 ----------TDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQN--EVEDLMLDVERTNAACAALDK 1448
Cdd:COG4913 596 rrirsryvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEA 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1449 KQRNFDK---ILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISdlTEQIAEGGK 1525
Cdd:COG4913 676 ELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALLEE 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1526 RIHELeKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQV----KSEVDRKIAE------------------- 1582
Cdd:COG4913 754 RFAAA-LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREwpaeTADLDADLESlpeylalldrleedglpey 832
|
650 660
....*....|....*....|....*....
gi 305632842 1583 KDEEIDQLKRNHIRIVESMQSTLDAEIRS 1611
Cdd:COG4913 833 EERFKELLNENSIEFVADLLSKLRRAIRE 861
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
844-1729 |
9.95e-14 |
|
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: 77.14 E-value: 9.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 844 LKSAETEKEmatmkeefqktkdelakseakRKELEEKMvtllkekNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKI 923
Cdd:pfam01576 419 ARLSESERQ---------------------RAELAEKL-------SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 924 KEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKAL 1003
Cdd:pfam01576 471 QDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRL 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1004 QEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLegDLKLAQEsimdienekqqldek 1083
Cdd:pfam01576 551 QRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKF--DQMLAEE--------------- 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1084 lkkkefeiSNLQSKIEDEQalgiqlqkkikelqarieeleeeieaeraSRAKAEkqrsdlSREleeiserleeaggatsa 1163
Cdd:pfam01576 614 --------KAISARYAEER-----------------------------DRAEAE------ARE----------------- 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1164 qiemnkkREAEFQKMRRDLEEAtlqheataatlrkkhadsvaelgeqidnlQRVKQKLEKEKSEMKMEIDDLASNVETVS 1243
Cdd:pfam01576 634 -------KETRALSLARALEEA-----------------------------LEAKEELERTNKQLRAEMEDLVSSKDDVG 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1244 KAKGNLEKMCRTLEDQVSELKSKEEEqqrLINDLTAqrgrlqTESGEFSRQLDEKdALVSQLSRGKQAFTQQIEELKRQL 1323
Cdd:pfam01576 678 KNVHELERSKRALEQQVEEMKTQLEE---LEDELQA------TEDAKLRLEVNMQ-ALKAQFERDLQARDEQGEEKRRQL 747
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1324 EEEIKAKNAlahalqssrhdcdllreqyEEEQESKaelQRALSKAntevaqwrtkyetdaiqrteeleeAKKKLAQRLQA 1403
Cdd:pfam01576 748 VKQVRELEA-------------------ELEDERK---QRAQAVA------------------------AKKKLELDLKE 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1404 AEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAAcaaldkkqrnFDKILAEWKQkyeethaeleaSQKEARSLGT 1483
Cdd:pfam01576 782 LEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARAS----------RDEILAQSKE-----------SEKKLKNLEA 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1484 ELFKMKnayeeslDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKIL 1563
Cdd:pfam01576 841 ELLQLQ-------EDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLR 913
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1564 RIQLELNQVKSEV--DRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAirLKKKMEGDLNEMEIQLNHANRMAA 1641
Cdd:pfam01576 914 KSTLQVEQLTTELaaERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKS--SIAALEAKIAQLEEQLEQESRERQ 991
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1642 EALRNYRNTQGILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLH 1721
Cdd:pfam01576 992 AANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMN 1071
|
....*...
gi 305632842 1722 TQNTSLIN 1729
Cdd:pfam01576 1072 REVSTLKS 1079
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1314-1918 |
1.45e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.49 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1314 QQIEELKRQLEEEIKAKNALAHALQssrhdcdlLREQYEEEQESKAELQRALSKANTEVAQwrTKYETdAIQRTEELEEA 1393
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRE--------LAERYAAARERLAELEYLRAALRLWFAQ--RRLEL-LEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1394 KKKLAQRLQAAEEHVEAVNAKCASLEKtkQRLQN---EVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAE 1470
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEA--QIRGNggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1471 LEASQKEARSLGTELFKMKNAYEESLDQLETLKREnknLQQEISDLTEQIAEggkriheLEKIKKQVEQEkceLQAALEE 1550
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRD---LRRELRELEAEIAS-------LERRKSNIPAR---LLALRDA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1551 AEASLEHEEGKiLRIQLELNQVKSE--------------------VD-RKIAEKDEEIDQLK-RNHIRIvESMQSTLDAE 1608
Cdd:COG4913 449 LAEALGLDEAE-LPFVGELIEVRPEeerwrgaiervlggfaltllVPpEHYAAALRWVNRLHlRGRLVY-ERVRTGLPDP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1609 IRSRNDAIRLKKKMEGDLNEMEIQLNH--ANRMA------AEALRNYRntQGILKDTQLHLDDALR---TQEDLKEQLAM 1677
Cdd:COG4913 527 ERPRLDPDSLAGKLDFKPHPFRAWLEAelGRRFDyvcvdsPEELRRHP--RAITRAGQVKGNGTRHekdDRRRIRSRYVL 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1678 ---VERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHtqntslintkkkletDISQMQGEMEDILQEARN 1754
Cdd:COG4913 605 gfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ---------------RLAEYSWDEIDVASAERE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1755 AEEKAkkaitdaammaEELKKEQDTSAHLERMkknmEQTVKDLQLRLDEAEQlalkggkkQIQKLEARVRELEGEVES-- 1832
Cdd:COG4913 670 IAELE-----------AELERLDASSDDLAAL----EEQLEELEAELEELEE--------ELDELKGEIGRLEKELEQae 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1833 -EQKRNAEAVKGLRkhERRVKELTYQTEEDRKNIL---RLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKlQHELE 1908
Cdd:COG4913 727 eELDELQDRLEAAE--DLARLELRALLEERFAAALgdaVERELRENLEERIDALRARLNRAEEELERAMRAFNR-EWPAE 803
|
650
....*....|
gi 305632842 1909 EAEERADIAE 1918
Cdd:COG4913 804 TADLDADLES 813
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1245-1909 |
1.56e-13 |
|
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: 76.31 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1245 AKGNLEKMCRTLEDQVSELKSKEEEQQRLIND----LTAQRGRLQTESGEFSRqldEKDALVSQLSRGKQAFTQQIEELK 1320
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKqkfyLRQSVIDLQTKLQEMQM---ERDAMADIRRRESQSQEDLRNQLQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1321 RQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALskANTEVAQWRTKYETDAIQRT------------- 1387
Cdd:pfam15921 149 NTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL--VDFEEASGKKIYEHDSMSTMhfrslgsaiskil 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1388 EELEEAKKKLAQRLQAAEEHVEAVNAKCAS-LEKTKQRLQNEVEDLMLDVErtnAACAALDKKQrnfdkilAEWKQKYEE 1466
Cdd:pfam15921 227 RELDTEISYLKGRIFPVEDQLEALKSESQNkIELLLQQHQDRIEQLISEHE---VEITGLTEKA-------SSARSQANS 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1467 THAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNL-QQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQ 1545
Cdd:pfam15921 297 IQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMyEDKIEELEKQLVLANSELTEARTERDQFSQESGNLD 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1546 AALE---------EAEASLEHEEGKILRIQLELNQVK-SEVDRKIAEKDEEIDQLKRnhirIVESMQSTLDAEIRSRNDA 1615
Cdd:pfam15921 377 DQLQklladlhkrEKELSLEKEQNKRLWDRDTGNSITiDHLRRELDDRNMEVQRLEA----LLKAMKSECQGQMERQMAA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1616 IRLKKKMEGDLNEMEIQLNHANRMAAEALRNyrntqgiLKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEELRAT 1695
Cdd:pfam15921 453 IQGKNESLEKVSSLTAQLESTKEMLRKVVEE-------LTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSR 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1696 LEqtersrkIAEQELldaservQLLHTQNTSLINTKKKLETDISQMQGE---MEDILQEARNaeekakkaitdaamMAEE 1772
Cdd:pfam15921 526 VD-------LKLQEL-------QHLKNEGDHLRNVQTECEALKLQMAEKdkvIEILRQQIEN--------------MTQL 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1773 LKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLAlkggkkqiQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVK 1852
Cdd:pfam15921 578 VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILK--------DKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVK 649
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305632842 1853 ELTYQTE----EDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEE 1909
Cdd:pfam15921 650 DIKQERDqllnEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1036-1630 |
5.19e-13 |
|
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: 74.37 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1036 DDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQldeKLKKKEFEISNLQSKIEDEQALGIQLQKKIKEL 1115
Cdd:pfam05483 190 NNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLEES 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1116 QARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatsaqIEMNKKREAEFQKMRRDLEEATLQHEATAAT 1195
Cdd:pfam05483 267 RDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRS-------MSTQKALEEDLQIATKTICQLTEEKEAQMEE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1196 LRK---KHADSVAELGEQIDNLQRV----KQKLEKEKSEMK---MEIDDLASNVETVSKAKGNLEKMCRTLEDQVSE--- 1262
Cdd:pfam05483 340 LNKakaAHSFVVTEFEATTCSLEELlrteQQRLEKNEDQLKiitMELQKKSSELEEMTKFKNNKEVELEELKKILAEdek 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1263 LKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEiKAKNALAHAlqssrh 1342
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKE-KLKNIELTA------ 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1343 DCDLLREQYEEEQESKAELQRALSKANTEVAQWRtKYETDAIQRTEELEEAKKKLAQRLQAAEEHV----EAVNAKCASL 1418
Cdd:pfam05483 493 HCDKLLLENKELTQEASDMTLELKKHQEDIINCK-KQEERMLKQIENLEEKEMNLRDELESVREEFiqkgDEVKCKLDKS 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1419 EKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNfdkilaewKQKYEEthaELEASQKEARSLGTELFKMKNAYEESLDQ 1498
Cdd:pfam05483 572 EENARSIEYEVLKKEKQMKILENKCNNLKKQIEN--------KNKNIE---ELHQENKALKKKGSAENKQLNAYEIKVNK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1499 LETLKRENKNLQQEISDLTEQIAEgGKRIHElEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDR 1578
Cdd:pfam05483 641 LELELASAKQKFEEIIDNYQKEIE-DKKISE-EKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDK 718
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 305632842 1579 KIAEKDEEIDqLKRNHIRIVESMQSTLDAEIRS-RNDAIRLKKKMEGDLNEME 1630
Cdd:pfam05483 719 IIEERDSELG-LYKNKEQEQSSAKAALEIELSNiKAELLSLKKQLEIEKEEKE 770
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1259-1925 |
6.73e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 74.44 E-value: 6.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1259 QVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQ-----------------LSRGKQAFTQQIEELKR 1321
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQlqaetelcaeaeemrarLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1322 QLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQraLSKANTEVAQwrTKYETDAI---QRTEELEEAKKKLA 1398
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQ--LEKVTTEAKI--KKLEEDILlleDQNSKLSKERKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1399 QRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEA 1478
Cdd:pfam01576 159 ERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1479 RSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHE 1558
Cdd:pfam01576 239 AKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1559 EGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANR 1638
Cdd:pfam01576 319 QELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1639 MAAEALRNYRNTQGILKDTQLHLDDALRTQEDLKEQLAMverranlLQAEIEELRATLEQTERSRKIAEQELLDASERVQ 1718
Cdd:pfam01576 399 AKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSK-------LQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQ 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1719 LLHTQNTSLINTKKKLETDISQMQGEmEDILQEARNAEEKAKKAITdaammaeelKKEQDTSAHLERMKKNMEQTVKDLQ 1798
Cdd:pfam01576 472 DTQELLQEETRQKLNLSTRLRQLEDE-RNSLQEQLEEEEEAKRNVE---------RQLSTLQAQLSDMKKKLEEDAGTLE 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1799 lrldeaeqlALKGGKKQIQklearvRELEGEVESEQKRnAEAVKGLRKHERRVKE----LTYQTEEDRKNILRL---QDL 1871
Cdd:pfam01576 542 ---------ALEEGKKRLQ------RELEALTQQLEEK-AAAYDKLEKTKNRLQQelddLLVDLDHQRQLVSNLekkQKK 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 305632842 1872 VDKLQAKVKS----YKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLR 1925
Cdd:pfam01576 606 FDQMLAEEKAisarYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLR 663
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1376-1889 |
7.23e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 7.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1376 RTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVN-------AKCASLEKTKQRLQ---NEVEDLMLDVERTNAACAA 1445
Cdd:PRK03918 177 RIERLEKFIKRTENIEELIKEKEKELEEVLREINEISselpelrEELEKLEKEVKELEelkEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1446 LDKKQRNFDKILAEWKQKYEETHaELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGK 1525
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1526 RIHELEKIKKQVEqekcELQAALEEAEASLEHEEgKILRIQLELNQVKSEV-DRKIAEKDEEIDQLKR------NHIRIV 1598
Cdd:PRK03918 336 KEERLEELKKKLK----ELEKRLEELEERHELYE-EAKAKKEELERLKKRLtGLTPEKLEKELEELEKakeeieEEISKI 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1599 ESMQSTLDAEIRSRNDAI-----------------------RLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILK 1655
Cdd:PRK03918 411 TARIGELKKEIKELKKAIeelkkakgkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1656 DtqlhlDDALRTQEDLKEQLAMVERRANLLQAEIEELRATLEQT--ERSRKIAEQ--ELLDASERVQLLHTQNTSLINTK 1731
Cdd:PRK03918 491 K-----ESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKlkEKLIKLKGEikSLKKELEKLEELKKKLAELEKKL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1732 KKLETDISQMQGEMEDI--------------LQEARNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTVKDL 1797
Cdd:PRK03918 566 DELEEELAELLKELEELgfesveeleerlkeLEPFYNEYLELKDAEKELEREEKELKKLEEE---LDKAFEELAETEKRL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1798 QLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDL------ 1871
Cdd:PRK03918 643 EELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLekaler 722
|
570
....*....|....*...
gi 305632842 1872 VDKLQAKVKSYKRQAEEA 1889
Cdd:PRK03918 723 VEELREKVKKYKALLKER 740
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1041-1938 |
1.57e-12 |
|
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: 73.16 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1041 SLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKiEDEQALGIQLQKKIKELQARIE 1120
Cdd:TIGR00606 187 ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSY-ENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1121 ELEeeieAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREA-EFQKMRRDLEEATLQHEATAATLRKK 1199
Cdd:TIGR00606 266 KLD----NEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVrEKERELVDCQRELEKLNKERRLLNQE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1200 HADSVAELGE-----QIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQ-------VSELKSKE 1267
Cdd:TIGR00606 342 KTELLVEQGRlqlqaDRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEaktaaqlCADLQSKE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1268 EEQQRLINDL----TAQRGRLQTESGEFSRQLDEKDALVSQLsrgkQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHD 1343
Cdd:TIGR00606 422 RLKQEQADEIrdekKGLGRTIELKKEILEKKQEELKFVIKEL----QQLEGSSDRILELDQELRKAERELSKAEKNSLTE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1344 CDLLREQYeeEQESKAELQRALSKANTEVAQwrTKYETDAIQRTEELEEAKKKLAQRLQAAE-EHVEAVNAKCA------ 1416
Cdd:TIGR00606 498 TLKKEVKS--LQNEKADLDRKLRKLDQEMEQ--LNHHTTTRTQMEMLTKDKMDKDEQIRKIKsRHSDELTSLLGyfpnkk 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1417 SLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQ---RNFDKILAEWKQKYEETHAELEASQKEARSLGtelfKMKNAYE 1493
Cdd:TIGR00606 574 QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKnhiNNELESKEEQLSSYEDKLFDVCGSQDEESDLE----RLKEEIE 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1494 ESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQV- 1572
Cdd:TIGR00606 650 KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMl 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1573 ------KSEVDRKIAEKDEEIDQLK---------RNHIRIVESMQSTLDAEIRSRND-----AIRLKKKMEGDLNEMEIQ 1632
Cdd:TIGR00606 730 glapgrQSIIDLKEKEIPELRNKLQkvnrdiqrlKNDIEEQETLLGTIMPEEESAKVcltdvTIMERFQMELKDVERKIA 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1633 LNHANRMAAEALRNYRNTQGILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEEL---RATLEQTERSRKIAEQE 1709
Cdd:TIGR00606 810 QQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELkseKLQIGTNLQRRQQFEEQ 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1710 LLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQearNAEEKAKKAITDAAMMAEELKK--------EQDTSA 1781
Cdd:TIGR00606 890 LVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS---SKETSNKKAQDKVNDIKEKVKNihgymkdiENKIQD 966
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1782 HLERMKKNMEQTVKDLQLRLDEAEQlalkgGKKQIQKlEARVRELEGEVESEQKRNAEAVKGLRKHERRVKEL-----TY 1856
Cdd:TIGR00606 967 GKDDYLKQKETELNTVNAQLEECEK-----HQEKINE-DMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVeeelkQH 1040
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1857 QTEEDRKNILRLQDLVDKLQAKVKSYKR-------QAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLRVKSR 1929
Cdd:TIGR00606 1041 LKEMGQMQVLQMKQEHQKLEENIDLIKRnhvlalgRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDL 1120
|
....*....
gi 305632842 1930 EVHTKVISE 1938
Cdd:TIGR00606 1121 DIYYKTLDQ 1129
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
845-1428 |
1.59e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.15 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 845 KSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLiktkiqleakik 924
Cdd:PRK02224 231 QARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDL------------ 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 925 eVTERAEDEEEINAeltakkrkLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQ 1004
Cdd:PRK02224 299 -LAEAGLDDADAEA--------VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1005 EAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDD----LEGSLEQEKKLRMDLERAKRK---LEGDLKLAQESImdieNEK 1077
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFGDapvdLGNAEDFLEELREERDELREReaeLEATLRTARERV----EEA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1078 QQLDEKLKKKEFEisnlQSKIEDEQALGIqlqkkikelqarieeleeeiEAERASRAKAEKQRSDLSRELEEISERLEEA 1157
Cdd:PRK02224 446 EALLEAGKCPECG----QPVEGSPHVETI--------------------EEDRERVEELEAELEDLEEEVEEVEERLERA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1158 GGATSAQIEMNKKREAefqkmRRDLEEATLQHEATaatlrkkhadsVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLAS 1237
Cdd:PRK02224 502 EDLVEAEDRIERLEER-----REDLEELIAERRET-----------IEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1238 NVETVSKAKGNLEKMCRTLEDQVSELKsKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSrgkqaftqqie 1317
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR----------- 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1318 ELKRQLEEEIKAKnalahALQSSRHDcdllREQYEEEQESKAELQRALSKANTEVaQWRTKYETDAIQRTEELEEAKKKL 1397
Cdd:PRK02224 634 ERKRELEAEFDEA-----RIEEARED----KERAEEYLEQVEEKLDELREERDDL-QAEIGAVENELEELEELRERREAL 703
|
570 580 590
....*....|....*....|....*....|.
gi 305632842 1398 AQRLQAaeehVEAVNAKCASLEKTKQRLQNE 1428
Cdd:PRK02224 704 ENRVEA----LEALYDEAEELESMYGDLRAE 730
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1388-1927 |
2.72e-12 |
|
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: 72.46 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1388 EELEEAKKKLAQRLQAAEE-HveavnakcaslEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEE 1466
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNElH-----------EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1467 THAELEAsqkeARSLGTELFKMKNAyeeSLDQLETLKRENKNLQQEISDLTEQIAEG-GKRIHELEKIKK-QVEQEKCEL 1544
Cdd:pfam15921 150 TVHELEA----AKCLKEDMLEDSNT---QIEQLRKMMLSHEGVLQEIRSILVDFEEAsGKKIYEHDSMSTmHFRSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1545 QAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIaekdeeiDQLKRNHirivesmqstldaeirsrndairlKKKMEG 1624
Cdd:pfam15921 223 SKILRELDTEISYLKGRIFPVEDQLEALKSESQNKI-------ELLLQQH------------------------QDRIEQ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1625 DLNEMEIQLNHANRMAAEALRNYRNTQgilkdTQLHLddalrTQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRK 1704
Cdd:pfam15921 272 LISEHEVEITGLTEKASSARSQANSIQ-----SQLEI-----IQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1705 IAEQELldaservqllhTQNTSLINTkkkletDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLE 1784
Cdd:pfam15921 342 DKIEEL-----------EKQLVLANS------ELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLW 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1785 RMKKNMEQTVKDLQLRLDEAEQlalkggkkQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKn 1864
Cdd:pfam15921 405 DRDTGNSITIDHLRRELDDRNM--------EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKE- 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305632842 1865 ilRLQDLVDKLQAkvksyKRQAEEAEEQSNTNLAKfrklqhELEEAEERADIAESQVNKLRVK 1927
Cdd:pfam15921 476 --MLRKVVEELTA-----KKMTLESSERTVSDLTA------SLQEKERAIEATNAEITKLRSR 525
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
839-1331 |
3.86e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.10 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 839 KIKPLLKSAETEKEMATMKEEFQKTKDElaksEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLiKTKIQ 918
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKAD----AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA-KKKAE 1428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 919 LEAKIKEVTERAedEEEINAELTAKKRKLEDECSELKKdiddleltlaKVEKEKHATENKVKnlTEEMAGLDETIAKLTK 998
Cdd:PTZ00121 1429 EKKKADEAKKKA--EEAKKADEAKKKAEEAKKAEEAKK----------KAEEAKKADEAKKK--AEEAKKADEAKKKAEE 1494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 999 EKKALQEAHQQTLDDLQAEEDKvntltkaKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgDLKLAQEsiMDIENEKQ 1078
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAK-------KAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD-ELKKAEE--LKKAEEKK 1564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1079 QLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDlsrelEEISERLEEAg 1158
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-----EEEKKKVEQL- 1638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1159 gatsaqiemnKKREAEFQKMRRDLEEATLQHEATAATLRKKHADS--VAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLA 1236
Cdd:PTZ00121 1639 ----------KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDkkKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1237 SNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTAQRGrlqtESGEFSRQLDEKDALVSQLSRGKQAFTQQ- 1315
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE----EKKKIAHLKKEEEKKAEEIRKEKEAVIEEe 1784
|
490
....*....|....*...
gi 305632842 1316 --IEELKRQLEEEIKAKN 1331
Cdd:PTZ00121 1785 ldEEDEKRRMEVDKKIKD 1802
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1073-1939 |
4.15e-12 |
|
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: 71.93 E-value: 4.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1073 IENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEeieaeRASRAKAEKQRSDLSRELEEISE 1152
Cdd:pfam02463 144 IEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEEL-----KLQELKLKEQAKKALEYYQLKEK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1153 RLEEAGGATSAQIEmnkKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDnlqrvkqKLEKEKSEMKMEI 1232
Cdd:pfam02463 219 LELEEEYLLYLDYL---KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENK-------EEEKEKKLQEEEL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1233 DDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAF 1312
Cdd:pfam02463 289 KLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1313 TQQIEEL--------KRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAI 1384
Cdd:pfam02463 369 EQLEEELlakkklesERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1385 QRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTkqrlQNEVEDLMLDVERTNAACAALD--KKQRNFDKILAEWKQ 1462
Cdd:pfam02463 449 EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ----LELLLSRQKLEERSQKESKARSglKVLLALIKDGVGGRI 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1463 KYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKC 1542
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1543 ELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKM 1622
Cdd:pfam02463 605 LAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1623 EGDLNEMEIQLNHANRMAAEALRNYRNTQgILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEELRATLEQTERS 1702
Cdd:pfam02463 685 AESELAKEEILRRQLEIKKKEQREKEELK-KLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKE 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1703 RKIAEQELLDASERVQLLHTQNTSLINTKKKLET--------DISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELK 1774
Cdd:pfam02463 764 EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKaqeeelraLEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELK 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1775 KEQDTSAHLERMKK--NMEQTVKDLQLRLDEAEQLALKGGKKQ-IQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRV 1851
Cdd:pfam02463 844 EEQKLEKLAEEELErlEEEITKEELLQELLLKEEELEEQKLKDeLESKEEKEKEEKKELEEESQKLNLLEEKENEIEERI 923
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1852 KELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLRVKSREV 1931
Cdd:pfam02463 924 KEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
....*...
gi 305632842 1932 HTKVISEE 1939
Cdd:pfam02463 1004 KKKLIRAI 1011
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
850-1516 |
4.17e-12 |
|
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: 71.92 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 850 EKEMATMKEEFQKTKDELAKSEAKRKELEEKMV--TLLKEKNDLQLQVQAEAEGLADAEERCDQLIKtKIQLEAKIKEVT 927
Cdd:TIGR00618 225 EKELKHLREALQQTQQSHAYLTQKREAQEEQLKkqQLLKQLRARIEELRAQEAVLEETQERINRARK-AAPLAAHIKAVT 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 928 ERAEDEEEINAELTAKKRKLEDE---CSELKKDIDDLElTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQ 1004
Cdd:TIGR00618 304 QIEQQAQRIHTELQSKMRSRAKLlmkRAAHVKQQSSIE-EQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1005 EAHQQtlddLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQ------ 1078
Cdd:TIGR00618 383 TLQQQ----KTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQceklek 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1079 ----QLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSR--ELEEISE 1152
Cdd:TIGR00618 459 ihlqESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRmqRGEQTYA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1153 RLEEAGGATSAQIEMNKKR----EAEFQKMRRDLEEATLQHEATAATLRK--KHADSVAELGEQIDNLQRVKQ-KLEKEK 1225
Cdd:TIGR00618 539 QLETSEEDVYHQLTSERKQraslKEQMQEIQQSFSILTQCDNRSKEDIPNlqNITVRLQDLTEKLSEAEDMLAcEQHALL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1226 SEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQtesgefSRQLDEKDALVSQL 1305
Cdd:TIGR00618 619 RKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASR------QLALQKMQSEKEQL 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1306 SRGKQAFTQQIEELKRQLEEEIKAK---NALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETD 1382
Cdd:TIGR00618 693 TYWKEMLAQCQTLLRELETHIEEYDrefNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTA 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1383 AIQRTEELEEAKKKLAQRLQAAEEHVEavnakcaSLEKTKQRLQNEVEDlmlDVERTNAACAALDKKQRNFDKILAEWKQ 1462
Cdd:TIGR00618 773 ALQTGAELSHLAAEIQFFNRLREEDTH-------LLKTLEAEIGQEIPS---DEDILNLQCETLVQEEEQFLSRLEEKSA 842
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 305632842 1463 KYEETHAELEAsqkearslgtelfkmknaYEESLDQLETLKRENKNLQQEISDL 1516
Cdd:TIGR00618 843 TLGEITHQLLK------------------YEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1210-1931 |
4.69e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.71 E-value: 4.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1210 QIDNLQRVKQKLEKEKSEMKMEIDDLASNV--ETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQTE 1287
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRadEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAED 1138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1288 SGEFSRQLDEKDALVSQLSRgkqaftqQIEElKRQLEEEIKAKNAlaHALQSSRHDCDLLREQYEEEQESKAELQRALSK 1367
Cdd:PTZ00121 1139 ARKAEEARKAEDAKRVEIAR-------KAED-ARKAEEARKAEDA--KKAEAARKAEEVRKAEELRKAEDARKAEAARKA 1208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1368 ANTEVAQWRTKYETDA-IQRTEELEEAKKKlaqrlqaAEEhveavnAKCASLEKTKQRLQNEVEDLMLDVERTNAACAAL 1446
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKkAEAVKKAEEAKKD-------AEE------AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1447 DKKQrnfdkilAEWKQKYEETHAELEASQKEARSLGTELfkmKNAYEEsldqletlKRENKNLQQEISDLTEQIAEGGKR 1526
Cdd:PTZ00121 1276 EARK-------ADELKKAEEKKKADEAKKAEEKKKADEA---KKKAEE--------AKKADEAKKKAEEAKKKADAAKKK 1337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1527 IhelEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLElnQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLD 1606
Cdd:PTZ00121 1338 A---EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA--KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK 1412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1607 AEiRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRTQEDLKEqlAMVERRANLLQ 1686
Cdd:PTZ00121 1413 AA-AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK--AEEAKKADEAK 1489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1687 AEIEELRatlEQTERSRKIAEQelldaservqllhtqntslintKKKLEtdiSQMQGEMEDILQEARNAEEKAKkaiTDA 1766
Cdd:PTZ00121 1490 KKAEEAK---KKADEAKKAAEA----------------------KKKAD---EAKKAEEAKKADEAKKAEEAKK---ADE 1538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1767 AMMAEELKKEQDTSaHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKglRK 1846
Cdd:PTZ00121 1539 AKKAEEKKKADELK-KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK--KA 1615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1847 HERRVK-ELTYQTEEDRKNILRLQDLVDKLQAKVKSYkRQAEEAEEQSNTNLAKF----RKLQHELEEAEERADIAESQV 1921
Cdd:PTZ00121 1616 EEAKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEEL-KKAEEENKIKAAEEAKKaeedKKKAEEAKKAEEDEKKAAEAL 1694
|
730
....*....|
gi 305632842 1922 NKLRVKSREV 1931
Cdd:PTZ00121 1695 KKEAEEAKKA 1704
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
918-1355 |
8.82e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.18 E-value: 8.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 918 QLEAKIKEVTErAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEK--HATENKVKNLTEEMAGLDETIAK 995
Cdd:COG4717 72 ELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqlLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 996 LTKEKKALQEAHQQtLDDLQAEedkvntLTKAKTKLEQQVDDLegSLEQEKKLRmDLERAKRKLEGDLKLAQESIMDIEN 1075
Cdd:COG4717 151 LEERLEELRELEEE-LEELEAE------LAELQEELEELLEQL--SLATEEELQ-DLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1076 EKQQLDEKLK--KKEFEISNLQSKIEDEQALG--------------------------IQLQKKIKELQARIEELEEEIE 1127
Cdd:COG4717 221 ELEELEEELEqlENELEAAALEERLKEARLLLliaaallallglggsllsliltiagvLFLVLGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1128 AERASRAKAEKQRSDLS-RELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQ------HEATAATLRKKH 1200
Cdd:COG4717 301 GKEAEELQALPALEELEeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElqleelEQEIAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1201 ADSVAELGEQIDNLQRvKQKLEKEKSEMKMEIDDLASNVETVSkAKGNLEkmcrTLEDQVSELKSKEEEQQRLINDLTAQ 1280
Cdd:COG4717 381 VEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELL-EALDEE----ELEEELEELEEELEELEEELEELREE 454
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305632842 1281 RGRLQTESgefsRQLDEKDALVSQLsrgkqaftQQIEELKRQLEEEIKAKNALAHALQSSRHdcdlLREQYEEEQ 1355
Cdd:COG4717 455 LAELEAEL----EQLEEDGELAELL--------QELEELKAELRELAEEWAALKLALELLEE----AREEYREER 513
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1277-1807 |
1.24e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.07 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1277 LTAQRGRLqtesGEFSRQLDEKDA--LVSQLSRGKQAFTQQIEELKRQLEEEIKAKnalahalqSSRHDCDLLREQYEEE 1354
Cdd:PRK02224 182 LSDQRGSL----DQLKAQIEEKEEkdLHERLNGLESELAELDEEIERYEEQREQAR--------ETRDEADEVLEEHEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1355 QESKAELQRALSKANTEVAQWRTKYET------DAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNE 1428
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREElaeevrDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1429 VEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARS-------LGTELFKMKNAYEESLDQLET 1501
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDrreeieeLEEEIEELRERFGDAPVDLGN 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1502 LKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQ--------------EKCELQAALEEAEASLEHEEGKILRIQL 1567
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1568 ELNQVKSEVDR--KIAEKDEEIDQLKRNHIRIVESMqSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALR 1645
Cdd:PRK02224 490 EVEEVEERLERaeDLVEAEDRIERLEERREDLEELI-AERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1646 NYRNTQGILKDTQLHLDDALRTQEDLKEQLAMVERranlLQAEIEELRATLEQ-----TERSRKIAEQelldaSERVQLL 1720
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIESLERIRTLLAAIAD----AEDEIERLREKREAlaelnDERRERLAEK-----RERKREL 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1721 HTQN-----TSLINTKKKLETDISQMQGEMEDiLQEARNAEEKAKKAITDAAMMAEELKKEQDTsahlermkknMEQTVK 1795
Cdd:PRK02224 640 EAEFdeariEEAREDKERAEEYLEQVEEKLDE-LREERDDLQAEIGAVENELEELEELRERREA----------LENRVE 708
|
570
....*....|..
gi 305632842 1796 DLQLRLDEAEQL 1807
Cdd:PRK02224 709 ALEALYDEAEEL 720
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
850-1763 |
1.25e-11 |
|
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: 70.46 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 850 EKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQlqvqaeaeglaDAEERCDQLIKTKIQLEAKIKEVTER 929
Cdd:TIGR00606 230 EAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIK-----------ALKSRKKQMEKDNSELELKMEKVFQG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 930 AEDE-EEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQeahq 1008
Cdd:TIGR00606 299 TDEQlNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLA---- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1009 qtlddlqaeedkvntltkaktkLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKE 1088
Cdd:TIGR00606 375 ----------------------TRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIR 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1089 FEISNLQSKIEDEQalgIQLQKKIKELQARIEELEeeieaerasraKAEKQRSDLSRELEEISERLEEAGGA-TSAQIEM 1167
Cdd:TIGR00606 433 DEKKGLGRTIELKK---EILEKKQEELKFVIKELQ-----------QLEGSSDRILELDQELRKAERELSKAeKNSLTET 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1168 NKKREAEFQKMRRDLEEaTLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVskakg 1247
Cdd:TIGR00606 499 LKKEVKSLQNEKADLDR-KLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNK----- 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1248 nlekmcRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSR------GKQAFTQQIEELKR 1321
Cdd:TIGR00606 573 ------KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfdvcGSQDEESDLERLKE 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1322 QLEEEIKAKNALAHALQssrhdcdlLREQYEEEQESKaelqralSKANTEVAQwrtkyetDAIQRTEELEEAKKKLAQRL 1401
Cdd:TIGR00606 647 EIEKSSKQRAMLAGATA--------VYSQFITQLTDE-------NQSCCPVCQ-------RVFQTEAELQEFISDLQSKL 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1402 QAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELE---ASQKEA 1478
Cdd:TIGR00606 705 RLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGtimPEEESA 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1479 RSLGTELFKMKNAYEEsldqletLKRENKNLQQEISDLteQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHE 1558
Cdd:TIGR00606 785 KVCLTDVTIMERFQME-------LKDVERKIAQQAAKL--QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQ 855
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1559 EGKILRIQLELNQVKSEvDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANR 1638
Cdd:TIGR00606 856 QEQIQHLKSKTNELKSE-KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKET 934
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1639 MAAEALRNYRNTQGILKDTQLHLDDALRTQEDLKE-QLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERV 1717
Cdd:TIGR00606 935 SNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDdYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQE 1014
|
890 900 910 920
....*....|....*....|....*....|....*....|....*....
gi 305632842 1718 QLLHTQNTSLI--NTKKKLETDISQMQGEM-EDILQEARNAEEKAKKAI 1763
Cdd:TIGR00606 1015 RWLQDNLTLRKreNELKEVEEELKQHLKEMgQMQVLQMKQEHQKLEENI 1063
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1247-1902 |
2.06e-11 |
|
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: 69.40 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1247 GNLEKMCRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQL-------DEKDALVSQLSrGKQAFTQQIEEL 1319
Cdd:pfam07111 59 QALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAvaekagqAEAEGLRAALA-GAEMVRKNLEEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1320 KRQLEEEIKA--KNALAHALQSSRHDCDLLREQYE--EEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKK 1395
Cdd:pfam07111 138 SQRELEEIQRlhQEQLSSLTQAHEEALSSLTSKAEglEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1396 KLAQRLQ--AAEEHVEAVNAKCASLEKtkQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILA----EWKQKYEETHA 1469
Cdd:pfam07111 218 TLVESLRkyVGEQVPPEVHSQTWELER--QELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLAlqeeELTRKIQPSDS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1470 ELEASQKEARSLgtelfkMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEggkrihELEKIKKQvEQEKCELQAALE 1549
Cdd:pfam07111 296 LEPEFPKKCRSL------LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAE------LQEQVTSQ-SQEQAILQRALQ 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1550 EAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKrnhiRIVESMQSTldaeirsrndAIRLKKKMeGDLNEM 1629
Cdd:pfam07111 363 DKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLK----FVVNAMSST----------QIWLETTM-TRVEQA 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1630 EIQLNHANRMAAEALRNYRNTQGILKD----TQLHLDD------ALRTQEDLKEQLAMVERRANLLQAEIeELRATLEQT 1699
Cdd:pfam07111 428 VARIPSLSNRLSYAVRKVHTIKGLMARkvalAQLRQEScpppppAPPVDADLSLELEQLREERNRLDAEL-QLSAHLIQQ 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1700 ERSRKIAEQElldaSERVQllhtqntsLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQdt 1779
Cdd:pfam07111 507 EVGRAREQGE----AERQQ--------LSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQ-- 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1780 sahlERMKKNMEQTVKDLQLRLDEaeqlalkggkkQIQKLEARVRElegevesEQKRNAEAVKGLRKHERRVKeltyQTE 1859
Cdd:pfam07111 573 ----EIYGQALQEKVAEVETRLRE-----------QLSDTKRRLNE-------ARREQAKAVVSLRQIQHRAT----QEK 626
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 305632842 1860 EDRKNILRLQDLVDKLQAkvKSYKRQAEEAEEQSNTNLAKFRK 1902
Cdd:pfam07111 627 ERNQELRRLQDEARKEEG--QRLARRVQELERDKNLMLATLQQ 667
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
944-1568 |
2.94e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 944 KRKLEDECSELKKDIDDLELTLAKVEKEKHATE--NKVKNLTEEMAGLDETIAKLTKEKKALQ-EAHQQTLDDLQAEEDK 1020
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1021 vntLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDlklaqeSIMDIENEKQQLDEKLKKKEFEISNLQSKIed 1100
Cdd:COG4913 300 ---LRAELARLEAELERLEARLDALREELDELEAQIRGNGGD------RLEQLEREIERLERELEERERRRARLEALL-- 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1101 eQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatSAQIEMNKKR----EAEFQ 1176
Cdd:COG4913 369 -AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL----EAEIASLERRksniPARLL 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1177 KMRRDLEEATLQHEA---------------------------TAAT---LRKKHADSVAELGEQID-----NLQRVKQKL 1221
Cdd:COG4913 444 ALRDALAEALGLDEAelpfvgelievrpeeerwrgaiervlgGFALtllVPPEHYAAALRWVNRLHlrgrlVYERVRTGL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1222 EKEKSeMKMEIDDLASNVET-VSKAKGNLEKM---------CRTLED------------QVSELKSKEEEQ--------- 1270
Cdd:COG4913 524 PDPER-PRLDPDSLAGKLDFkPHPFRAWLEAElgrrfdyvcVDSPEElrrhpraitragQVKGNGTRHEKDdrrrirsry 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1271 ------QRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFtQQIEELK------RQLEEEIKAKNALAHALQ 1338
Cdd:COG4913 603 vlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSwdeidvASAEREIAELEAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1339 SSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYEtdaiQRTEELEEAKKKLAQRLQAAEEHV---------- 1408
Cdd:COG4913 682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELE----QAEEELDELQDRLEAAEDLARLELralleerfaa 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1409 ----EAVNAKCASLEKTKQRLQNEVEDLMLDVERtnaacaaldkkqrnfdkILAEWKQKYEETHAELEASQKEARSlgte 1484
Cdd:COG4913 758 algdAVERELRENLEERIDALRARLNRAEEELER-----------------AMRAFNREWPAETADLDADLESLPE---- 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1485 lfkmknaYEESLDQLET----------LKRENKNLQQEISDLTEQIAEggkrihELEKIKKQVEqekcELQAALEEaeas 1554
Cdd:COG4913 817 -------YLALLDRLEEdglpeyeerfKELLNENSIEFVADLLSKLRR------AIREIKERID----PLNDSLKR---- 875
|
730
....*....|....
gi 305632842 1555 LEHEEGKILRIQLE 1568
Cdd:COG4913 876 IPFGPGRYLRLEAR 889
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1184-1761 |
3.18e-11 |
|
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: 68.59 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1184 EATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEiddLASNVETVSKAKGNLEKMCRTLEDQVSEL 1263
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFK---LKEDHEKIQHLEEEYKKEINDKEKQVSLL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1264 KSKEEEQQRLINDLTAqrgrLQTESGEFSRQLDEKDALVS----QLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQ- 1338
Cdd:pfam05483 246 LIQITEKENKMKDLTF----LLEESRDKANQLEEKTKLQDenlkELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQi 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1339 SSRHDCDLLRE---QYEEEQESKAELQRALSKANTEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQAAEEHVEavnakc 1415
Cdd:pfam05483 322 ATKTICQLTEEkeaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQ-QRLEKNEDQLKIITMELQKKSSELE------ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1416 aslEKTKQRLQNEVEdlMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEES 1495
Cdd:pfam05483 395 ---EMTKFKNNKEVE--LEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1496 LDQLETLKR---------------------ENKNLQQEISDLT-------EQIAEGGKRIHELEKIKKQVEQEKCELQAA 1547
Cdd:pfam05483 470 LKEVEDLKTelekeklknieltahcdklllENKELTQEASDMTlelkkhqEDIINCKKQEERMLKQIENLEEKEMNLRDE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1548 LEEAEASL--EHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEG- 1624
Cdd:pfam05483 550 LESVREEFiqKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENk 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1625 -------DLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRTQEDLKEQLAMVERRANL-LQAEIEELRATL 1696
Cdd:pfam05483 630 qlnayeiKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKrCQHKIAEMVALM 709
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 305632842 1697 EQTERS-RKIAEQElldaSERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKK 1761
Cdd:pfam05483 710 EKHKHQyDKIIEER----DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEK 771
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1574-1921 |
3.29e-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: 68.94 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1574 SEVDRKIAEKDEEIDQLKRNHIR---IVESMQSTLDAEIRSRNDAIR---LKKKME--------GDLNEMEIQLNHANRM 1639
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERldlIIDEKRQQLERLRREREKAERyqaLLKEKReyegyellKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1640 AAEALRNYRNTQGILKDTQLHLDDALRTQEDLKEQL-AMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQ 1718
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1719 LLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSA----HLERMKKNMEQTV 1794
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKdyreKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1795 KDLQLRLDEAEQLALKGG--KKQIQKLEARVRELEGEVESEQKRnaeavkgLRKHERRVKELTYQTEEDRKNILRLQDLV 1872
Cdd:TIGR02169 406 RELDRLQEELQRLSEELAdlNAAIAGIEAKINELEEEKEDKALE-------IKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 305632842 1873 DKLQAKVksykrqaeeaeeqsntnlakfRKLQHELEEAEERADIAESQV 1921
Cdd:TIGR02169 479 DRVEKEL---------------------SKLQRELAEAEAQARASEERV 506
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
851-1308 |
4.44e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.87 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 851 KEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEA--EGLADAEERCDQLIKTKIQLEAKIKEVTE 928
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 929 RAEDEEEINAELTAKKRKLEDEC-----------SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT 997
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLeqlslateeelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 998 KEKKALQE-----------AHQQTLDDLQAEEDKV---------------NTLTKAKTKLEQQVDDLEGSLEQEKKLRMD 1051
Cdd:COG4717 241 LEERLKEArlllliaaallALLGLGGSLLSLILTIagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1052 LERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEfeisnlqskIEDEQALGIQLQKKIKELqarIEELEEEIEAERA 1131
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAE---------ELEEELQLEELEQEIAAL---LAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1132 SRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKR--EAEFQKMRRDLEEATLQHEAtaatLRKKHADSVAELG- 1208
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEE----LREELAELEAELEq 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1209 -EQIDNLQRVKQKLEKEKSEMKMEIDDLASNvetvSKAKGNLEKMCRTLEDQ-VSELKskeEEQQRLINDLTAQRGRLQT 1286
Cdd:COG4717 465 lEEDGELAELLQELEELKAELRELAEEWAAL----KLALELLEEAREEYREErLPPVL---ERASEYFSRLTDGRYRLIR 537
|
490 500
....*....|....*....|....*
gi 305632842 1287 ESGEFSRQLDEKDAL---VSQLSRG 1308
Cdd:COG4717 538 IDEDLSLKVDTEDGRtrpVEELSRG 562
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1202-1701 |
5.22e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.02 E-value: 5.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1202 DSVAELGEQIDNLQRVKQKLEKEKSEMKM--EIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSkeEEQQRLINDLTA 1279
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLWFAQRRL--ELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1280 QRGRLQTESGEFSRQLDEKDALVSQLSRGKQAF-TQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESK 1358
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1359 AELQRALSKANTEVAQWRtkyetdaiqrtEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTK---------------Q 1423
Cdd:COG4913 383 AALRAEAAALLEALEEEL-----------EALEEALAEAEAALRDLRRELRELEAEIASLERRKsniparllalrdalaE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1424 RLQNEVEDL-----MLDVER-----TNAACAALdkkqRNF-------DKILAEWKQKYEETH--------------AELE 1472
Cdd:COG4913 452 ALGLDEAELpfvgeLIEVRPeeerwRGAIERVL----GGFaltllvpPEHYAAALRWVNRLHlrgrlvyervrtglPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1473 ASQKEARSLGTELFKMKNAYEESLDQL-------------ETLKRENK-------------------------------- 1507
Cdd:COG4913 528 RPRLDPDSLAGKLDFKPHPFRAWLEAElgrrfdyvcvdspEELRRHPRaitragqvkgngtrhekddrrrirsryvlgfd 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1508 ------NLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEegkilriqlelnqvksEVDRKIA 1581
Cdd:COG4913 608 nraklaALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA----------------SAEREIA 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1582 EKDEEIDQLKRNHIRiVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHL 1661
Cdd:COG4913 672 ELEAELERLDASSDD-LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 305632842 1662 DDALRTQEDLKEQLAMVERRanlLQAEIEELRATLEQTER 1701
Cdd:COG4913 751 LEERFAAALGDAVERELREN---LEERIDALRARLNRAEE 787
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
856-1522 |
5.47e-11 |
|
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: 67.82 E-value: 5.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 856 MKEEFQKTKDELAKSEAKRKELEEKMVTLlkeKNDLQLQVQAEAEGLADAEercdqliKTKIQLEAKIKEVTERAED-EE 934
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVYMDL---NNNIEKMILAFEELRVQAE-------NARLEMHFKLKEDHEKIQHlEE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 935 EINAELTAKKRK---LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTL 1011
Cdd:pfam05483 230 EYKKEINDKEKQvslLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSM 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1012 DDLQAEEDKVNTLTKAKTKL----EQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKK 1087
Cdd:pfam05483 310 STQKALEEDLQIATKTICQLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKK 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1088 EFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEM 1167
Cdd:pfam05483 390 SSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1168 NKkreaEFQKMRRDLEEATLQHeataatlrkkhadsvAELGEQIDNLQRVKQKLEKEKSEMKMEiddLASNVETVSKAKG 1247
Cdd:pfam05483 470 LK----EVEDLKTELEKEKLKN---------------IELTAHCDKLLLENKELTQEASDMTLE---LKKHQEDIINCKK 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1248 NLEKMCRTLEdqvselkSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKdalvsqlsrgkqaftqqiEELKRQLEEEI 1327
Cdd:pfam05483 528 QEERMLKQIE-------NLEEKEMNLRDELESVREEFIQKGDEVKCKLDKS------------------EENARSIEYEV 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1328 KAKNALAHALQSSrhdCDLLREQYEEEQESKAELQ---RALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAA 1404
Cdd:pfam05483 583 LKKEKQMKILENK---CNNLKKQIENKNKNIEELHqenKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNY 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1405 EEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAAC--------AALDKKQRNFDKILAEWKQKYEETHAELEASQK 1476
Cdd:pfam05483 660 QKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCqhkiaemvALMEKHKHQYDKIIEERDSELGLYKNKEQEQSS 739
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 305632842 1477 EARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAE 1522
Cdd:pfam05483 740 AKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
895-1516 |
9.06e-11 |
|
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: 67.56 E-value: 9.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 895 VQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRkledecSELKKDIDDLELTLAKVEKEKHA 974
Cdd:pfam12128 239 IRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGELSA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 975 TENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAE-----------EDKVNTLTKAKTKL-----EQQVDDL 1038
Cdd:pfam12128 313 ADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSElenleerlkalTGKHQDVTAKYNRRrskikEQNNRDI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1039 EGSLEQEKKLRMDLERAKRKLEGDLKlAQESIMDIENEKQQLDEKLKKKEFE--ISNLQSKIEDEQA---LGIQLQKKIK 1113
Cdd:pfam12128 393 AGIKDKLAKIREARDRQLAVAEDDLQ-ALESELREQLEAGKLEFNEEEYRLKsrLGELKLRLNQATAtpeLLLQLENFDE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1114 EL---QARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRR----DLEEAT 1186
Cdd:pfam12128 472 RIeraREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRkeapDWEQSI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1187 LQHEATAATLRKK-HADSVAELGEQIDNL-------------------QRVKQKLEKEKSEMKMEIDDLASNVETVSKAK 1246
Cdd:pfam12128 552 GKVISPELLHRTDlDPEVWDGSVGGELNLygvkldlkridvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQAN 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1247 GNLEKMCRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEK----DALVSQLSRGKQAFTQQIeelKRQ 1322
Cdd:pfam12128 632 GELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERlnslEAQLKQLDKKHQAWLEEQ---KEQ 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1323 LEEEIKAKNALAHALQSSRHD-CDLLREQYEEEQESKAELQRALSKAN-TEVAQWRTKYETDAIQRTE--ELEEAKKKLA 1398
Cdd:pfam12128 709 KREARTEKQAYWQVVEGALDAqLALLKAAIAARRSGAKAELKALETWYkRDLASLGVDPDVIAKLKREirTLERKIERIA 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1399 QRLQAAEE-----------HVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAAC----AALDKKQ----------RNF 1453
Cdd:pfam12128 789 VRRQEVLRyfdwyqetwlqRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLemerKASEKQQvrlsenlrglRCE 868
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305632842 1454 DKILAEWKQKYEETHAELEASQKEARslgTELFKMKNAYEEsldqlETLKRENKNLQQEISDL 1516
Cdd:pfam12128 869 MSKLATLKEDANSEQAQGSIGERLAQ---LEDLKLKRDYLS-----ESVKKYVEHFKNVIADH 923
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1491-1918 |
1.38e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.33 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1491 AYEESLDQLETLK-RENKNLQQEISDLTEQIAEGGK---RIHELEKIKKQVEQEKCELQAALEEAEASLEHEEgkILRIQ 1566
Cdd:COG4717 50 RLEKEADELFKPQgRKPELNLKELKELEEELKEAEEkeeEYAELQEELEELEEELEELEAELEELREELEKLE--KLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1567 LELNQVKSEVDRKIAEKDEEIDQLKRnhirivesmqstldaEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRN 1646
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEE---------------RLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1647 YrntqgiLKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTS 1726
Cdd:COG4717 193 E------LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1727 LINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKK--EQDTSAHLERMKKNMEQTVKDLQLRLDEA 1804
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1805 EQLALKGGKKQIQKLEARVRELEGE---------VESEQK--RNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVD 1873
Cdd:COG4717 347 EELQELLREAEELEEELQLEELEQEiaallaeagVEDEEElrAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD 426
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 305632842 1874 K--LQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAE 1918
Cdd:COG4717 427 EeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1215-1900 |
2.07e-10 |
|
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: 65.81 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1215 QRVKQKLEKEKSEMK---MEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESgef 1291
Cdd:TIGR04523 36 KQLEKKLKTIKNELKnkeKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEI--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1292 SRQLDEKDALVSQLSRGKQaftqQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTE 1371
Cdd:TIGR04523 113 KNDKEQKNKLEVELNKLEK----QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1372 VAQWRTKYetdaiQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQR 1451
Cdd:TIGR04523 189 IDKIKNKL-----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1452 NFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQleTLKRENKNLQQEISDLTEQIAEGGKRIHELE 1531
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNK--ELKSELKNQEKKLEEIQNQISQNNKIISQLN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1532 KIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLE----------LNQVKSEVDRKIaEKDEEIDQLKRNHIRIVESM 1601
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEnqsykqeiknLESQINDLESKI-QNQEKLNQQKDEQIKKLQQE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1602 QSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNhanrmaaealrnyrntqgilkdtqLHLDDALRTQEDLKEQLAMVERr 1681
Cdd:TIGR04523 421 KELLEKEIERLKETIIKNNSEIKDLTNQDSVKE------------------------LIIKNLDNTRESLETQLKVLSR- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1682 anllqaEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKK 1761
Cdd:TIGR04523 476 ------SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1762 aitdaamMAEELKKEQdtsahLERMKKNMEQTVKDLqlrldeaeqlalkggKKQIQKLEARVRELEGEVESEQKRNAEAV 1841
Cdd:TIGR04523 550 -------DDFELKKEN-----LEKEIDEKNKEIEEL---------------KQTQKSLKKKQEEKQELIDQKEKEKKDLI 602
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 305632842 1842 KGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKF 1900
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKW 661
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1224-1806 |
4.04e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.32 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1224 EKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLE--DQVSELKSKEEEQQRLINDLTAQRGRLQTESGEfsRQLDEKDAL 1301
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1302 VSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHD-CDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYE 1380
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1381 TDAiqrtEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVertnaacAALDKKQRNFDKILAEW 1460
Cdd:COG4913 377 ASA----EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI-------ASLERRKSNIPARLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1461 KQKYEEthaELEASQKEARSLGtELFKMKNAYEESLDQLETLKRENK-------NLQQEISDLTEQIAEGGK-RIHELEK 1532
Cdd:COG4913 446 RDALAE---ALGLDEAELPFVG-ELIEVRPEEERWRGAIERVLGGFAltllvppEHYAAALRWVNRLHLRGRlVYERVRT 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1533 IKKQVEQEKCELQAALEEaeasLEHEEGKILR-IQLELNQvksevdRKIAEKDEEIDQLKRNHIRIVESMQSTLDAE--- 1608
Cdd:COG4913 522 GLPDPERPRLDPDSLAGK----LDFKPHPFRAwLEAELGR------RFDYVCVDSPEELRRHPRAITRAGQVKGNGTrhe 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1609 ------IRSRN----DAIRLKKKMEGDLNEMEIQLNHANRmAAEALRNYRNTQGILKDTQLHLDDALRTQEDLKEQLAMV 1678
Cdd:COG4913 592 kddrrrIRSRYvlgfDNRAKLAALEAELAELEEELAEAEE-RLEALEAELDALQERREALQRLAEYSWDEIDVASAEREI 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1679 ERranlLQAEIEELRAT---LEQTERSRKIAEQELLDASERVQLLHTQntslintKKKLETDISQMQGEMEDILQEARNA 1755
Cdd:COG4913 671 AE----LEAELERLDASsddLAALEEQLEELEAELEELEEELDELKGE-------IGRLEKELEQAEEELDELQDRLEAA 739
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 305632842 1756 EEKAKKAITDAammAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQ 1806
Cdd:COG4913 740 EDLARLELRAL---LEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
918-1118 |
4.10e-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: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 918 QLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT 997
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 998 KEKK----ALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDI 1073
Cdd:COG4942 104 EELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 305632842 1074 ENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQAR 1118
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1198-1775 |
4.69e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 64.92 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1198 KKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDdlasnvetvskakgNLEKMCRTLEDQVSELKSKEEEQQRLINDL 1277
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKSHSITLKEIERLSIEYN--------------NAMDDYNNLKSALNELSSLEDMKNRYESEI 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1278 TAQRGRLQTESGEFSR--QLDEK------DALVSQLSRGKQAFT--QQIEElKRQLEEEIKAKNALAHALQSSRHDCDLL 1347
Cdd:PRK01156 259 KTAESDLSMELEKNNYykELEERhmkiinDPVYKNRNYINDYFKykNDIEN-KKQILSNIDAEINKYHAIIKKLSVLQKD 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1348 REQYEEEQESKAELQRALSKANTevaqwrtkYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQN 1427
Cdd:PRK01156 338 YNDYIKKKSRYDDLNNQILELEG--------YEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1428 EVEDLMLDVERTNAACAALDKKQRNfdkiLAEWKQKYEETHAELEASQKE---ARSLGTE-LFKMKNAYEESLDQLETLK 1503
Cdd:PRK01156 410 ELNEINVKLQDISSKVSSLNQRIRA----LRENLDELSRNMEMLNGQSVCpvcGTTLGEEkSNHIINHYNEKKSRLEEKI 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1504 REnknLQQEISDLTEQIAEGGKRIHELEKikKQVEQEKCELQAaLEEAEASLEHEEGKILRIQlELNQVKSEVDRKIAEK 1583
Cdd:PRK01156 486 RE---IEIEVKDIDEKIVDLKKRKEYLES--EEINKSINEYNK-IESARADLEDIKIKINELK-DKHDKYEEIKNRYKSL 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1584 DEEIDQLKRNHIRIVESMQSTLDAE-IRSRNDAIRLK-KKMEGDLNEMEIQLNHAN-------RMAAEALRNYRNTQGIL 1654
Cdd:PRK01156 559 KLEDLDSKRTSWLNALAVISLIDIEtNRSRSNEIKKQlNDLESRLQEIEIGFPDDKsyidksiREIENEANNLNNKYNEI 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1655 KDTQLHLDDALRTQEDLKEQLAMVERRanllQAEIEELRATLEQTERSRKIAEQELLDAServqllhTQNTSLINTKKKL 1734
Cdd:PRK01156 639 QENKILIEKLRGKIDNYKKQIAEIDSI----IPDLKEITSRINDIEDNLKKSRKALDDAK-------ANRARLESTIEIL 707
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 305632842 1735 ETDISQMQGEMEDIlQEARNAEEKAKKAITDAAMMAEELKK 1775
Cdd:PRK01156 708 RTRINELSDRINDI-NETLESMKKIKKAIGDLKRLREAFDK 747
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
850-1663 |
5.03e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 65.07 E-value: 5.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 850 EKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLA--DAEERCDQL----------IKTKI 917
Cdd:TIGR00606 311 QRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRarDSLIQSLATrleldgfergPFSER 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 918 QLEAKIKEVTERAEDE--------EEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL 989
Cdd:TIGR00606 391 QIKNFHTLVIERQEDEaktaaqlcADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSS 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 990 DETIAKLTKEKKALQEAhqqtldDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQES 1069
Cdd:TIGR00606 471 DRILELDQELRKAEREL------SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDK 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1070 ImdieNEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEE 1149
Cdd:TIGR00606 545 M----DKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQ 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1150 ISERLEEAGGATSAQIEmnkkrEAEFQKMRRDLEEATLQhEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMK 1229
Cdd:TIGR00606 621 LSSYEDKLFDVCGSQDE-----ESDLERLKEEIEKSSKQ-RAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQ 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1230 MEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINdltaqrgRLQTESGEFSRQLdekdalvSQLSRGK 1309
Cdd:TIGR00606 695 EFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIID-------LKEKEIPELRNKL-------QKVNRDI 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1310 QAFTQQIEELKRQLeEEIKAKNALAHALQSsrhDCDLLREQYEEEQESKAELQRALSKANTeVAQWRTKYETDaiQRTEE 1389
Cdd:TIGR00606 761 QRLKNDIEEQETLL-GTIMPEEESAKVCLT---DVTIMERFQMELKDVERKIAQQAAKLQG-SDLDRTVQQVN--QEKQE 833
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1390 LEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHA 1469
Cdd:TIGR00606 834 KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSP 913
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1470 ELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGgkriheLEKIKKQVEQEKCELQAALE 1549
Cdd:TIGR00606 914 LETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDG------KDDYLKQKETELNTVNAQLE 987
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1550 EAEASLE----------------HEEGKILRIQLELNQVKS---EVDRKIAEKDEEIDQLKRNHIRIV-ESMQSTLDAEI 1609
Cdd:TIGR00606 988 ECEKHQEkinedmrlmrqdidtqKIQERWLQDNLTLRKRENelkEVEEELKQHLKEMGQMQVLQMKQEhQKLEENIDLIK 1067
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 305632842 1610 RSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEAlrNYRNTQGILKDTQLHLDD 1663
Cdd:TIGR00606 1068 RNHVLALGRQKGYEKEIKHFKKELREPQFRDAEE--KYREMMIVMRTTELVNKD 1119
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1493-1934 |
5.76e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 5.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1493 EESLDQLETL--KRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEheegkilriqleln 1570
Cdd:PRK02224 186 RGSLDQLKAQieEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-------------- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1571 qvksevdrKIAEKDEEIDQLkRNHIRIVESMQSTLDAEIRSRndairlkkkmegdlnemeiqlnhanRMAAEALRNYRNt 1650
Cdd:PRK02224 252 --------ELETLEAEIEDL-RETIAETEREREELAEEVRDL-------------------------RERLEELEEERD- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1651 qGILKDTQLhlDDAlrTQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINT 1730
Cdd:PRK02224 297 -DLLAEAGL--DDA--DAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1731 KKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLaLK 1810
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAL-LE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1811 GGK---------------------KQIQKLEARVRELEGEVESEQKRnAEAVKGLRKHERRVKELtyqtEEDRKNilrLQ 1869
Cdd:PRK02224 451 AGKcpecgqpvegsphvetieedrERVEELEAELEDLEEEVEEVEER-LERAEDLVEAEDRIERL----EERRED---LE 522
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305632842 1870 DLVDKLQAKVKSYKRQAEEAEEQSNtnlakfrKLQHELEEAEERADIAESQVNKLRVKSREVHTK 1934
Cdd:PRK02224 523 ELIAERRETIEEKRERAEELRERAA-------ELEAEAEEKREAAAEAEEEAEEAREEVAELNSK 580
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1382-1805 |
6.64e-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: 64.70 E-value: 6.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1382 DAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLmldvERtnaacaaldkkqrnFDKILAEwK 1461
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA----ER--------------YQALLKE-K 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1462 QKYEethaeleasqkearslGTELFKMKNAYEEsldQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEK 1541
Cdd:TIGR02169 221 REYE----------------GYELLKEKEALER---QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1542 CELQaaleeaeasleheEGKILRIQLELNQVKSEV---DRKIAEKDEEIDQLKrNHIRIVESMQSTLDAEIRSRNDAIRL 1618
Cdd:TIGR02169 282 KDLG-------------EEEQLRVKEKIGELEAEIaslERSIAEKERELEDAE-ERLAKLEAEIDKLLAEIEELEREIEE 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1619 KKKMEGDLNEmeiqlnhanrmaaealrnyrntqgilkdtqlHLDDALRTQEDLKEQLAMVERRANLLQAEIEELRATLEQ 1698
Cdd:TIGR02169 348 ERKRRDKLTE-------------------------------EYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1699 TERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAitdAAMMAEELKKEQD 1778
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL---AADLSKYEQELYD 473
|
410 420
....*....|....*....|....*..
gi 305632842 1779 TSAHLERmkknMEQTVKDLQLRLDEAE 1805
Cdd:TIGR02169 474 LKEEYDR----VEKELSKLQRELAEAE 496
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1201-1417 |
6.92e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1201 ADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELkskEEEQQRLINDLTAQ 1280
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL---EAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1281 RGRLQTESGEFSRQL---------DEKDALVS-----QLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDL 1346
Cdd:COG4942 96 RAELEAQKEELAELLralyrlgrqPPLALLLSpedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305632842 1347 LREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCAS 1417
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1230-1703 |
7.49e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 7.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1230 MEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGK 1309
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1310 QAFT--QQIEELKRQLEEEIKAKNALAHALQSSRHdcdlLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRT 1387
Cdd:COG4717 126 QLLPlyQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1388 EELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQ--NEVEDLMLDVERTNAACAALDKKQRNFDKILaewkqkye 1465
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAleERLKEARLLLLIAAALLALLGLGGSLLSLIL-------- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1466 eTHAELEASQKEARSLG-TELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCEL 1544
Cdd:COG4717 274 -TIAGVLFLVLGLLALLfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1545 QAALEEAEASLEHEEGKILRIQL-ELNQVKSEVD-RKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAirLKKKM 1622
Cdd:COG4717 353 LREAEELEEELQLEELEQEIAALlAEAGVEDEEElRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL--DEEEL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1623 EGDLNEMEIQLNHANRMAAEALRNYRNTQGILKD--TQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEELRATLEQTE 1700
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELEAELEQleEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
...
gi 305632842 1701 RSR 1703
Cdd:COG4717 511 EER 513
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1666-1935 |
8.27e-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: 8.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1666 RTQEDLKEQLAMVERRANLLQAEIEELRATLE--QTERSRKIAEQELLDASERVQLlhtqnTSLINTKKKLETDISQMQG 1743
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLErlRREREKAERYQALLKEKREYEG-----YELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1744 EMEDILQEARNAEEKAkkaitdaammaEELKKEqdtSAHLERMKKNMEQTVKDLqlrlDEAEQLALKGG----KKQIQKL 1819
Cdd:TIGR02169 245 QLASLEEELEKLTEEI-----------SELEKR---LEEIEQLLEELNKKIKDL----GEEEQLRVKEKigelEAEIASL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1820 EARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAK 1899
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
|
250 260 270
....*....|....*....|....*....|....*.
gi 305632842 1900 FRKLQHELEEAEERADIAESQVNKLRVKSREVHTKV 1935
Cdd:TIGR02169 387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEEL 422
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
894-1213 |
1.31e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 894 QVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAE--------DEEEINAeltakkRKLEDECSELKKDIDDLELT- 964
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREalqrlaeySWDEIDV------ASAEREIAELEAELERLDASs 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 965 --LAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKtkLEQQVDDLEGSl 1042
Cdd:COG4913 685 ddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEERFAAALGD- 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1043 EQEKKLRMDLERAKRKLEGDLKLAQESIMDIenekqqLDEKLKKKEFEISNLQSKIED------------EQALgIQLQK 1110
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEEELERA------MRAFNREWPAETADLDADLESlpeylalldrleEDGL-PEYEE 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1111 KIKELQARIEELEEEIEAerasrAKAEKQRSDLSRELEEISERLEEA--GGATSAQIEMNKKREAEFQKMRRDLEEATLQ 1188
Cdd:COG4913 835 RFKELLNENSIEFVADLL-----SKLRRAIREIKERIDPLNDSLKRIpfGPGRYLRLEARPRPDPEVREFRQELRAVTSG 909
|
330 340
....*....|....*....|....*
gi 305632842 1189 HEATAATLRKKHADSVAELGEQIDN 1213
Cdd:COG4913 910 ASLFDEELSEARFAALKRLIERLRS 934
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
843-1297 |
2.33e-09 |
|
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: 62.53 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 843 LLKSAETEKEMATMK-----EEFQKTKDELAKSEAKRKE-----LEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQL 912
Cdd:pfam10174 264 LLHTEDREEEIKQMEvykshSKFMKNKIDQLKQELSKKEsellaLQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 913 iktkiqlEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDET 992
Cdd:pfam10174 344 -------QTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 993 IAKLTKEKKALQEAHQQ------TLDDLQAEEDKV-NTLTKAKTKLEQQVDDlegSLEQEKKLRMDLERAKRKLEGDLKL 1065
Cdd:pfam10174 417 LAGLKERVKSLQTDSSNtdtaltTLEEALSEKERIiERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1066 AQESIMDIENEKQQLDEKLKKKEFEISNLQskiedeqalgIQLQKKIKELQARIEELEEEIEAERASRAKAEkqRSDLSR 1145
Cdd:pfam10174 494 KESSLIDLKEHASSLASSGLKKDSKLKSLE----------IAVEQKKEECSKLENQLKKAHNAEEAVRTNPE--INDRIR 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1146 ELEEISERLEEAGGATSAQIE--MNKKREAEFQKMRRDLEEATLqhEATAATLRKKHADSVAELgeqidnlqRVKQKLEK 1223
Cdd:pfam10174 562 LLEQEVARYKEESGKAQAEVErlLGILREVENEKNDKDKKIAEL--ESLTLRQMKEQNKKVANI--------KHGQQEMK 631
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305632842 1224 EKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDE 1297
Cdd:pfam10174 632 KKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEE 705
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1052-1592 |
2.37e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 62.61 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1052 LERAKRKLEGDLKLAQESIMDIENekqqLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERA 1131
Cdd:PRK01156 164 LERNYDKLKDVIDMLRAEISNIDY----LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1132 SR-----------------AKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAA 1194
Cdd:PRK01156 240 ALnelssledmknryeseiKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1195 TLRKKHADSVAELGEQIDNLQRVKQKleKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLI 1274
Cdd:PRK01156 320 EINKYHAIIKKLSVLQKDYNDYIKKK--SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEIL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1275 NDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEE 1354
Cdd:PRK01156 398 KIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEK 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1355 ----QESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQ-------------RLQAAEEHVEAVNAKCAS 1417
Cdd:PRK01156 478 ksrlEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESaradledikikinELKDKHDKYEEIKNRYKS 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1418 LEKTKQRLQNEvEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLD 1497
Cdd:PRK01156 558 LKLEDLDSKRT-SWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYN 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1498 QLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVkSEVD 1577
Cdd:PRK01156 637 EIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRI-NELS 715
|
570
....*....|....*
gi 305632842 1578 RKIAEKDEEIDQLKR 1592
Cdd:PRK01156 716 DRINDINETLESMKK 730
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1462-1930 |
2.56e-09 |
|
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: 62.50 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1462 QKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEIS----DLTEQIAEGGKRIHELEKIKKQV 1537
Cdd:pfam01576 15 QKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAarkqELEEILHELESRLEEEEERSQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1538 EQEKCELQAALEEAEASLEHEEGKILRIQLElnqvKSEVDRKIAEKDEEIdqlkrnhiRIVESMQSTLDAEirsrndair 1617
Cdd:pfam01576 95 QNEKKKMQQHIQDLEEQLDEEEAARQKLQLE----KVTTEAKIKKLEEDI--------LLLEDQNSKLSKE--------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1618 lKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEELRATLE 1697
Cdd:pfam01576 154 -RKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1698 QTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQeARNAEEKAKKaitdaammaeelkkeq 1777
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERA-ARNKAEKQRR---------------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1778 DTSAHLERMKKNMEQTVKDlqlrldEAEQLALKGgkkqiqKLEARVRELEGEVESEQKRNAEAVKGLR-KHERRVKELTY 1856
Cdd:pfam01576 296 DLGEELEALKTELEDTLDT------TAAQQELRS------KREQEVTELKKALEEETRSHEAQLQEMRqKHTQALEELTE 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305632842 1857 QTEEDRKNilrlqdlvdklqakvKSYKRQAEEAEEQSNTNL-AKFRKLQHELEEAEERADIAESQVNKLRVKSRE 1930
Cdd:pfam01576 364 QLEQAKRN---------------KANLEKAKQALESENAELqAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE 423
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
984-1857 |
2.75e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 62.67 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 984 EEMAGLDETIAKLTKEK---KALQEAHQQTLDDLQAEEDkvnTLTKAKTKLEQQVDDLEGSL----------EQEKKLRM 1050
Cdd:PRK04863 279 NERRVHLEEALELRRELytsRRQLAAEQYRLVEMARELA---ELNEAESDLEQDYQAASDHLnlvqtalrqqEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1051 DLERAKRKLEGDL---KLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQarieeleeeie 1127
Cdd:PRK04863 356 DLEELEERLEEQNevvEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALE----------- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1128 aerasRAKAEKQRSDLsrELEEISERLEEAggATSAQIEMNKKREAEfQKMRrDLEEATLQHEATAATLRKkhadsvaeL 1207
Cdd:PRK04863 425 -----RAKQLCGLPDL--TADNAEDWLEEF--QAKEQEATEELLSLE-QKLS-VAQAAHSQFEQAYQLVRK--------I 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1208 GEQID--NLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMcRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQ 1285
Cdd:PRK04863 486 AGEVSrsEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQ-QRAERLLAEFCKRLGKNLDDEDELEQLQEELE 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1286 TESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHalqssrhdcdlLREQYEEEQESK------- 1358
Cdd:PRK04863 565 ARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALAR-----------LREQSGEEFEDSqdvteym 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1359 ---AELQRALSKANTEVAQwrtkyetdaiqRTEELEEAKKKLAQ-------RLQAAEEHVEAV----------------- 1411
Cdd:PRK04863 634 qqlLERERELTVERDELAA-----------RKQALDEEIERLSQpggsedpRLNALAERFGGVllseiyddvsledapyf 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1412 -----NAKCA----SLEKTKQRLQNEvEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEEthAELEASQ-KEARSL 1481
Cdd:PRK04863 703 salygPARHAivvpDLSDAAEQLAGL-EDCPEDLYLIEGDPDSFDDSVFSVEELEKAVVVKIAD--RQWRYSRfPEVPLF 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1482 GtelfkmKNAYEESLDQLetlkrenknlQQEISDLTEQIAEGGKRIHELEKIKKQV----------------EQEKCELQ 1545
Cdd:PRK04863 780 G------RAAREKRIEQL----------RAEREELAERYATLSFDVQKLQRLHQAFsrfigshlavafeadpEAELRQLN 843
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1546 AALEEAEASLEHEEGKILRIQLELNQVKSEVD--RKIAekdEEIDQLKRNHI--RIVEsmqstLDAEIRSRNDAIRLKKK 1621
Cdd:PRK04863 844 RRRVELERALADHESQEQQQRSQLEQAKEGLSalNRLL---PRLNLLADETLadRVEE-----IREQLDEAEEAKRFVQQ 915
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1622 MEGDLNEMEIQLNhanrmaaeALRNYRNTQGILKDtqlHLDDALRTQEDLKEQL----AMVERRA--------NLLQAE- 1688
Cdd:PRK04863 916 HGNALAQLEPIVS--------VLQSDPEQFEQLKQ---DYQQAQQTQRDAKQQAfaltEVVQRRAhfsyedaaEMLAKNs 984
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1689 --IEELRATLEQTERSRKIAEQELLDASERvqllHTQN----TSLINTKKKLETDISQMQGEMEDI-LQEARNAEEKakk 1761
Cdd:PRK04863 985 dlNEKLRQRLEQAEQERTRAREQLRQAQAQ----LAQYnqvlASLKSSYDAKRQMLQELKQELQDLgVPADSGAEER--- 1057
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1762 aitdAAMMAEELKKEQDTSahleRMKKN-MEQTVKDLQLRLDEAEqlalkggkKQIQKLEARVRELEGEVESEQKRNAEA 1840
Cdd:PRK04863 1058 ----ARARRDELHARLSAN----RSRRNqLEKQLTFCEAEMDNLT--------KKLRKLERDYHEMREQVVNAKAGWCAV 1121
|
970 980
....*....|....*....|.
gi 305632842 1841 VKGLRKH--ERRV--KELTYQ 1857
Cdd:PRK04863 1122 LRLVKDNgvERRLhrRELAYL 1142
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
835-1508 |
3.56e-09 |
|
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: 62.37 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 835 KLFFKIKPLLKSAETEKEMATMKEEFQKTKDELAKSE--AKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAE------ 906
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEknSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNhhtttr 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 907 ERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDID-------DLELTLAKVEKEKHATENKV 979
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtrdrlaKLNKELASLEQNKNHINNEL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 980 KNLTEEMAGLDETI----------AKLTKEKKALQEAHQQtlddLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLR 1049
Cdd:TIGR00606 615 ESKEEQLSSYEDKLfdvcgsqdeeSDLERLKEEIEKSSKQ----RAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTE 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1050 MDLERAKRKLEGDLKLAqesimdiENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELqarieeleeeieae 1129
Cdd:TIGR00606 691 AELQEFISDLQSKLRLA-------PDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPEL-------------- 749
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1130 rasRAKAEKQRSDLSRELEEISERlEEAGGATSAQIEMNKKREAEFQKMRRdLEEATLQHEataatlrKKHADSVAELge 1209
Cdd:TIGR00606 750 ---RNKLQKVNRDIQRLKNDIEEQ-ETLLGTIMPEEESAKVCLTDVTIMER-FQMELKDVE-------RKIAQQAAKL-- 815
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1210 QIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKS---------------------KEE 1268
Cdd:TIGR00606 816 QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklqigtnlqrrqqfeeqlveLST 895
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1269 EQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLR 1348
Cdd:TIGR00606 896 EVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQK 975
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1349 E-QYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQ------------RTEELEEAKKKLAQRLQAAEEhveavnAKC 1415
Cdd:TIGR00606 976 EtELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQerwlqdnltlrkRENELKEVEEELKQHLKEMGQ------MQV 1049
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1416 ASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWK-QKYEETHAELEASQKEARSLGTELFKMKNAYEE 1494
Cdd:TIGR00606 1050 LQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQfRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQ 1129
|
730
....*....|....
gi 305632842 1495 SLDQLETLKRENKN 1508
Cdd:TIGR00606 1130 AIMKFHSMKMEEIN 1143
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1681-1939 |
5.41e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1681 RANLLQAE--IEELRATLEQTERSRKIAEQ--------ELLDASERVQLLHTQNTSLintkKKLETDISQMQGEMEDILQ 1750
Cdd:COG1196 185 EENLERLEdiLGELERQLEPLERQAEKAERyrelkeelKELEAELLLLKLRELEAEL----EELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1751 EARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlalkggkkQIQKLEARVRELEGEV 1830
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE--------RLEELEEELAELEEEL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1831 ESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEA 1910
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
250 260
....*....|....*....|....*....
gi 305632842 1911 EERADIAESQVNKLRVKSREVHTKVISEE 1939
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEE 441
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1490-1933 |
5.44e-09 |
|
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: 61.38 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1490 NAYEESLDQL-ETL--KRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALE-EAEASLEHEEGKILRI 1565
Cdd:pfam10174 154 GARDESIKKLlEMLqsKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHrRNQLQPDPAKTKALQT 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1566 QLELNQVK-SEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKME---GDLNEMEIQLnHANRMAA 1641
Cdd:pfam10174 234 VIEMKDTKiSSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDqlkQELSKKESEL-LALQTKL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1642 EALRNYRNtqgilkDTQLHLddalrtqEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLH 1721
Cdd:pfam10174 313 ETLTNQNS------DCKQHI-------EVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLA 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1722 TQNTSLINTKKKLETDISQMQGEMEDILQEARNAE-------EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNM-EQT 1793
Cdd:pfam10174 380 GEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDkqlaglkERVKSLQTDSSNTDTALTTLEEALSEKERIIERLkEQR 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1794 VKDLQLRLDEAEQL--ALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDL 1871
Cdd:pfam10174 460 EREDRERLEELESLkkENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQ 539
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 305632842 1872 VDKLQakvksykrQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLRVKSREVHT 1933
Cdd:pfam10174 540 LKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVEN 593
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1392-1602 |
6.39e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1392 EAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAEL 1471
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1472 EASQKEARSLGTELFKMKNA-----------YEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQe 1540
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA- 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 305632842 1541 kceLQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQ 1602
Cdd:COG4942 179 ---LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1673-1895 |
6.56e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1673 EQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEA 1752
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1753 RNAEEKAKKAITDAAMMAE----ELKKEQDTSAHLERMKKNMEQTVKDLQLRLDE--AEQLALKGGKKQIQKLEARVREL 1826
Cdd:COG4942 100 EAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEElrADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305632842 1827 EGEVESEQKRNAEAVKglrKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNT 1895
Cdd:COG4942 180 LAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1176-1926 |
7.69e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 61.01 E-value: 7.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1176 QKMRRDLEEATLQHEATAATLRKKHadSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRT 1255
Cdd:pfam12128 217 RLNRQQVEHWIRDIQAIAGIMKIRP--EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRT 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1256 LEDQVSELKSkeeeqqrlindltAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAftqQIEELKRQLEEEIKAKNALah 1335
Cdd:pfam12128 295 LDDQWKEKRD-------------ELNGELSAADAAVAKDRSELEALEDQHGAFLDA---DIETAAADQEQLPSWQSEL-- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1336 ALQSSRHDCdLLREQYEEEQESKAELQRALSKANTEVAqwRTKYETDAIQRTEELEEAKKKLAqrLQAAEEHV-EAVNAK 1414
Cdd:pfam12128 357 ENLEERLKA-LTGKHQDVTAKYNRRRSKIKEQNNRDIA--GIKDKLAKIREARDRQLAVAEDD--LQALESELrEQLEAG 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1415 CASLEKTKQRLQNEVEDLMLdveRTNAACAALDKK--QRNFDKILaewkqkyEETHAELEASQKEARSLGTELFKMKNAY 1492
Cdd:pfam12128 432 KLEFNEEEYRLKSRLGELKL---RLNQATATPELLlqLENFDERI-------ERAREEQEAANAEVERLQSELRQARKRR 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1493 EESLDQLETLKRENKNLQQEISDLTEQ-IAEGGKRIHEL--------EKIKKQVEQE---KCELQAALEEAEASLEHEEG 1560
Cdd:pfam12128 502 DQASEALRQASRRLEERQSALDELELQlFPQAGTLLHFLrkeapdweQSIGKVISPEllhRTDLDPEVWDGSVGGELNLY 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1561 KIlRIQLELNQVKSEVDRKiaekdeeiDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEiqlnhanrMA 1640
Cdd:pfam12128 582 GV-KLDLKRIDVPEWAASE--------EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREET--------FA 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1641 AEALRNYRNTQGILKDTQLHLDDALrtQEDLKEQLAMVERRANLLQaeieelratleqtersrkiAEQELLDASERVQLL 1720
Cdd:pfam12128 645 RTALKNARLDLRRLFDEKQSEKDKK--NKALAERKDSANERLNSLE-------------------AQLKQLDKKHQAWLE 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1721 HTQNTSLINTKKKletdisqmqgemedilQEARNAEEKAKKAiTDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLR 1800
Cdd:pfam12128 704 EQKEQKREARTEK----------------QAYWQVVEGALDA-QLALLKAAIAARRSGAKAELKALETWYKRDLASLGVD 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1801 LDeaeqlalkggkkQIQKLEARVRELEGEVESEQKRNAEAVKGLR----KHERRVKELTYQTEEDRKNILRLQDLVDKLQ 1876
Cdd:pfam12128 767 PD------------VIAKLKREIRTLERKIERIAVRRQEVLRYFDwyqeTWLQRRPRLATQLSNIERAISELQQQLARLI 834
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 305632842 1877 AKVKSYKRQAEeaeeqsnTNLAKFRKLQHELEEAEERADIAESQVNKLRV 1926
Cdd:pfam12128 835 ADTKLRRAKLE-------MERKASEKQQVRLSENLRGLRCEMSKLATLKE 877
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1066-1281 |
8.39e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 8.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1066 AQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSR 1145
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1146 ELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKhadsVAELGEQIDNLQRVKQKLEKEK 1225
Cdd:COG4942 105 ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERAELEALL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 305632842 1226 SEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTAQR 1281
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
902-1878 |
1.47e-08 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 60.45 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 902 LADAEERCDQLIKTKIqlEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKE-------KHA 974
Cdd:TIGR01612 527 GFDIDQNIKAKLYKEI--EAGLKESYELAKNWKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEiiyinklKLE 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 975 TENKVKNLTEE-----------------MAGLDEtIAKLTKE----------------KKALQEAHQQTLDDLQAE---- 1017
Cdd:TIGR01612 605 LKEKIKNISDKneyikkaidlkkiiennNAYIDE-LAKISPYqvpehlknkdkiystiKSELSKIYEDDIDALYNElssi 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1018 ---------EDKVNtLTKAKTKLEQQVDDLEGSLEQEKKLRM-DLERAKRKLEGDLKLAQESIM-DIENEKQQLDEKLKK 1086
Cdd:TIGR01612 684 vkenaidntEDKAK-LDDLKSKIDKEYDKIQNMETATVELHLsNIENKKNELLDIIVEIKKHIHgEINKDLNKILEDFKN 762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1087 KEFEISNlqsKIEDEQALGIQLQK---KIKELQarieELEEEIEAERASRAKAEKQRSDLSRE-LEEISERLEEaggaTS 1162
Cdd:TIGR01612 763 KEKELSN---KINDYAKEKDELNKyksKISEIK----NHYNDQINIDNIKDEDAKQNYDKSKEyIKTISIKEDE----IF 831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1163 AQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQI--DNLQRVKQKLEKEKS---EMKMEIDDLAS 1237
Cdd:TIGR01612 832 KIINEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEIsdDKLNDYEKKFNDSKSlinEINKSIEEEYQ 911
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1238 NVETVSKAKGNLeKMCRTLEDQVSELKSKeeeqQRLINDLTAQRGRLQTESGEFSRQLDEK--DALVSQLSRGKQAFTQ- 1314
Cdd:TIGR01612 912 NINTLKKVDEYI-KICENTKESIEKFHNK----QNILKEILNKNIDTIKESNLIEKSYKDKfdNTLIDKINELDKAFKDa 986
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1315 QIEELKRQLEEEIKAKNALAHALQSSRHdcDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAK 1394
Cdd:TIGR01612 987 SLNDYEAKNNELIKYFNDLKANLGKNKE--NMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEI 1064
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1395 KKLAQRLQaaEEHVEAVNAKCASLEKTKQRLqnevedlmldvertnaacaaldkKQRNFDKILAEWKQKYEEthaELEAS 1474
Cdd:TIGR01612 1065 GKNIELLN--KEILEEAEINITNFNEIKEKL-----------------------KHYNFDDFGKEENIKYAD---EINKI 1116
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1475 QKEARSLGTELFKMKNAYEESLDQLETLKREnknLQQEISDLtEQIAEGGKRIHELEKIKKQVEQ--EKCELQAALEEAE 1552
Cdd:TIGR01612 1117 KDDIKNLDQKIDHHIKALEEIKKKSENYIDE---IKAQINDL-EDVADKAISNDDPEEIEKKIENivTKIDKKKNIYDEI 1192
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1553 ASLEHEEGKILRIQLELNQVKS-------EVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDaEIRSRNDAIRLKKKMEGD 1625
Cdd:TIGR01612 1193 KKLLNEIAEIEKDKTSLEEVKGinlsygkNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLD-EIKEKSPEIENEMGIEMD 1271
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1626 LN-EME--------------IQLNHANRMAAEALRNYRNTQG---------ILKDTQLHLDDALRTQEDLKEQLAMVERR 1681
Cdd:TIGR01612 1272 IKaEMEtfnishdddkdhhiISKKHDENISDIREKSLKIIEDfseesdindIKKELQKNLLDAQKHNSDINLYLNEIANI 1351
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1682 ANLLQAE-----IEELRATLEQTERSRKIAEQElLDASERVQLLHTQNTSLINTKKKLETD---------ISQMQGEMED 1747
Cdd:TIGR01612 1352 YNILKLNkikkiIDEVKEYTKEIEENNKNIKDE-LDKSEKLIKKIKDDINLEECKSKIESTlddkdidecIKKIKELKNH 1430
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1748 ILQEA-------RNAEE-------------------------KAKKAITDAAMMAEELKKEQDTS-----------AHLE 1784
Cdd:TIGR01612 1431 ILSEEsnidtyfKNADEnnenvlllfkniemadnksqhilkiKKDNATNDHDFNINELKEHIDKSkgckdeadknaKAIE 1510
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1785 RMKKNMEQTVKDLQLRLDEAEQLALKGG----KKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEE 1860
Cdd:TIGR01612 1511 KNKELFEQYKKDVTELLNKYSALAIKNKfaktKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDK 1590
|
1130
....*....|....*...
gi 305632842 1861 DRKNILRLQDLVDKLQAK 1878
Cdd:TIGR01612 1591 SNKAAIDIQLSLENFENK 1608
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
858-1407 |
1.87e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 858 EEFQKTKDELAKSEAKRKEL-----EEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEV-TERAE 931
Cdd:COG4913 262 ERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 932 D-EEEInAELTAKKRKLEDECSELKKDIDDLELTLAKVEKE----KHATENKVKNLTEEMAGLDETIAKLTKEKKALQEA 1006
Cdd:COG4913 342 QlEREI-ERLERELEERERRRARLEALLAALGLPLPASAEEfaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1007 HQQTLDDLQAEEDKVNT----LTKAKTKLEQQVDDLEGSL----------EQEKKLRMDLERA----------------- 1055
Cdd:COG4913 421 LRELEAEIASLERRKSNiparLLALRDALAEALGLDEAELpfvgelievrPEEERWRGAIERVlggfaltllvppehyaa 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1056 ------KRKLEGDL-----KLAQESIMDIENEKQQLDEKLKKKEFEISN-LQSKI---------EDEQAL-----GIQLQ 1109
Cdd:COG4913 501 alrwvnRLHLRGRLvyervRTGLPDPERPRLDPDSLAGKLDFKPHPFRAwLEAELgrrfdyvcvDSPEELrrhprAITRA 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1110 KKIKelqARIEELEEEIEAERASR----AKAEKQRSDLSRELEEISERLEEAggatSAQIEMNKKREAEFQKMRRDLEEA 1185
Cdd:COG4913 581 GQVK---GNGTRHEKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEELAEA----EERLEALEAELDALQERREALQRL 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1186 TLQHEAtaatlrkkhADSVAELGEQIDNLQRVKQKLEKEKSEMkmeiddlasnvetvskakgnlekmcRTLEDQVSELKS 1265
Cdd:COG4913 654 AEYSWD---------EIDVASAEREIAELEAELERLDASSDDL-------------------------AALEEQLEELEA 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1266 KEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAftQQIEELKRQLEEEIKAK--NALAHALQSSRHD 1343
Cdd:COG4913 700 ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEERFAAALGDAveRELRENLEERIDA 777
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305632842 1344 CDLLREQYEEEQESKaeLQRALSKANTEVAQWRTKYET----DAI---QRTEELEEAKKKLAQRLQAAEEH 1407
Cdd:COG4913 778 LRARLNRAEEELERA--MRAFNREWPAETADLDADLESlpeyLALldrLEEDGLPEYEERFKELLNENSIE 846
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1132-1710 |
2.02e-08 |
|
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: 59.37 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1132 SRAKAEKQRSDLSRELEEISerLEEAGGATSAQIEMNKKREAEFQKMRRDLEEatLQHEATAAtlrkkhadsvaeLGEQI 1211
Cdd:pfam05557 12 SQLQNEKKQMELEHKRARIE--LEKKASALKRQLDRESDRNQELQKRIRLLEK--REAEAEEA------------LREQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1212 DNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLindltaqrgrlqtesgef 1291
Cdd:pfam05557 76 ELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEEL------------------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1292 SRQLDEKDALVSQLSRGKQAFTQQIEELKRQlEEEIKaknALAHALQSSRHDCDLLREQyEEEQESKAELQRALSKANTE 1371
Cdd:pfam05557 138 QERLDLLKAKASEAEQLRQNLEKQQSSLAEA-EQRIK---ELEFEIQSQEQDSEIVKNS-KSELARIPELEKELERLREH 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1372 VAQWRTKYETDAIQRtEELEEAKKKLaqrlqaaeEHVEAVNAKCASLEKTKQRLQNEvedlmldvertnaacaaldkkqr 1451
Cdd:pfam05557 213 NKHLNENIENKLLLK-EEVEDLKRKL--------EREEKYREEAATLELEKEKLEQE----------------------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1452 nfdkiLAEWKQKYEETHAELEASQKEARslgtelfkmknayeesldQLETLKRENKNLQQEISDLTEQiaeggkrIHELE 1531
Cdd:pfam05557 261 -----LQSWVKLAQDTGLNLRSPEDLSR------------------RIEQLQQREIVLKEENSSLTSS-------ARQLE 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1532 KIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQlelnqvksevdRKIAEKDEEIDQLKrnhiRIVESMQSTLDAEIRS 1611
Cdd:pfam05557 311 KARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQ-----------RRVLLLTKERDGYR----AILESYDKELTMSNYS 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1612 RNDAIRLK------KKMEGDLNEMEIQLNHANRmaaealrnyrnTQGILKDTQLHLD---DALRTQEDLKEQLAMVERRA 1682
Cdd:pfam05557 376 PQLLERIEeaedmtQKMQAHNEEMEAQLSVAEE-----------ELGGYKQQAQTLErelQALRQQESLADPSYSKEEVD 444
|
570 580
....*....|....*....|....*...
gi 305632842 1683 NLLQaEIEELRATLEQTERSRKIAEQEL 1710
Cdd:pfam05557 445 SLRR-KLETLELERQRLREQKNELEMEL 471
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1166-1939 |
2.02e-08 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 60.07 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1166 EMNKKREAEFQKMRrDLEEATLQ-HEATAATLRKKHADSVAEL-----GEQIDNLQRVKQKLEKEKSEMKMEIDDLASNV 1239
Cdd:TIGR01612 700 DLKSKIDKEYDKIQ-NMETATVElHLSNIENKKNELLDIIVEIkkhihGEINKDLNKILEDFKNKEKELSNKINDYAKEK 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1240 ETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINdltaqrgrlqtESGEFSRQLDEKDALVSQLsrgkqaftqqIEEL 1319
Cdd:TIGR01612 779 DELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYD-----------KSKEYIKTISIKEDEIFKI----------INEM 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1320 KRQLEEEIKAKNALAHAlqssRHDCdllREQYEEEQESKAELqraLSKANTEVAQWR-TKYETDAIQRTEELEEAKKKLA 1398
Cdd:TIGR01612 838 KFMKDDFLNKVDKFINF----ENNC---KEKIDSEHEQFAEL---TNKIKAEISDDKlNDYEKKFNDSKSLINEINKSIE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1399 QR------LQAAEEHVEAVNAKCASLEK--TKQRLQNEVEDLMLDV-ERTNaacaALDKKQRN-FDKILAEWKQKYEETH 1468
Cdd:TIGR01612 908 EEyqnintLKKVDEYIKICENTKESIEKfhNKQNILKEILNKNIDTiKESN----LIEKSYKDkFDNTLIDKINELDKAF 983
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1469 AELEASQKEARSlgTELFKMKNAYEESL---------DQLETLKRENKNLQQEISDLTEQIAEGGKRIH--------ELE 1531
Cdd:TIGR01612 984 KDASLNDYEAKN--NELIKYFNDLKANLgknkenmlyHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHtsiyniidEIE 1061
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1532 K-IKKQVEQEKCELqaaLEEAEASLEHEEGkiLRIQLELNQVKSEVDRKIAEKDEEIDQLKRNhiriVESMQSTLDAEIr 1610
Cdd:TIGR01612 1062 KeIGKNIELLNKEI---LEEAEINITNFNE--IKEKLKHYNFDDFGKEENIKYADEINKIKDD----IKNLDQKIDHHI- 1131
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1611 srNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNyRNTQGILKDTQ---LHLDDALRTQEDLKEQLAMVerranllqA 1687
Cdd:TIGR01612 1132 --KALEEIKKKSENYIDEIKAQINDLEDVADKAISN-DDPEEIEKKIEnivTKIDKKKNIYDEIKKLLNEI--------A 1200
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1688 EIEELRATLEQTersrkiaeqelldasERVQLLHTQNTSLI------NTKKKLETDISQMQGEMEDI--LQEARNAEEKA 1759
Cdd:TIGR01612 1201 EIEKDKTSLEEV---------------KGINLSYGKNLGKLflekidEEKKKSEHMIKAMEAYIEDLdeIKEKSPEIENE 1265
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1760 KKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQlrldeAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNAE 1839
Cdd:TIGR01612 1266 MGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIR-----EKSLKIIEDFSEESDINDIKKELQKNLLDAQKHNSD 1340
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1840 AVKGLRKherrvkeltyqtEEDRKNILRLQDlVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKL------QHELEEAEER 1913
Cdd:TIGR01612 1341 INLYLNE------------IANIYNILKLNK-IKKIIDEVKEYTKEIEENNKNIKDELDKSEKLikkikdDINLEECKSK 1407
|
810 820
....*....|....*....|....*...
gi 305632842 1914 AD--IAESQVNKLRVKSREVHTKVISEE 1939
Cdd:TIGR01612 1408 IEstLDDKDIDECIKKIKELKNHILSEE 1435
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1510-1720 |
2.17e-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: 58.62 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1510 QQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNqvksEVDRKIAEKDEEIDQ 1589
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----ALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1590 LKRNHIRIVESMQSTLDAEIR-SRNDAIRLKKKMEG--DLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALR 1666
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRlGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 305632842 1667 TQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLL 1720
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1385-1831 |
2.48e-08 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 58.93 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1385 QRTEELE-------EAKKKLAQ---RLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFD 1454
Cdd:pfam05622 14 QRCHELDqqvsllqEEKNSLQQenkKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1455 KILAEWKQKYEEthaeLEASQKEARSLGTELFKMKNA-------------YEESLDQLETLKRENKNLQQEISDLTEQIA 1521
Cdd:pfam05622 94 KEVLELQHRNEE----LTSLAEEAQALKDEMDILRESsdkvkkleatvetYKKKLEDLGDLRRQVKLLEERNAEYMQRTL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1522 EGGKRIHELEKIKKQVEQEKCELQaaleEAEASLEHEEGKILRIQLELNQ-------VKSEVDRKIAEKD---EEIDQLK 1591
Cdd:pfam05622 170 QLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKKleekleaLQKEKERLIIERDtlrETNEELR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1592 RNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQgiLKDTQLHLDDALRTQEDL 1671
Cdd:pfam05622 246 CAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRER--LTELQQLLEDANRRKNEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1672 KEQLAMVERRANLLQAEIEELRATLeqtersrkiaeqelldaservQLLHTQNTSLINTKKKLETDISQMQgEMEDILQE 1751
Cdd:pfam05622 324 ETQNRLANQRILELQQQVEELQKAL---------------------QEQGSKAEDSSLLKQKLEEHLEKLH-EAQSELQK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1752 ARNA-EEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNMEQT---VKDLQLRLDEAEQLALKGGKKQIQKLEAR 1822
Cdd:pfam05622 382 KKEQiEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKAksvIKTLDPKQNPASPPEIQALKNQLLEKDKK 461
|
....*....
gi 305632842 1823 VRELEGEVE 1831
Cdd:pfam05622 462 IEHLERDFE 470
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
973-1203 |
3.05e-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: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 973 HATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSL----EQEKKL 1048
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1049 RMDLERAKRKLEGDLKLAQESimdieNEKQQLDEKLKKKEFE-----ISNLQSKIEDEQALGIQLQKKIKELQARIEELE 1123
Cdd:COG4942 96 RAELEAQKEELAELLRALYRL-----GRQPPLALLLSPEDFLdavrrLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1124 EEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADS 1203
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARL----EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
918-1246 |
3.29e-08 |
|
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: 58.37 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 918 QLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT 997
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 998 KEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEK 1077
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1078 QQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSR------------ 1145
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSmaaqrdrtqael 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1146 -----ELEEISERLEEA------GGATSAQ--------IEMNKKR----EAEFQKMRRDLEEATLQHEATAATL------ 1196
Cdd:pfam07888 275 hqarlQAAQLTLQLADAslalreGRARWAQeretlqqsAEADKDRieklSAELQRLEERLQEERMEREKLEVELgrekdc 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 305632842 1197 -RKKHADSVAELGEQIDNL---QRVKQKLEKEKSEMKMEIDDLASNVETVSKAK 1246
Cdd:pfam07888 355 nRVQLSESRRELQELKASLrvaQKEKEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1661-1889 |
3.33e-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: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1661 LDDALRTQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQ 1740
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1741 MQGEMEDILQEA-RNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQlRLDEAEQlALKGGKKQIQKL 1819
Cdd:COG4942 102 QKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-ELAALRA-ELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1820 EARVRELEGEVESEQKRNAEAVKGLRKherRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEA 1889
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEK---ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1291-1891 |
3.47e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.76 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1291 FSRQlDEKDALVSQLSRGKQAFTQQIEELKR-------------QLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQES 1357
Cdd:PRK01156 134 FVGQ-GEMDSLISGDPAQRKKILDEILEINSlernydklkdvidMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKS 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1358 KAELQRALSKANTEVAQWRTKYE--TDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLqNEVEDLMLD 1435
Cdd:PRK01156 213 HSITLKEIERLSIEYNNAMDDYNnlKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERH-MKIINDPVY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1436 VERTNAACAALDKKQ-RNFDKILAEWK---QKYEETHAELEASQKEArslgtelfkmknayeeslDQLETLKRENKNLQQ 1511
Cdd:PRK01156 292 KNRNYINDYFKYKNDiENKKQILSNIDaeiNKYHAIIKKLSVLQKDY------------------NDYIKKKSRYDDLNN 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1512 EISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDR---KIAEKDEEID 1588
Cdd:PRK01156 354 QILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDissKVSSLNQRIR 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1589 QLKRNHIRIVESMQ-----------STLDAEIRSRndaiRLKKKMEGDLNEMEIQLNHANRMAAEalrnyrntqgilkdt 1657
Cdd:PRK01156 434 ALRENLDELSRNMEmlngqsvcpvcGTTLGEEKSN----HIINHYNEKKSRLEEKIREIEIEVKD--------------- 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1658 qlhLDDALRTQEDLKEQLAMVE-RRANLLQAEIEELRATLEQTersrKIAEQELLDASERVQLLHTQNTSL-INTKKKLE 1735
Cdd:PRK01156 495 ---IDEKIVDLKKRKEYLESEEiNKSINEYNKIESARADLEDI----KIKINELKDKHDKYEEIKNRYKSLkLEDLDSKR 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1736 TDISQMQGEMEDILQEA-RNAEEKAKKAITDAAMMAEELKKE-QDTSAHLERMKKNMEQTVKDLQLRLDEAEQLalkggK 1813
Cdd:PRK01156 568 TSWLNALAVISLIDIETnRSRSNEIKKQLNDLESRLQEIEIGfPDDKSYIDKSIREIENEANNLNNKYNEIQEN-----K 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1814 KQIQKLEARVRELE---GEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAE 1890
Cdd:PRK01156 643 ILIEKLRGKIDNYKkqiAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDIN 722
|
.
gi 305632842 1891 E 1891
Cdd:PRK01156 723 E 723
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1349-1586 |
3.94e-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: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1349 EQYEEEQESKAELQRALSKANTEVAQWRTKyETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNE 1428
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1429 vedlmldvertnaacaaLDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKN 1508
Cdd:COG4942 99 -----------------LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305632842 1509 LQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEE 1586
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1005-1494 |
6.43e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1005 EAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQesimdIENEKQQLDEKL 1084
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA-----LEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1085 KKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEEleeeieaeraSRAKAEKQRSDLSRELEEISERLEEAGGATsaq 1164
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQ----------LSLATEEELQDLAEELEELQQRLAELEEEL--- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1165 iemnKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSK 1244
Cdd:COG4717 216 ----EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1245 AKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEElkRQLE 1324
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL--EELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1325 EEIKAknALAHALQSSRHDCDLLREQYEEEQESKAELQRAlskantevaqwrtkyetdaiqrTEELEEAKKKLAQRLQAA 1404
Cdd:COG4717 370 QEIAA--LLAEAGVEDEEELRAALEQAEEYQELKEELEEL----------------------EEQLEELLGELEELLEAL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1405 EEhvEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRnfdkiLAEWKQKYEETHAELEASQKEARSLGTE 1484
Cdd:COG4717 426 DE--EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE-----LAELLQELEELKAELRELAEEWAALKLA 498
|
490
....*....|
gi 305632842 1485 LFKMKNAYEE 1494
Cdd:COG4717 499 LELLEEAREE 508
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
851-1717 |
1.00e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.66 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 851 KEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKiQLEAKIKEVTERA 930
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIE-RYQADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 931 EDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKV-----EKEKHATE-NKVKNLTEEMAGLDEtIAKLTKEKkaLQ 1004
Cdd:PRK04863 365 EEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYqqaldVQQTRAIQyQQAVQALERAKQLCG-LPDLTADN--AE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1005 EAHQQtlddLQAEEDkvnTLTKAKTKLEQQVDDLEGSLEQ-EKKLR--------MDLERAKRKlegdlklAQESIMDIEN 1075
Cdd:PRK04863 442 DWLEE----FQAKEQ---EATEELLSLEQKLSVAQAAHSQfEQAYQlvrkiageVSRSEAWDV-------ARELLRRLRE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1076 EKQQlDEKLKKKEFEISNLQSKIEDEQalgiQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLE 1155
Cdd:PRK04863 508 QRHL-AEQLQQLRMRLSELEQRLRQQQ----RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRM 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1156 EaggaTSAQIEMNKKREAEFQKmrrdLEEATLQHEATAATLRKKHADSVA---ELGEQIDNLQRVKQKLEKEKSEMKMEI 1232
Cdd:PRK04863 583 A----LRQQLEQLQARIQRLAA----RAPAWLAAQDALARLREQSGEEFEdsqDVTEYMQQLLERERELTVERDELAARK 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1233 DDLASNVETVSKAKGNLEKMCRTLEDQ-----VSELKSKEEEQQR--------------LINDLTAQRGRLQTE------ 1287
Cdd:PRK04863 655 QALDEEIERLSQPGGSEDPRLNALAERfggvlLSEIYDDVSLEDApyfsalygparhaiVVPDLSDAAEQLAGLedcped 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1288 ------------SGEFSRQLDEKDALV------SQLSR-------GKQAFTQQIEELKRQLEEEIKAKNALAHALQssrh 1342
Cdd:PRK04863 735 lyliegdpdsfdDSVFSVEELEKAVVVkiadrqWRYSRfpevplfGRAAREKRIEQLRAEREELAERYATLSFDVQ---- 810
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1343 DCDLLREQYEE--------------EQESKA------ELQRALSKANTEVAQWRTKYET--------------------- 1381
Cdd:PRK04863 811 KLQRLHQAFSRfigshlavafeadpEAELRQlnrrrvELERALADHESQEQQQRSQLEQakeglsalnrllprlnllade 890
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1382 DAIQRTEEL-------EEAKKKLAQR-------------LQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNA 1441
Cdd:PRK04863 891 TLADRVEEIreqldeaEEAKRFVQQHgnalaqlepivsvLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAH 970
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1442 -----ACAALDKKQRNFDKILAEWKQKYEE-THAELEASQKEARslgtelFKMKNAYEESLDQLETLKREN-KNLQQEIS 1514
Cdd:PRK04863 971 fsyedAAEMLAKNSDLNEKLRQRLEQAEQErTRAREQLRQAQAQ------LAQYNQVLASLKSSYDAKRQMlQELKQELQ 1044
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1515 DLTEQIAEGgkrihelekIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNqvksEVDRKIAEKDEEIDQLKRNH 1594
Cdd:PRK04863 1045 DLGVPADSG---------AEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMD----NLTKKLRKLERDYHEMREQV 1111
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1595 IRIVESMQSTLDAeIRSRNDAIRLKKKMEGDLNEMEiqLNHANRMAAEALRnyrntQGILKDTqlHLDDALRTQEDLK-- 1672
Cdd:PRK04863 1112 VNAKAGWCAVLRL-VKDNGVERRLHRRELAYLSADE--LRSMSDKALGALR-----LAVADNE--HLRDVLRLSEDPKrp 1181
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305632842 1673 EQL--------AMVERRAN------------LLQAEIEELRATLEQTERsrkiaEQELLDASERV 1717
Cdd:PRK04863 1182 ERKvqfyiavyQHLRERIRqdiirtddpveaIEQMEIELSRLTEELTSR-----EQKLAISSESV 1241
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
863-1320 |
1.01e-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: 57.04 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 863 TKDELAKSEAKRKELEE---KMVTLLKEKNDLQLQVQAEAEGLADAE-ERCDQLIKTKIQLEAKIKEVteraedeEEINA 938
Cdd:pfam05483 360 SLEELLRTEQQRLEKNEdqlKIITMELQKKSSELEEMTKFKNNKEVElEELKKILAEDEKLLDEKKQF-------EKIAE 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 939 ELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT--------KEKKALQEAHQQT 1010
Cdd:pfam05483 433 ELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTahcdklllENKELTQEASDMT 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1011 LDdLQAEEDKVNTLTKAKTKLEQQVDDLEgslEQEKKLRMDLERAKRKL--EGD-----LKLAQESIMDIENEKQQLDEK 1083
Cdd:pfam05483 513 LE-LKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVREEFiqKGDevkckLDKSEENARSIEYEVLKKEKQ 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1084 LKKKEFEISNLQSKIEDEQalgiqlqKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSA 1163
Cdd:pfam05483 589 MKILENKCNNLKKQIENKN-------KNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1164 QIEMNKKREaefQKMRRDLEEAtlqheataatlrKKHADSVAELGEQIDnlQRVKQKLekeksemkmeiddlASNVETVS 1243
Cdd:pfam05483 662 EIEDKKISE---EKLLEEVEKA------------KAIADEAVKLQKEID--KRCQHKI--------------AEMVALME 710
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 305632842 1244 KAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELK 1320
Cdd:pfam05483 711 KHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
845-1458 |
1.03e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.54 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 845 KSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGL---------------------- 902
Cdd:pfam12128 302 KRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLeerlkaltgkhqdvtakynrrr 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 903 ADAEERCDQLIKTKIQLEAKIKEVTER----AED-----EEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKH 973
Cdd:pfam12128 382 SKIKEQNNRDIAGIKDKLAKIREARDRqlavAEDdlqalESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 974 ATENKvKNLTEEMAGLDETIAKLTKEKKALQE-------AHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSL-EQE 1045
Cdd:pfam12128 462 LLLQL-ENFDERIERAREEQEAANAEVERLQSelrqarkRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLlHFL 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1046 KKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDE------KLKKKEFEISnlqSKIEDEQALGIQLQKKIKELQARI 1119
Cdd:pfam12128 541 RKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGElnlygvKLDLKRIDVP---EWAASEEELRERLDKAEEALQSAR 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1120 EeleeeieaeraSRAKAEKQRSDLSRELEEISERLEEAGGAtsaqiemnkkreaeFQKMRRDLEEATLQHEATAATLRKK 1199
Cdd:pfam12128 618 E-----------KQAAAEEQLVQANGELEKASREETFARTA--------------LKNARLDLRRLFDEKQSEKDKKNKA 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1200 HADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGN-LEKMCRTLEDQVSELKSKEEEQqrlindLT 1278
Cdd:pfam12128 673 LAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQvVEGALDAQLALLKAAIAARRSG------AK 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1279 AQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRhdcDLLREQYEEEQESK 1358
Cdd:pfam12128 747 AELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRR---PRLATQLSNIERAI 823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1359 AELQRALSKANTEVAQWRTKYET--DAIQRTE-ELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQneVEDLMLD 1435
Cdd:pfam12128 824 SELQQQLARLIADTKLRRAKLEMerKASEKQQvRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQ--LEDLKLK 901
|
650 660
....*....|....*....|...
gi 305632842 1436 VERtnaACAALDKKQRNFDKILA 1458
Cdd:pfam12128 902 RDY---LSESVKKYVEHFKNVIA 921
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
655-679 |
1.38e-07 |
|
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: 53.12 E-value: 1.38e-07
10 20
....*....|....*....|....*
gi 305632842 655 FRENLNKLMTNLRSTHPHFVRCIIP 679
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
856-1412 |
1.58e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.83 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 856 MKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEE---RCDQLIKTKIQLEAKIKEVTERAED 932
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSalnELSSLEDMKNRYESEIKTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 933 EEEINAELTA--------------KKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIakltk 998
Cdd:PRK01156 268 ELEKNNYYKEleerhmkiindpvyKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYI----- 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 999 EKKALQEAHQQTLDDLQAEEDKVNTLTKaktkleqQVDDLEGSLEQEKKlrmDLERAKRKLEGDLKLAQESIMDIENEKQ 1078
Cdd:PRK01156 343 KKKSRYDDLNNQILELEGYEMDYNSYLK-------SIESLKKKIEEYSK---NIERMSAFISEILKIQEIDPDAIKKELN 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1079 QLDEKLKKKEFEISNLQSKIEdeqalgiQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAG 1158
Cdd:PRK01156 413 EINVKLQDISSKVSSLNQRIR-------ALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKI 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1159 GATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMK-MEIDDLAS 1237
Cdd:PRK01156 486 REIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKsLKLEDLDS 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1238 NVETVSKAKGNLEKMcrtledQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIE 1317
Cdd:PRK01156 566 KRTSWLNALAVISLI------DIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQ 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1318 ELKRQLEE---EIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDaIQRTEELEEAK 1394
Cdd:PRK01156 640 ENKILIEKlrgKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEIL-RTRINELSDRI 718
|
570
....*....|....*...
gi 305632842 1395 KKLAQRLQAAEEHVEAVN 1412
Cdd:PRK01156 719 NDINETLESMKKIKKAIG 736
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
922-1537 |
2.03e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.45 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 922 KIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT---K 998
Cdd:PRK01156 170 KLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSsleD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 999 EKKALQEAHQQTLDDLQAEEDKVNtltkaktkleqqvdDLEGSLEQEKKLRMDLERAKRklegdlklaqESIMDIENEKQ 1078
Cdd:PRK01156 250 MKNRYESEIKTAESDLSMELEKNN--------------YYKELEERHMKIINDPVYKNR----------NYINDYFKYKN 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1079 QLDEKLKKkefeISNLQSKIEDEQAlgiqLQKKIKELQARIEELEeeieaerasraKAEKQRSDLSRELEEISERLEEAG 1158
Cdd:PRK01156 306 DIENKKQI----LSNIDAEINKYHA----IIKKLSVLQKDYNDYI-----------KKKSRYDDLNNQILELEGYEMDYN 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1159 GATSAQIEMNKKREAEFQKMRR---DLEEATLQHEATAATLRKKHAD---SVAELGEQIDNLQRVKQKLEKEKSEMKMEI 1232
Cdd:PRK01156 367 SYLKSIESLKKKIEEYSKNIERmsaFISEILKIQEIDPDAIKKELNEinvKLQDISSKVSSLNQRIRALRENLDELSRNM 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1233 DDL-ASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTAQrgrlqteSGEFSRQLDEKDALVSQLSRGKQA 1311
Cdd:PRK01156 447 EMLnGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDI-------DEKIVDLKKRKEYLESEEINKSIN 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1312 FTQQIEELKRQLEEEIKAKNALAHAlqssrhdcDLLREQYEEEQES-KAELQRALSKANTEVAQWRTKYETDAIQ-RTEE 1389
Cdd:PRK01156 520 EYNKIESARADLEDIKIKINELKDK--------HDKYEEIKNRYKSlKLEDLDSKRTSWLNALAVISLIDIETNRsRSNE 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1390 LEEAKKKLAQRLQAAEEHVEAVNakcASLEKTKQRLQNEVEDL---MLDVERTNAACAALDKKQRNFDKILAEwKQKYEE 1466
Cdd:PRK01156 592 IKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIENEANNLnnkYNEIQENKILIEKLRGKIDNYKKQIAE-IDSIIP 667
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305632842 1467 THAELEAsqkEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQV 1537
Cdd:PRK01156 668 DLKEITS---RINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1132-1334 |
2.07e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1132 SRAKAEKQRSDLSRELEEISERLEEAggatsaqiemnkkrEAEFQKMRRDLEEATLQHEATAATLRKKHADsVAELGEQI 1211
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAA--------------QAELDALQAELEELNEEYNELQAELEALQAE-IDKLQAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1212 DNLQrvkQKLEKEKSEMKM----------------------EIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEE 1269
Cdd:COG3883 75 AEAE---AEIEERREELGEraralyrsggsvsyldvllgseSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305632842 1270 QQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALA 1334
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1254-1495 |
2.71e-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: 55.16 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1254 RTLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNAL 1333
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1334 AHALQssrhdcDLLREQYEEEQESKAELqrALSKANTEVAQWRTKYETDAIQ----RTEELEEAKKKLAQRLQAAEEHVE 1409
Cdd:COG4942 103 KEELA------ELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAParreQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1410 AVNAKCASLEKTKQRLQNEvedlmldvertnaacaaldKKQRNfdKILAEWKQKYEETHAELEASQKEARSLGTELFKMK 1489
Cdd:COG4942 175 ELEALLAELEEERAALEAL-------------------KAERQ--KLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
....*.
gi 305632842 1490 NAYEES 1495
Cdd:COG4942 234 AEAAAA 239
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1668-1916 |
2.90e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1668 QEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKI--AEQELLDASERVQLLHTQNTSLintkkklETDISQMQGEm 1745
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSEL-------ESQLAEARAE- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1746 ediLQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMkknmeqtvkdLQLRLDEAEQLALKGGK-KQIQKLEARVR 1824
Cdd:COG3206 235 ---LAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQL----------AELEAELAELSARYTPNhPDVIALRAQIA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1825 ELEGEVESEQKRNAEAVKG-LRKHERRVKELTYQTEEDRKNILRLQdlvdKLQAKVKSYKRQAEEAEEQSNTNLAKFRKL 1903
Cdd:COG3206 302 ALRAQLQQEAQRILASLEAeLEALQAREASLQAQLAQLEARLAELP----ELEAELRRLEREVEVARELYESLLQRLEEA 377
|
250
....*....|...
gi 305632842 1904 QheLEEAEERADI 1916
Cdd:COG3206 378 R--LAEALTVGNV 388
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1095-1329 |
3.37e-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: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1095 QSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEaggaTSAQIEMNKKREAE 1174
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA----LEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1175 FQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETvskakgnlekmcr 1254
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE------------- 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305632842 1255 tLEDQVSELKSKEEEQQRLINDLTAQRGRLQtesgefsRQLDEKDALVSQLSRGKQAFTQQIEELKRQ---LEEEIKA 1329
Cdd:COG4942 162 -LAALRAELEAERAELEALLAELEEERAALE-------ALKAERQKLLARLEKELAELAAELAELQQEaeeLEALIAR 231
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1391-1612 |
3.37e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1391 EEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAAcaaLDKKQRNFDKILAEWKQKYEETHAE 1470
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE---IDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1471 LEASQKEARSLGT-ELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEggkriheLEKIKKQVEQEKCELQAALE 1549
Cdd:COG3883 92 ARALYRSGGSVSYlDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAE-------LEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305632842 1550 EAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSR 1612
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1436-1913 |
3.78e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1436 VERTNAACAALDKKQRNFDKILAEwKQKYEETHAELEASQKEARSLGTELFKMKNAYEEsLDQLETLKRENKNLQQEISD 1515
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQLLPL-YQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1516 LTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHI 1595
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1596 RIVESMQSTLDAEIRSRNDAIRLkkkmegDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRTQEDLKEQL 1675
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLL------IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1676 AMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLEtdISQMQGEMEDILQEARNA 1755
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1756 EEkakKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlalkggKKQIQKLEARVRELEGEVESEQK 1835
Cdd:COG4717 383 DE---EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL------EEELEELEEELEELEEELEELRE 453
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305632842 1836 RNAEAVKGLRKHERrvkeltyqteedrknilrlQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEER 1913
Cdd:COG4717 454 ELAELEAELEQLEE-------------------DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
848-1245 |
3.96e-07 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 55.15 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 848 ETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEgladaEERCDQLIKTKIQLEAKIKEVT 927
Cdd:pfam09731 53 EDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEE-----KEATKDAAEAKAQLPKSEQEKE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 928 ERAEDEEEINAELTAKKRKLEdecselkkdiddLELTLAKVEKEKHATEN-KVKNLTEEMAGLDETIAKLTKEKKALQEA 1006
Cdd:pfam09731 128 KALEEVLKEAISKAESATAVA------------KEAKDDAIQAVKAHTDSlKEASDTAEISREKATDSALQKAEALAEKL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1007 HQQTLDDLQAEEDKVN-TLTKAKTKLEQQVDDL---EGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDE 1082
Cdd:pfam09731 196 KEVINLAKQSEEEAAPpLLDAAPETPPKLPEHLdnvEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1083 KLKKkeFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEaerasrakaEKQRSDLSRELEEISERLEEAGGATS 1162
Cdd:pfam09731 276 EDNL--LSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERAL---------EKQKEELDKLAEELSARLEEVRAADE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1163 AQIEmnKKREAEFQKMRRDLEE---ATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNV 1239
Cdd:pfam09731 345 AQLR--LEFEREREEIRESYEEklrTELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEERAGRLLKLNELLANL 422
|
....*.
gi 305632842 1240 ETVSKA 1245
Cdd:pfam09731 423 KGLEKA 428
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
821-1613 |
5.74e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 55.06 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 821 NIRAFMNVKHWPWMKLFFKIKPLLKSAETEKemaTMKEEFQKT----KDELAK--SEAKRKELEEKMVTLLKEKNDLQLQ 894
Cdd:TIGR01612 932 SIEKFHNKQNILKEILNKNIDTIKESNLIEK---SYKDKFDNTlidkINELDKafKDASLNDYEAKNNELIKYFNDLKAN 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 895 VQAEAEGLA----DAEERCDQLIKTKIQ------------LEAKIKEVTERAEDEEEINAELTAKK--RKLEDECSELKK 956
Cdd:TIGR01612 1009 LGKNKENMLyhqfDEKEKATNDIEQKIEdanknipnieiaIHTSIYNIIDEIEKEIGKNIELLNKEilEEAEINITNFNE 1088
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 957 DIDDLEL----TLAKVEKEKHATE-NKVKNlteEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEedkVNTLTKAKTKL 1031
Cdd:TIGR01612 1089 IKEKLKHynfdDFGKEENIKYADEiNKIKD---DIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQ---INDLEDVADKA 1162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1032 EQQvDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQEsIMDIENEK----------------------QQLDEKLKKKEF 1089
Cdd:TIGR01612 1163 ISN-DDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNE-IAEIEKDKtsleevkginlsygknlgklflEKIDEEKKKSEH 1240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1090 EISNLQSKIEDEQALGIQLQKKIKELqARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEaggatSAQIEMNK 1169
Cdd:TIGR01612 1241 MIKAMEAYIEDLDEIKEKSPEIENEM-GIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREK-----SLKIIEDF 1314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1170 KREAEFQKMRRDLEEATLQHEataatlrkKHADSVAELGEQIDNLQRVKQ--KLEKEKSEMKMEIDDLASNVETVSKAKG 1247
Cdd:TIGR01612 1315 SEESDINDIKKELQKNLLDAQ--------KHNSDINLYLNEIANIYNILKlnKIKKIIDEVKEYTKEIEENNKNIKDELD 1386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1248 NLEKMCRTLEDQVS--ELKSKEEEQ------QRLINDLTAQRGRLQTESGE---FSRQLDEKDALVSQLSRgkqafTQQI 1316
Cdd:TIGR01612 1387 KSEKLIKKIKDDINleECKSKIESTlddkdiDECIKKIKELKNHILSEESNidtYFKNADENNENVLLLFK-----NIEM 1461
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1317 EELKRQLEEEIKAKNAlahalqSSRHDCDL--LREQYEEEQESKAELQRalskantevaqwrtkyETDAIQRTEELEEAK 1394
Cdd:TIGR01612 1462 ADNKSQHILKIKKDNA------TNDHDFNIneLKEHIDKSKGCKDEADK----------------NAKAIEKNKELFEQY 1519
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1395 KKLAQRLQAAEEHVEAVNaKCASLEKTKQRLQNEVEDL----MLDVERTNAACAALDKKQRNFDKILAewkqKYEETHAE 1470
Cdd:TIGR01612 1520 KKDVTELLNKYSALAIKN-KFAKTKKDSEIIIKEIKDAhkkfILEAEKSEQKIKEIKKEKFRIEDDAA----KNDKSNKA 1594
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1471 LEASQKEARSLGTELFKMKNAYEESLDQLetlkRENKNLQQEISDLT-----EQIAEGGKRIHELEKIKKQVEQEKcelq 1545
Cdd:TIGR01612 1595 AIDIQLSLENFENKFLKISDIKKKINDCL----KETESIEKKISSFSidsqdTELKENGDNLNSLQEFLESLKDQK---- 1666
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305632842 1546 AALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIR-IVESMQSTLDAEIRSRN 1613
Cdd:TIGR01612 1667 KNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEIEsIKELIEPTIENLISSFN 1735
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
866-1021 |
7.37e-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: 52.23 E-value: 7.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 866 ELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTER-AEDEEEINAELTAKK 944
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARiKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305632842 945 RK-LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKV 1021
Cdd:COG1579 91 YEaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1193-1554 |
7.48e-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: 54.13 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1193 AATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQR 1272
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1273 LINDLTAQRGRLQTESGEFS---RQLDEKDALVSQLSRGKQA----FTQQIEELKRQLEEEIKAKNALAHALQSSRHDCD 1345
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEariRELEEDIKTLTQRVLERETelerMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1346 LLREQYEEEQESKAELQRALSKANTEVAQWRTKYETdAIQRTEELEEAKKKLA---QRLQAAEEHVEAVNAKCASLEKTK 1422
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTT-AHRKEAENEALLEELRslqERLNASERKVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1423 QRLQNEVEDLMLDVERTNAACAALDKKQRNFDkilAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEE-------- 1494
Cdd:pfam07888 268 DRTQAELHQARLQAAQLTLQLADASLALREGR---ARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEermerekl 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 305632842 1495 ----------SLDQLETLKRENKNL-------QQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEAS 1554
Cdd:pfam07888 345 evelgrekdcNRVQLSESRRELQELkaslrvaQKEKEQLQAEKQELLEYIRQLEQRLETVADAKWSEAALTSTERPD 421
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
850-1839 |
8.09e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 54.67 E-value: 8.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 850 EKEMATMKEEFQKTKDELAKSEAKRKELeekmvtllkeKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTER 929
Cdd:TIGR01612 764 EKELSNKINDYAKEKDELNKYKSKISEI----------KNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKI 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 930 AEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVekekhatENKVKNlteEMAglDETIAKLTKEKKALQEAHQQ 1009
Cdd:TIGR01612 834 INEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAEL-------TNKIKA---EIS--DDKLNDYEKKFNDSKSLINE 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1010 TLDDLQAEEDKVNTLtkakTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKL--KKK 1087
Cdd:TIGR01612 902 INKSIEEEYQNINTL----KKVDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLidKIN 977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1088 EFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASraKAEKQRSDLSRELEE------------------ 1149
Cdd:TIGR01612 978 ELDKAFKDASLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQFD--EKEKATNDIEQKIEDanknipnieiaihtsiyn 1055
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1150 ISERLEEAGGATSAQIEMNKKREAE-----FQKMRRDLEEATLQHEATAATLR-----KKHADSVAELGEQIDN----LQ 1215
Cdd:TIGR01612 1056 IIDEIEKEIGKNIELLNKEILEEAEinitnFNEIKEKLKHYNFDDFGKEENIKyadeiNKIKDDIKNLDQKIDHhikaLE 1135
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1216 RVKQKLEKEKSEMKMEIDDLaSNVETVSKAKGNLEKMCRTLEDQVSELKSKE---EEQQRLINDLTaqrgrlQTESGEFS 1292
Cdd:TIGR01612 1136 EIKKKSENYIDEIKAQINDL-EDVADKAISNDDPEEIEKKIENIVTKIDKKKniyDEIKKLLNEIA------EIEKDKTS 1208
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1293 rqLDEKDALvsQLSRGK---QAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQrALSKAN 1369
Cdd:TIGR01612 1209 --LEEVKGI--NLSYGKnlgKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEME-TFNISH 1283
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1370 TEvaqwRTKYETDAIQRTEELEEAKKKLAQRLQAaeehveavNAKCASLEKTKQRLQNEVedlmLDVERTNAACAALDKK 1449
Cdd:TIGR01612 1284 DD----DKDHHIISKKHDENISDIREKSLKIIED--------FSEESDINDIKKELQKNL----LDAQKHNSDINLYLNE 1347
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1450 QRNFDKILaewkqkyeethaeleasqkearslgtELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIaeggkrihe 1529
Cdd:TIGR01612 1348 IANIYNIL--------------------------KLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLI--------- 1392
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1530 lEKIKKQVEQEKCElqaalEEAEASLEHEE--GKILRIQLELNQVKSEVDR-----KIAEKDEEIDQLKRNHIRIVESmQ 1602
Cdd:TIGR01612 1393 -KKIKDDINLEECK-----SKIESTLDDKDidECIKKIKELKNHILSEESNidtyfKNADENNENVLLLFKNIEMADN-K 1465
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1603 STLDAEIRSRNDAirlkKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQG---ILKDTQLHLDDALR--TQEDLKEQLAM 1677
Cdd:TIGR01612 1466 SQHILKIKKDNAT----NDHDFNINELKEHIDKSKGCKDEADKNAKAIEKnkeLFEQYKKDVTELLNkySALAIKNKFAK 1541
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1678 VERRANLLQAEIEELRA--TLEQTERSRKIAE--QELLDASERVQLLHTQNTSLINTKKKLET------DISQMQGEMED 1747
Cdd:TIGR01612 1542 TKKDSEIIIKEIKDAHKkfILEAEKSEQKIKEikKEKFRIEDDAAKNDKSNKAAIDIQLSLENfenkflKISDIKKKIND 1621
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1748 ILQEARNAEEKAKKAITDAamMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRldeaeqlalkggKKQIQKLEARVRELE 1827
Cdd:TIGR01612 1622 CLKETESIEKKISSFSIDS--QDTELKENGDNLNSLQEFLESLKDQKKNIEDK------------KKELDELDSEIEKIE 1687
|
1050
....*....|..
gi 305632842 1828 GEVEsEQKRNAE 1839
Cdd:TIGR01612 1688 IDVD-QHKKNYE 1698
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1677-1939 |
8.42e-07 |
|
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: 54.29 E-value: 8.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1677 MVERranLLQAEIEELRATLEQ-------TERsRKIAEQELLDASE---RVQLLHTQntslinTKKKLETdiSQMQGEME 1746
Cdd:TIGR02168 145 KISE---IIEAKPEERRAIFEEaagiskyKER-RKETERKLERTREnldRLEDILNE------LERQLKS--LERQAEKA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1747 DILQEARNAEEKAKKAItdAAMMAEELKKEQDTsahLERMKKNMEQTVKDLQLRLDEAEQlalkggkkQIQKLEARVREL 1826
Cdd:TIGR02168 213 ERYKELKAELRELELAL--LVLRLEELREELEE---LQEELKEAEEELEELTAELQELEE--------KLEELRLEVSEL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1827 EGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHE 1906
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
250 260 270
....*....|....*....|....*....|...
gi 305632842 1907 LEEAEERADIAESQVNKLRVKSREVHTKVISEE 1939
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1469-1621 |
8.78e-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: 52.23 E-value: 8.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1469 AELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRI-------------HELEKIKK 1535
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnkeyealqKEIESLKR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1536 QV---EQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNhiriVESMQSTLDAEIRSR 1612
Cdd:COG1579 104 RIsdlEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE----REELAAKIPPELLAL 179
|
....*....
gi 305632842 1613 NDAIRLKKK 1621
Cdd:COG1579 180 YERIRKRKN 188
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1454-1619 |
8.89e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 8.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1454 DKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAE----------- 1522
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreelgerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1523 ----GG------------------KRIHELEKI----KKQVEQEKcELQAALEEAEASLEHEEGKILRIQLELNQVKSEV 1576
Cdd:COG3883 95 lyrsGGsvsyldvllgsesfsdflDRLSALSKIadadADLLEELK-ADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 305632842 1577 DRKIAEKDEEIDQLKRNhIRIVESMQSTLDAEIRSRNDAIRLK 1619
Cdd:COG3883 174 EAQQAEQEALLAQLSAE-EAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1081-1326 |
9.45e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 9.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1081 DEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIeeleeeieaerasrAKAEKQRSDLSRELEEISERLEEAgga 1160
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEY--------------NELQAELEALQAEIDKLQAEIAEA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1161 tSAQIEmnkKREAEFQKMRRDLEEATLQHEATAATLrkkHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVE 1240
Cdd:COG3883 78 -EAEIE---ERREELGERARALYRSGGSVSYLDVLL---GSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1241 TVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELK 1320
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
....*.
gi 305632842 1321 RQLEEE 1326
Cdd:COG3883 231 AAAAAA 236
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
857-1047 |
1.41e-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: 52.84 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 857 KEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEI 936
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 937 NAELTAKKRKLEDECS-------------------------ELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDE 991
Cdd:COG4942 106 LAELLRALYRLGRQPPlalllspedfldavrrlqylkylapARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 305632842 992 TIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKK 1047
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1250-1522 |
1.65e-06 |
|
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: 53.32 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1250 EKMCRtLEDQVSELKSK-------EEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQ 1322
Cdd:pfam09726 395 DALVR-LEQDIKKLKAElqasrqtEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKR 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1323 LEEEIKAKNALAHALQSSRhdcdllreQYEEEQESKAELQRALSKANTevaqwrtKYETDAI-QRTEELEEAKKKLAQRL 1401
Cdd:pfam09726 474 LKAEQEARASAEKQLAEEK--------KRKKEEEATAARAVALAAASR-------GECTESLkQRKRELESEIKKLTHDI 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1402 QAAEEHVEAVNAKCASLEKTKQRlQNEVEDLMldvertnAACAALDKKQRNFDKILAewkqkyEETHAELeasqkearsl 1481
Cdd:pfam09726 539 KLKEEQIRELEIKVQELRKYKES-EKDTEVLM-------SALSAMQDKNQHLENSLS------AETRIKL---------- 594
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 305632842 1482 gtELFkmkNAYEESLDQLETLKRENKNLQQEISDLTEQIAE 1522
Cdd:pfam09726 595 --DLF---SALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAE 630
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1563-1913 |
1.79e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1563 LRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESmQSTLDAEIRSRND-------AIRLKKKME---GDLNEMEIQ 1632
Cdd:PRK04863 285 LEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEA-ESDLEQDYQAASDhlnlvqtALRQQEKIEryqADLEELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1633 LNHANRMAAEAlrnyrntQGILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQaeieelratleqterSRKIAEQELLD 1712
Cdd:PRK04863 364 LEEQNEVVEEA-------DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQ---------------TRAIQYQQAVQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1713 ASERVQLLhTQNTSLinTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERmkKNMEQ 1792
Cdd:PRK04863 422 ALERAKQL-CGLPDL--TADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSR--SEAWD 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1793 TVKDLQLRLDEAEQLAlkggkKQIQKLEARVRELEGEVESEQkrnaEAVKGLRKHERRVkELTYQTEEDrknilrLQDLV 1872
Cdd:PRK04863 497 VARELLRRLREQRHLA-----EQLQQLRMRLSELEQRLRQQQ----RAERLLAEFCKRL-GKNLDDEDE------LEQLQ 560
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 305632842 1873 DKLQAKVKSYKRQAEEAEEQSNTnlakfrkLQHELEEAEER 1913
Cdd:PRK04863 561 EELEARLESLSESVSEARERRMA-------LRQQLEQLQAR 594
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
984-1866 |
1.84e-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: 53.42 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 984 EEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEED---KVNTLTKAKTKLEQQVDDLEgsleqekklrmDLERAKRKLE 1060
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAASDhlnLVQTALRQQEKIERYQEDLE-----------ELTERLEEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1061 GDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQarieeleeeieaerasRAKAEKQR 1140
Cdd:COG3096 368 EVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALE----------------KARALCGL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1141 SDLSreLEEISERLEEAGGATSAQIEmnKKREAEfQKMRrDLEEATLQHEATAATLRK-------KHADSVA-ELGEQID 1212
Cdd:COG3096 432 PDLT--PENAEDYLAAFRAKEQQATE--EVLELE-QKLS-VADAARRQFEKAYELVCKiageverSQAWQTArELLRRYR 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1213 NLQRVKQKLEkeksEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLindlTAQRGRLQTESGEFS 1292
Cdd:COG3096 506 SQQALAQRLQ----QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAEL----EAQLEELEEQAAEAV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1293 RQLdekdalvSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHalqssrhdcdlLREQYEEEQESKAELQRALSK-ANTE 1371
Cdd:COG3096 578 EQR-------SELRQQLEQLRARIKELAARAPAWLAAQDALER-----------LREQSGEALADSQEVTAAMQQlLERE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1372 VAQWRTKYEtdAIQRTEELEEAKKKLAQ-------RLQAAEEHVEAVnakcaslektkqrLQNEV-EDLMLD-------- 1435
Cdd:COG3096 640 REATVERDE--LAARKQALESQIERLSQpggaedpRLLALAERLGGV-------------LLSEIyDDVTLEdapyfsal 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1436 ---------VERTNAACAALDKK----------QRNFDKILAEWKQKYEETHAEL-EASQKEAR-SLGTELFKMKNAYEE 1494
Cdd:COG3096 705 ygparhaivVPDLSAVKEQLAGLedcpedlyliEGDPDSFDDSVFDAEELEDAVVvKLSDRQWRySRFPEVPLFGRAARE 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1495 SldQLETLKRENKnlqqeisDLTEQIAEGGKRIHELEKIKKQVEQ----------------EKCELQAALEEAEASLEHE 1558
Cdd:COG3096 785 K--RLEELRAERD-------ELAEQYAKASFDVQKLQRLHQAFSQfvgghlavafapdpeaELAALRQRRSELERELAQH 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1559 EGKILRIQLELNQVKSEVD--RKIA----------------EKDEEIDQLK---------RNHIRIVESMQSTLDAEIRS 1611
Cdd:COG3096 856 RAQEQQLRQQLDQLKEQLQllNKLLpqanlladetladrleELREELDAAQeaqafiqqhGKALAQLEPLVAVLQSDPEQ 935
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1612 rNDAIRLkkkmegDLNEMEIQLNHAnRMAAEALrnyrnTQGILKDTQLHLDDAlrtQEDLKEQLAMVERranllqaeiee 1691
Cdd:COG3096 936 -FEQLQA------DYLQAKEQQRRL-KQQIFAL-----SEVVQRRPHFSYEDA---VGLLGENSDLNEK----------- 988
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1692 LRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKK-KLETdISQMQGEMEDI-LQEARNAEEKAKkaitdaamm 1769
Cdd:COG3096 989 LRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDaKQQT-LQELEQELEELgVQADAEAEERAR--------- 1058
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1770 aeELKKEQDTSAHLERMKKNmeQTVKDLQLRLDEAEQLAlkggkKQIQKLEARVRELEGEVESeQKRNAEAVKGLRKH-- 1847
Cdd:COG3096 1059 --IRRDELHEELSQNRSRRS--QLEKQLTRCEAEMDSLQ-----KRLRKAERDYKQEREQVVQ-AKAGWCAVLRLARDnd 1128
|
970 980
....*....|....*....|..
gi 305632842 1848 -ERRV--KELTYQTEEDRKNIL 1866
Cdd:COG3096 1129 vERRLhrRELAYLSADELRSMS 1150
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
839-1463 |
2.00e-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: 53.20 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 839 KIKPLLKSAETEKEM-ATMKEEFQKTKDELAKSEAKRKELEEKM-------------VTLLKEKNDLQLQ----VQAEAE 900
Cdd:pfam15921 462 KVSSLTAQLESTKEMlRKVVEELTAKKMTLESSERTVSDLTASLqekeraieatnaeITKLRSRVDLKLQelqhLKNEGD 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 901 GLADAEERCDQLiktKIQLEAK---IKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATEN 977
Cdd:pfam15921 542 HLRNVQTECEAL---KLQMAEKdkvIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDA 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 978 KVKNLTEEMAGLDETIAKLT-------KEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQE-KKLR 1049
Cdd:pfam15921 619 KIRELEARVSDLELEKVKLVnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTtNKLK 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1050 MDLERAKRKLE---GDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIedeqalgiqlqkkikelqariEELEEEI 1126
Cdd:pfam15921 699 MQLKSAQSELEqtrNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKI---------------------QFLEEAM 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1127 EAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQ----------HEATAATL 1196
Cdd:pfam15921 758 TNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQfaecqdiiqrQEQESVRL 837
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1197 RKKHADSVAEL-GEQIDNLQRVKQKLEKEKSEMKMEiDDLASNVETVS-------KAKGNLEKMCRTLEDQVSELKSKEE 1268
Cdd:pfam15921 838 KLQHTLDVKELqGPGYTSNSSMKPRLLQPASFTRTH-SNVPSSQSTASflshhsrKTNALKEDPTRDLKQLLQELRSVIN 916
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1269 EQQRLINDLTAQRGRlQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQ-SSRHDCDLL 1347
Cdd:pfam15921 917 EEPTVQLSKAEDKGR-APSLGALDDRVRDCIIESSLRSDICHSSSNSLQTEGSKSSETCSREPVLLHAGElEDPSSCFTF 995
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1348 REQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKklaqrLQAAEEHVEAVNAKCASLEKTKQRLQN 1427
Cdd:pfam15921 996 PSTASPSVKNSASRSFHSSPKKSPVHSLLTSSAEGSIGSSSQYRSAKT-----IHSPDSVKDSQSLPIETTGKTCRKLQN 1070
|
650 660 670
....*....|....*....|....*....|....*.
gi 305632842 1428 EVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQK 1463
Cdd:pfam15921 1071 RLESLQTLVEDLQLKNQAMSSMIRNQEKRIQKVKDQ 1106
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1282-1701 |
2.03e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.59 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1282 GRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAEL 1361
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1362 ---QRALSKANTEvaqwrtkyetdAIQRTEELEEAKKKLAQRLQAAEehveavnakcASLEKTKQRLQnevedlmldver 1438
Cdd:pfam07888 114 seeKDALLAQRAA-----------HEARIRELEEDIKTLTQRVLERE----------TELERMKERAK------------ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1439 tnaacaaldkkqrnfdKILAEWKQKYEE---THAELEASQKEARSLGTELFKMKNAYEESLDQLETlkrenknLQQEISD 1515
Cdd:pfam07888 161 ----------------KAGAQRKEEEAErkqLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1516 LTEQIAEGGKRIHELEKIKKqveqekcELQAALEEAEASLEHEEGkilrIQLELNQVKSEVDRKIAEKdeeidqlkrnHI 1595
Cdd:pfam07888 218 LTQKLTTAHRKEAENEALLE-------ELRSLQERLNASERKVEG----LGEELSSMAAQRDRTQAEL----------HQ 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1596 RIVESMQSTL---DAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQ-------------GILKDTQL 1659
Cdd:pfam07888 277 ARLQAAQLTLqlaDASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQeermereklevelGREKDCNR 356
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 305632842 1660 -HLDDALRTQEDLKEQLAMVERRANLLQAEIEELRATLEQTER 1701
Cdd:pfam07888 357 vQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQ 399
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1473-1701 |
2.41e-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: 52.07 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1473 ASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAE 1552
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1553 ASLEHEEGKILRiQLELNQVKSEVDR-----------KIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKK 1621
Cdd:COG4942 97 AELEAQKEELAE-LLRALYRLGRQPPlalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1622 MEGDLNEMEIQlnhanRMAAEALRNYRNTQgilkdtqlhLDDALRTQEDLKEQLAMVERRANLLQAEIEELRATLEQTER 1701
Cdd:COG4942 176 LEALLAELEEE-----RAALEALKAERQKL---------LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1579-1930 |
3.21e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 52.60 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1579 KIAEKDEEIDQLKRNHIRIVESM--QSTLDAEIRSRNDAIRLKKKMEGDLNEMEiqlnhaNRMAAEALRNYR--NTQGIL 1654
Cdd:PLN02939 64 KLQSNTDENGQLENTSLRTVMELpqKSTSSDDDHNRASMQRDEAIAAIDNEQQT------NSKDGEQLSDFQleDLVGMI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1655 KDTQ---LHLDDA-LRTQEDLKEQLAmvERRAnlLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINT 1730
Cdd:PLN02939 138 QNAEkniLLLNQArLQALEDLEKILT--EKEA--LQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIR 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1731 KKKLETDISQMQGEMEDILQEarNAEEKAkkaitDAAMMAEELKKEQDTS---AHLERMKKNMEQTVKDLQLRLDEAEQL 1807
Cdd:PLN02939 214 GATEGLCVHSLSKELDVLKEE--NMLLKD-----DIQFLKAELIEVAETEervFKLEKERSLLDASLRELESKFIVAQED 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1808 ALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKH---ERRVKELTYQTEEdrKNILRLQ-DLVDKLQAKVKSYK 1883
Cdd:PLN02939 287 VSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNqdlRDKVDKLEASLKE--ANVSKFSsYKVELLQQKLKLLE 364
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 305632842 1884 RQAEEAEEQSNTNLAKFrklQHELEEAEeraDIAESQVNKLRVKSRE 1930
Cdd:PLN02939 365 ERLQASDHEIHSYIQLY---QESIKEFQ---DTLSKLKEESKKRSLE 405
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1005-1166 |
4.11e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1005 EAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRM-------DLERAKRKLEGDLKLAQEsimDIENEK 1077
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEaakteleDLEKEIKRLELEIEEVEA---RIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1078 QQLDEKLKKKEFEisNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEA 1157
Cdd:COG1579 80 EQLGNVRNNKEYE--ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
....*....
gi 305632842 1158 GGATSAQIE 1166
Cdd:COG1579 158 LEELEAERE 166
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1076-1567 |
4.18e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1076 EKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIeaeraSRAKAEKQRSDLSRELEEISERLE 1155
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1156 EAggatsaqiemnKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDL 1235
Cdd:COG4717 150 EL-----------EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1236 ASNVETVSKAKGNLEKmcrtlEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDAL----------VSQL 1305
Cdd:COG4717 219 QEELEELEEELEQLEN-----ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallFLLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1306 SRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTkyetdaiq 1385
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL-------- 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1386 rtEELEEAKKKLAQRLQAAEEhvEAVNAKCASLEKtkqrlqnevedlmldvertnaacaaldkkqrnfdkiLAEWKQKYE 1465
Cdd:COG4717 366 --EELEQEIAALLAEAGVEDE--EELRAALEQAEE------------------------------------YQELKEELE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1466 ETHAELEASQKEARSLGTELfkmknayeesldQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKC--E 1543
Cdd:COG4717 406 ELEEQLEELLGELEELLEAL------------DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGElaE 473
|
490 500
....*....|....*....|....
gi 305632842 1544 LQAALEEAEASLEHEEGKILRIQL 1567
Cdd:COG4717 474 LLQELEELKAELRELAEEWAALKL 497
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
938-1164 |
4.19e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 938 AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQ-- 1015
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1016 -AEEDKVNTLTKAK--TKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKlaqesimDIENEKQQLDEKLKKKEFEIS 1092
Cdd:COG3883 99 gGSVSYLDVLLGSEsfSDFLDRLSALSKIADADADLLEELKADKAELEAKKA-------ELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 305632842 1093 NLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQ 1164
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1042-1552 |
4.51e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1042 LEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQalgiqLQKKIKELQARIEE 1121
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA-----LEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1122 LEeeieaerasraKAEKQRSDLSRELEEISERLEEAggatsaqiemnkkreaefqkmRRDLEEATLQHEATAATLRKKHA 1201
Cdd:COG4717 151 LE-----------ERLEELRELEEELEELEAELAEL---------------------QEELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1202 DSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKgNLEKMCRTLEdQVSELKSKEEEQQRLINDLTAQR 1281
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE-RLKEARLLLL-IAAALLALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1282 GRLQTESGEFSrqldekdALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAEL 1361
Cdd:COG4717 277 GVLFLVLGLLA-------LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1362 QRALSKANTEVAQWRTKYETDAIQrtEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNA 1441
Cdd:COG4717 350 QELLREAEELEEELQLEELEQEIA--ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1442 acAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTElfkmkNAYEESLDQLETLKRENKNLQQEIS--DLTEQ 1519
Cdd:COG4717 428 --EELEEELEELEEELEELEEELEELREELAELEAELEQLEED-----GELAELLQELEELKAELRELAEEWAalKLALE 500
|
490 500 510
....*....|....*....|....*....|...
gi 305632842 1520 IaeggkriheLEKIKKQVEQEKceLQAALEEAE 1552
Cdd:COG4717 501 L---------LEEAREEYREER--LPPVLERAS 522
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1373-1615 |
4.71e-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: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1373 AQWRTKYETDAIQRTEELEEAKKKLAQrlqaAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRN 1452
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAA----LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1453 FDKILAEWKQKYEEThaeLEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAeggkrihELEK 1532
Cdd:COG4942 95 LRAELEAQKEELAEL---LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-------ELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1533 IKKQVEQEKCELQAALEEAEAslehEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQStLDAEIRSR 1612
Cdd:COG4942 165 LRAELEAERAELEALLAELEE----ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR-LEAEAAAA 239
|
...
gi 305632842 1613 NDA 1615
Cdd:COG4942 240 AER 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1457-1938 |
5.82e-06 |
|
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: 51.65 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1457 LAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQ 1536
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1537 VEQEKCELQAALEEAEASLEHeegkiLRIQLElnQVKSEVDRKIAEKDEEIDQLKRNHIRIV---ESMQSTLDAEIRSRN 1613
Cdd:pfam05483 181 TRQVYMDLNNNIEKMILAFEE-----LRVQAE--NARLEMHFKLKEDHEKIQHLEEEYKKEIndkEKQVSLLLIQITEKE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1614 DAIR----LKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEI 1689
Cdd:pfam05483 254 NKMKdltfLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1690 EELRATLEQTERSRKIAEQELLDASERVQ-LLHTQNTSLINTKKKLETDISQMQ---GEMEDILQEARNAE---EKAKKA 1762
Cdd:pfam05483 334 EAQMEELNKAKAAHSFVVTEFEATTCSLEeLLRTEQQRLEKNEDQLKIITMELQkksSELEEMTKFKNNKEvelEELKKI 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1763 ITDAAMMAEELKKEQDTSahlERMKKNMEQTVKDLQLRLDEAEQLALK--GGKKQIQKLEARVRELEGEVESEQKRNAE- 1839
Cdd:pfam05483 414 LAEDEKLLDEKKQFEKIA---EELKGKEQELIFLLQAREKEIHDLEIQltAIKTSEEHYLKEVEDLKTELEKEKLKNIEl 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1840 --------------------AVKGLRKHERRVKELTYQTEEDRKNILRLQD----LVDKLQAKVKSYKRQAEEAEEQSNT 1895
Cdd:pfam05483 491 tahcdklllenkeltqeasdMTLELKKHQEDIINCKKQEERMLKQIENLEEkemnLRDELESVREEFIQKGDEVKCKLDK 570
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 305632842 1896 NLAKFRKLQHELEEAEERADIAESQVNKLRvKSREVHTKVISE 1938
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNNLK-KQIENKNKNIEE 612
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1493-1691 |
6.41e-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: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1493 EESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKikkqveqEKCELQAALEEAEASLEHEEGKILRIQLELNQv 1572
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA-------EVEELEAELEEKDERIERLERELSEARSEERR- 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1573 KSEVDRKIAEKDEEIDQLKrnhiRIVESMQSTLDaEIRSRNDaiRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQG 1652
Cdd:COG2433 460 EIRKDREISRLDREIERLE----RELEEERERIE-ELKRKLE--RLKELWKLEHSGELVPVKVVEKFTKEAIRRLEEEYG 532
|
170 180 190
....*....|....*....|....*....|....*....
gi 305632842 1653 ILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEE 1691
Cdd:COG2433 533 LKEGDVVYLRDASGAGRSTAELLAEAGPRAVIVPGELSE 571
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1681-1939 |
6.54e-06 |
|
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: 51.60 E-value: 6.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1681 RANLLQAE--IEELRATLEQTERSRKIAE--QELLDASERVQ--LLHTQNTSLINTKKKLETDISQMQGEMEDILQEARN 1754
Cdd:TIGR02168 185 RENLDRLEdiLNELERQLKSLERQAEKAEryKELKAELRELElaLLVLRLEELREELEELQEELKEAEEELEELTAELQE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1755 AEEKAkkaitdaammaEELKKEqdtsahlermKKNMEQTVKDLQLRLDEAEQLaLKGGKKQIQKLEARVRELEGEVESEQ 1834
Cdd:TIGR02168 265 LEEKL-----------EELRLE----------VSELEEEIEELQKELYALANE-ISRLEQQKQILRERLANLERQLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1835 KRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHE-------- 1906
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiaslnnei 402
|
250 260 270
....*....|....*....|....*....|....*....
gi 305632842 1907 ------LEEAEERADIAESQVNKLRVKSREVHTKVISEE 1939
Cdd:TIGR02168 403 erlearLERLEDRRERLQQEIEELLKKLEEAELKELQAE 441
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1015-1245 |
7.09e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 7.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1015 QAEEDKVNTLTKAKTKLEQQVDDLEGSLEQ-EKKlrmdLERAKRK-----LEGDLKLAQESIMDIENEKQQLDEKLKKKE 1088
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEaEAA----LEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1089 FEISNLQSKIED---------EQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEagg 1159
Cdd:COG3206 240 ARLAALRAQLGSgpdalpellQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILA--- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1160 ATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRkkhadsvaELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNV 1239
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAELPELEAELR--------RLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
....*.
gi 305632842 1240 ETVSKA 1245
Cdd:COG3206 389 RVIDPA 394
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1003-1559 |
7.50e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 51.34 E-value: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1003 LQEAHQQTLDD-LQAEEDKVNTLTKAKTKLEQQVDdlegSLEQEKKLRMDLERAKRKLegdlklaQESIMDIENEKQQLD 1081
Cdd:PRK10246 213 LTPEQVQSLTAsLQVLTDEEKQLLTAQQQQQQSLN----WLTRLDELQQEASRRQQAL-------QQALAAEEKAQPQLA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1082 E-KLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAErasRAKAEKQRSDLSRELEEISERLEEAGGA 1160
Cdd:PRK10246 282 AlSLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARI---RHHAAKQSAELQAQQQSLNTWLAEHDRF 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1161 TSAQIEMNKKReAEFQKMRRDLEEATLQHEATAATLRKKHA----------DSVAELGEQIDNLQRVKQKLEKEKSEMKM 1230
Cdd:PRK10246 359 RQWNNELAGWR-AQFSQQTSDREQLRQWQQQLTHAEQKLNAlpaitltltaDEVAAALAQHAEQRPLRQRLVALHGQIVP 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1231 EIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEE---------EQQRLINDLTAQRGRLQT--------------- 1286
Cdd:PRK10246 438 QQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQqladvkticEQEARIKDLEAQRAQLQAgqpcplcgstshpav 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1287 ------ESGEFSRQLDEKDALVSQLS------RGK-QAFTQQI----EELKRQLEEE---IKAKNALAHALQSSRHDCD- 1345
Cdd:PRK10246 518 eayqalEPGVNQSRLDALEKEVKKLGeegaalRGQlDALTKQLqrdeSEAQSLRQEEqalTQQWQAVCASLNITLQPQDd 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1346 ---LLREQYEEEQE-----SKAELQRALSKANTEVAQWRTKYETDAIQRTEELEE----------------AKKKLAQRL 1401
Cdd:PRK10246 598 iqpWLDAQEEHERQlrllsQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGyaltlpqedeeaswlaTRQQEAQSW 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1402 QAAEEHVEAVNAKCASLEKTKQRL------QNEVEDLMLDVER-TNAACAALDKKQRNFDKILAEWKQKYEETHAELEAS 1474
Cdd:PRK10246 678 QQRQNELTALQNRIQQLTPLLETLpqsddlPHSEETVALDNWRqVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTA 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1475 QKEARSLGTELFKMKNAYEESLDQLETLKRENKN-----------------------------------LQQEISDLTEQ 1519
Cdd:PRK10246 758 LQASVFDDQQAFLAALLDEETLTQLEQLKQNLENqrqqaqtlvtqtaqalaqhqqhrpdgldltvtveqIQQELAQLAQQ 837
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 305632842 1520 IAEGGKRIHELEKIKKQVEQEKCELQAALEE-AEASLEHEE 1559
Cdd:PRK10246 838 LRENTTRQGEIRQQLKQDADNRQQQQALMQQiAQATQQVED 878
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1355-1538 |
8.27e-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: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1355 QESKAELQRALSKANTEVAQWRTKYE-TDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLM 1433
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGlVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1434 ldverTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLD-QLETLKRENKNLQQE 1512
Cdd:COG3206 261 -----QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEaELEALQAREASLQAQ 335
|
170 180
....*....|....*....|....*.
gi 305632842 1513 ISDLTEQIAEGGKRIHELEKIKKQVE 1538
Cdd:COG3206 336 LAQLEARLAELPELEAELRRLEREVE 361
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1390-1593 |
8.71e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.78 E-value: 8.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1390 LEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALdkkqrnfdkilaewKQKYEETHA 1469
Cdd:PHA02562 204 IEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKL--------------NTAAAKIKS 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1470 ELEASQKEARSL--GTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEqekcELQAA 1547
Cdd:PHA02562 270 KIEQFQKVIKMYekGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLL----ELKNK 345
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 305632842 1548 LEEAEASLEHEEGKILRIQLELNQVKSEVdrkiAEKDEEIDQLKRN 1593
Cdd:PHA02562 346 ISTNKQSLITLVDKAKKVKAAIEELQAEF----VDNAEELAKLQDE 387
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
864-1090 |
1.05e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 50.67 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 864 KDELAKSEAKRKELEEkMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKI-------QLEAKIKEVTERAEDEEEI 936
Cdd:PLN02939 142 KNILLLNQARLQALED-LEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIhveileeQLEKLRNELLIRGATEGLC 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 937 NAELTAKKRKLEDECSELKKDIDDLELTLAKVEKekhaTENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQtLDDLQA 1016
Cdd:PLN02939 221 VHSLSKELDVLKEENMLLKDDIQFLKAELIEVAE----TEERVFKLEKERSLLDASLRELESKFIVAQEDVSK-LSPLQY 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1017 EE--DKVNTLT----KAKTKLEQ-------------QVDDLEGSLEQE-----------------KKLRMDLERAKRKLE 1060
Cdd:PLN02939 296 DCwwEKVENLQdlldRATNQVEKaalvldqnqdlrdKVDKLEASLKEAnvskfssykvellqqklKLLEERLQASDHEIH 375
|
250 260 270
....*....|....*....|....*....|
gi 305632842 1061 GDLKLAQESIMDIENEKQQLDEKLKKKEFE 1090
Cdd:PLN02939 376 SYIQLYQESIKEFQDTLSKLKEESKKRSLE 405
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1545-1931 |
1.13e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.22 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1545 QAALEEAEASLEHEEGKILRIQLELNQ-VKSEvdrkiAEKDEEIDQLKRNHirivESMQSTLDAEIRSRNDAIrlkKKME 1623
Cdd:PRK04778 104 KHEINEIESLLDLIEEDIEQILEELQElLESE-----EKNREEVEQLKDLY----RELRKSLLANRFSFGPAL---DELE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1624 GDLNEMEIQLNHANRMAAEAlrNYRNTQGILKDTQLHLDDalrTQEDLKEQLAMVERRANLLQAEIEELRATLEQ-TERS 1702
Cdd:PRK04778 172 KQLENLEEEFSQFVELTESG--DYVEAREILDQLEEELAA---LEQIMEEIPELLKELQTELPDQLQELKAGYRElVEEG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1703 RKIAEQELLdasERVQLLHTQNTSLINTKKKLE--------TDISQMQGEMEDILQ---EARNAEEKAKKAITDAAMMAE 1771
Cdd:PRK04778 247 YHLDHLDIE---KEIQDLKEQIDENLALLEELDldeaeeknEEIQERIDQLYDILErevKARKYVEKNSDTLPDFLEHAK 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1772 ELKKEqdTSAHLERMKKNMEqtvkdlqlrLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRV 1851
Cdd:PRK04778 324 EQNKE--LKEEIDRVKQSYT---------LNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQL 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1852 KELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAE---EQSN------TNLAKFRKLQHELEEAEER--------- 1913
Cdd:PRK04778 393 EEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKrylEKSNlpglpeDYLEMFFEVSDEIEALAEEleekpinme 472
|
410 420
....*....|....*....|...
gi 305632842 1914 -----ADIAESQVNKLRVKSREV 1931
Cdd:PRK04778 473 avnrlLEEATEDVETLEEETEEL 495
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
853-1717 |
1.37e-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: 50.34 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 853 MATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLAdaeercdqLIKTKIQLEAKIK-------E 925
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLN--------LVQTALRQQEKIEryqedleE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 926 VTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKekhatenkvknlteemaGLDE--TIA-KLTKEKKA 1002
Cdd:COG3096 359 LTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQ-----------------ALDVqqTRAiQYQQAVQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1003 LQEAHQQT-LDDLqAEEDKVNTLTKAKTKLEQQVDDLegsLEQEKKLRMDlERAKRKLEGDLKLAQEsiMDIENEKQQLD 1081
Cdd:COG3096 422 LEKARALCgLPDL-TPENAEDYLAAFRAKEQQATEEV---LELEQKLSVA-DAARRQFEKAYELVCK--IAGEVERSQAW 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1082 EKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQarieeleeeieaeraSRAKAEKQRSDLSR----------ELEEIS 1151
Cdd:COG3096 495 QTARELLRRYRSQQALAQRLQQLRAQLAELEQRLR---------------QQQNAERLLEEFCQrigqqldaaeELEELL 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1152 ERLEeaggatsAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKK-----HADSVAE-----LGEQIDNLQRV---- 1217
Cdd:COG3096 560 AELE-------AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlAAQDALErlreqSGEALADSQEVtaam 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1218 KQKLEKEKsEMKMEIDDLA-------SNVETVSKAKGNLEKMCRTLEDQVS-ELKSKEEE------------------QQ 1271
Cdd:COG3096 633 QQLLERER-EATVERDELAarkqaleSQIERLSQPGGAEDPRLLALAERLGgVLLSEIYDdvtledapyfsalygparHA 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1272 RLINDLTAQRGRLQTE----------SGE--------FSRQlDEKDALVSQLSR--------------GKQAFTQQIEEL 1319
Cdd:COG3096 712 IVVPDLSAVKEQLAGLedcpedlyliEGDpdsfddsvFDAE-ELEDAVVVKLSDrqwrysrfpevplfGRAAREKRLEEL 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1320 KRQLEEEIK--AKNA--------LAHALQS--SRHDCDLLREQYEEE----QESKAELQRALSKANTEVAQWRTKY---- 1379
Cdd:COG3096 791 RAERDELAEqyAKASfdvqklqrLHQAFSQfvGGHLAVAFAPDPEAElaalRQRRSELERELAQHRAQEQQLRQQLdqlk 870
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1380 -----------------ETDAIQRTEELEEAkkklAQRLQAAEEHVEAVNAKCASLEKTKQRLQN---EVEDLMLDVERT 1439
Cdd:COG3096 871 eqlqllnkllpqanllaDETLADRLEELREE----LDAAQEAQAFIQQHGKALAQLEPLVAVLQSdpeQFEQLQADYLQA 946
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1440 NAACAALdkKQRNFdkILAEWKQK-----YEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEIS 1514
Cdd:COG3096 947 KEQQRRL--KQQIF--ALSEVVQRrphfsYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLA 1022
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1515 DLT-------EQIAEGGKRIHELE-----KIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLE---LNQVKSEVDRK 1579
Cdd:COG3096 1023 SLKssrdakqQTLQELEQELEELGvqadaEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEmdsLQKRLRKAERD 1102
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1580 IAEKDEEIDQLKRNHIRIVEsmqstldaeiRSRNDAirlkkkMEGDLNEMEIQLNHANR---MAAEALRNYRNTQGILKd 1656
Cdd:COG3096 1103 YKQEREQVVQAKAGWCAVLR----------LARDND------VERRLHRRELAYLSADElrsMSDKALGALRLAVADNE- 1165
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1657 tqlHLDDALRTQEDLKEQLAMV-----------ER-----------RANLLQAEIEELRATLEQTERsrkiaEQELLDAS 1714
Cdd:COG3096 1166 ---HLRDALRLSEDPRRPERKVqfyiavyqhlrERirqdiirtddpVEAIEQMEIELARLTEELTSR-----EQKLAISS 1237
|
...
gi 305632842 1715 ERV 1717
Cdd:COG3096 1238 ESV 1240
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1485-1931 |
1.47e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 49.85 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1485 LFKMKNAYEEsLDQLETLKRE--NKNLQQEISDLtEQIAEGGKRIHELEKIKKQ----VEQEKCELQAALEEAEASLEhe 1558
Cdd:pfam06160 2 LLLRKKIYKE-IDELEERKNElmNLPVQEELSKV-KKLNLTGETQEKFEEWRKKwddiVTKSLPDIEELLFEAEELND-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1559 EGKILRIQLELNQVKS---EVDRKIAEKDEEIDQLK------RNHIRIVESMQSTLDAEIRSRNDAI-RLKKKMEGDLNE 1628
Cdd:pfam06160 78 KYRFKKAKKALDEIEElldDIEEDIKQILEELDELLeseeknREEVEELKDKYRELRKTLLANRFSYgPAIDELEKQLAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1629 MEIQLNHANRMAAEAlrNYRNTQGILKDTQLHLDDalrTQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQ 1708
Cdd:pfam06160 158 IEEEFSQFEELTESG--DYLEAREVLEKLEEETDA---LEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGYALEH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1709 elLDASERVQLLHTQNTSLINTKKKLETDisQMQGEMEDI------LQEARNAEEKAKKaitdaammaeELKKEQDT-SA 1781
Cdd:pfam06160 233 --LNVDKEIQQLEEQLEENLALLENLELD--EAEEALEEIeeridqLYDLLEKEVDAKK----------YVEKNLPEiED 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1782 HLERMKKNMEQTVKDLQL-----RLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRN-------AEAVKGLRKHER 1849
Cdd:pfam06160 299 YLEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYselqeelEEILEQLEEIEE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1850 RVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAE----------------EAEEQSNTNLAKFRKLQHELEEAEER 1913
Cdd:pfam06160 379 EQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEksnlpglpesyldyffDVSDEIEDLADELNEVPLNMDEVNRL 458
|
490
....*....|....*...
gi 305632842 1914 ADIAESQVNKLRVKSREV 1931
Cdd:pfam06160 459 LDEAQDDVDTLYEKTEEL 476
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
858-1088 |
1.58e-05 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 50.16 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 858 EEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEErCDQLIKTKIQLEAKIKEVTERAEDeeeIN 937
Cdd:pfam18971 610 DEVKKAQKDLEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANSQKDE-IFALINKEANRDARAIAYTQNLKG---IK 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 938 AELTAKKRKLEDECSELKKDIDDLE----LTLAKVEKEKHATENKVKNLteemaGLD-ETIAKLTKEKKALQEAHQQTLD 1012
Cdd:pfam18971 686 RELSDKLEKISKDLKDFSKSFDEFKngknKDFSKAEETLKALKGSVKDL-----GINpEWISKVENLNAALNEFKNGKNK 760
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305632842 1013 DLqaeedkvNTLTKAKTKLEQQVDDLEGSLEQEKKL-RMDLERAKRKLEGDLKLAQESIMDIEN-EKQQLDEKLKKKE 1088
Cdd:pfam18971 761 DF-------SKVTQAKSDLENSVKDVIINQKVTDKVdNLNQAVSVAKAMGDFSRVEQVLADLKNfSKEQLAQQAQKNE 831
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1352-1481 |
1.60e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1352 EEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRlqaaeehVEAVNAKCASLEKTKQRLQNEVED 1431
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK-------EENLDRKLELLEKREEELEKKEKE 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 305632842 1432 lmldvertnaacaaLDKKQRNFDKILAEWKQKYEETHAELEA----SQKEARSL 1481
Cdd:PRK12704 119 --------------LEQKQQELEKKEEELEELIEEQLQELERisglTAEEAKEI 158
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1731-1930 |
1.94e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1731 KKKLETDISQMQGEMEDiLQEARNAEEKAKKAI---TDAAMMAEELKKEQDTSAHLERMKK-----NMEQTVKDLQLRLD 1802
Cdd:COG4913 220 EPDTFEAADALVEHFDD-LERAHEALEDAREQIellEPIRELAERYAAARERLAELEYLRAalrlwFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1803 EAEQlALKGGKKQIQKLEARVRELEGEVES-EQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKS 1881
Cdd:COG4913 299 ELRA-ELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 305632842 1882 YKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNK-LRVKSRE 1930
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRReLRELEAE 427
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
860-1199 |
2.05e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.45 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 860 FQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKI-----------QLEAKIKEVTE 928
Cdd:PRK04778 100 FRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLanrfsfgpaldELEKQLENLEE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 929 RAEDEEEINAE---LTAKK--RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKN----LTEEMAGLDETiaKLTKE 999
Cdd:PRK04778 180 EFSQFVELTESgdyVEAREilDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyreLVEEGYHLDHL--DIEKE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1000 KKALQEAHQQTLDDLqaEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQ 1079
Cdd:PRK04778 258 IQDLKEQIDENLALL--EELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDR 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1080 LDEKlkkkeFEISnlqskiEDEQALGIQLQKKIKELQARIEELEEEIeaerasrAKAEKQRSDLSRELEEISERLEEAgg 1159
Cdd:PRK04778 336 VKQS-----YTLN------ESELESVRQLEKQLESLEKQYDEITERI-------AEQEIAYSELQEELEEILKQLEEI-- 395
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 305632842 1160 atsaqiemnKKREAEFQKMRRDLEEATLQHEATAATLRKK 1199
Cdd:PRK04778 396 ---------EKEQEKLSEMLQGLRKDELEAREKLERYRNK 426
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1455-1891 |
2.49e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1455 KILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKR--ENKNLQQEISDLTEQIAEGGKRIHELEK 1532
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1533 IKKQVEqekcELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDaEIRSR 1612
Cdd:COG4717 154 RLEELR----ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE-ELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1613 NDAIRLKKKMEGDLNEMEIQLNHANRMAA---------EALRNYRNTQGILKDTQ----LHLDDALRTQEDLKEQLAMVE 1679
Cdd:COG4717 229 LEQLENELEAAALEERLKEARLLLLIAAAllallglggSLLSLILTIAGVLFLVLgllaLLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1680 RRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQ-------------GEME 1746
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiaallaeagvedeEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1747 DILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHL--ERMKKNMEQTVKDLQLRLDEAEQLalkggKKQIQKLEARVR 1824
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeEELEEELEELEEELEELEEELEEL-----REELAELEAELE 463
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305632842 1825 ELEGEVESEQKRnaeavkglRKHERRVKELTYQTEEDRKNILrLQDLVDKLQAKVKSYKRQA--EEAEE 1891
Cdd:COG4717 464 QLEEDGELAELL--------QELEELKAELRELAEEWAALKL-ALELLEEAREEYREERLPPvlERASE 523
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1737-1930 |
2.59e-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: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1737 DISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlALKGGKKQI 1816
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1817 QKLEARVRELEGEVESEQKRNAEAV----KGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQ 1892
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 305632842 1893 SNTNLAKFRKLQHELEEAEERADIAESQVNKLRVKSRE 1930
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1686-1913 |
2.73e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 49.35 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1686 QAEIEELRATLEQTERSRKiaEQELLDASERVQLLHTQNTSlintKKKLETDISQMQgEMEDILQEARNAEEKAKKAITD 1765
Cdd:pfam05557 1 RAELIESKARLSQLQNEKK--QMELEHKRARIELEKKASAL----KRQLDRESDRNQ-ELQKRIRLLEKREAEAEEALRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1766 AAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRL-DEAEQLalkggKKQIQKLEARVRELEGEVESEQKRNAEAVKGL 1844
Cdd:pfam05557 74 QAELNRLKKKYLEALNKKLNEKESQLADAREVISCLkNELSEL-----RRQIQRAELELQSTNSELEELQERLDLLKAKA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305632842 1845 RKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVksykrQAEEAEEQSNTNLAKFRKLQHELEEAEER 1913
Cdd:pfam05557 149 SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQE-----QDSEIVKNSKSELARIPELEKELERLREH 212
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1106-1428 |
3.29e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.97 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1106 IQLQKKIKELQARIEELEEEIEaerasRAKAEKQrsDLSRELEEiSERLEEAGGATSAQIEMNKKREAEFQK--MRRDLE 1183
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQE-----RLRQEKE--EKAREVER-RRKLEEAEKARQAEMDRQAAIYAEQERmaMERERE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1184 EATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIddlasnvETVSKAKGNLEKMCRTLEDQVSEL 1263
Cdd:pfam17380 350 LERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQEL-------EAARKVKILEEERQRKIQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1264 ----KSKEEEQQRLINDLTAQRGRL--QTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKAKnALAHAL 1337
Cdd:pfam17380 423 eqirAEQEEARQREVRRLEEERAREmeRVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK-ILEKEL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1338 QSSRhdcdllREQYEEEQESKAeLQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCAS 1417
Cdd:pfam17380 502 EERK------QAMIEEERKRKL-LEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERE 574
|
330
....*....|.
gi 305632842 1418 LEKTKQRLQNE 1428
Cdd:pfam17380 575 REMMRQIVESE 585
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1453-1914 |
3.40e-05 |
|
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: 49.20 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1453 FDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEisdlTEQIAEGGKRIHELEK 1532
Cdd:TIGR00618 178 YTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ----TQQSHAYLTQKREAQE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1533 IKKQVEQEKCELQAALEEAEAslehEEGKILRIQLELNQVKSEVdrKIAEKDEEIDQLKRNHIRIVESMQSTLdaeiRSR 1612
Cdd:TIGR00618 254 EQLKKQQLLKQLRARIEELRA----QEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQAQRIHTELQSKM----RSR 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1613 NDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGIL-----KDTQLHLDDALRTQEDLKEQLAMVERRANLLQA 1687
Cdd:TIGR00618 324 AKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATsireiSCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1688 EIEELRATLEQTERSRKIAEQELLDASERVQL---------LHTQNTSLINTKKKLE-TDISQMQGEMEDILQEARNAEE 1757
Cdd:TIGR00618 404 ILQREQATIDTRTSAFRDLQGQLAHAKKQQELqqryaelcaAAITCTAQCEKLEKIHlQESAQSLKEREQQLQTKEQIHL 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1758 KAKKAITDAAMMAEELKKEQdtsahLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRN 1837
Cdd:TIGR00618 484 QETRKKAVVLARLLELQEEP-----CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQR 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1838 AE-------AVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEA 1910
Cdd:TIGR00618 559 ASlkeqmqeIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCS 638
|
....
gi 305632842 1911 EERA 1914
Cdd:TIGR00618 639 QELA 642
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1455-1939 |
4.13e-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: 48.89 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1455 KILAEWKQKYEETHAELEASQKEARSLGtelfKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIK 1534
Cdd:TIGR00606 210 KYLKQYKEKACEIRDQITSKEAQLESSR----EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDN 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1535 KQVEQEKCELQAALEEAEASLEHEEG--------KILRIQLE----------LNQVKSEVDRKIAEKDEEIDQ-----LK 1591
Cdd:TIGR00606 286 SELELKMEKVFQGTDEQLNDLYHNHQrtvrekerELVDCQREleklnkerrlLNQEKTELLVEQGRLQLQADRhqehiRA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1592 RNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRTQEDL 1671
Cdd:TIGR00606 366 RDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELK 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1672 KEQLAMVERRANLLQAEIEELRAT----LEQTERSRKiAEQELLDASE---------RVQLLHTQNTSLINTKKKLETDI 1738
Cdd:TIGR00606 446 KEILEKKQEELKFVIKELQQLEGSsdriLELDQELRK-AERELSKAEKnsltetlkkEVKSLQNEKADLDRKLRKLDQEM 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1739 SQMQGEMEDILQEARNAEEKAKK-------------AITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAE 1805
Cdd:TIGR00606 525 EQLNHHTTTRTQMEMLTKDKMDKdeqirkiksrhsdELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1806 QLA------LKGGKKQIQKLEARVRE-------------LEGEVESEQKRNAEAVKGLRKHERRVKELTYQT-------E 1859
Cdd:TIGR00606 605 QNKnhinneLESKEEQLSSYEDKLFDvcgsqdeesdlerLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvcQ 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1860 EDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKVISEE 1939
Cdd:TIGR00606 685 RVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK 764
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
999-1407 |
4.38e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 48.53 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 999 EKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgdlkLAQESIMDIENEKQ 1078
Cdd:pfam05622 8 EKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLE----QLQEENFRLETARD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1079 QLDEKLKKKEFEISNLQSKIEDEQALG---IQLQKKIKELQARIEELEEEIEAERASRAKAEkQRSDLSRELEEISER-- 1153
Cdd:pfam05622 84 DYRIKCEELEKEVLELQHRNEELTSLAeeaQALKDEMDILRESSDKVKKLEATVETYKKKLE-DLGDLRRQVKLLEERna 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1154 --------LEEA---GGATSAQIEMNKKREAEFQKMrrdLEEATLQHEATAATLRKKHadsvaelgEQIDNLQRVKQKLE 1222
Cdd:pfam05622 163 eymqrtlqLEEElkkANALRGQLETYKRQVQELHGK---LSEESKKADKLEFEYKKLE--------EKLEALQKEKERLI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1223 KEKSEMKMEIDDL---ASNVETVSKAKGNLEKMCRTLEDQVSELKSKE--EEQQRLIND----LTAQRGRLQTESGEFSR 1293
Cdd:pfam05622 232 IERDTLRETNEELrcaQLQQAELSQADALLSPSSDPGDNLAAEIMPAEirEKLIRLQHEnkmlRLGQEGSYRERLTELQQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1294 QLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAhalqSSRHDCDLLREQYEEEQESKAELQRALSKANTEVA 1373
Cdd:pfam05622 312 LLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQG----SKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIE 387
|
410 420 430
....*....|....*....|....*....|....
gi 305632842 1374 QWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEH 1407
Cdd:pfam05622 388 ELEPKQDSNLAQKIDELQEALRKKDEDMKAMEER 421
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1317-1826 |
4.68e-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: 48.80 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1317 EELKRQLEEEIKAKNALAHAlqssrhdcdllREQYEEEQESKAELQRALskantevaqwrtkyetdaiqrtEELEEAKKK 1396
Cdd:COG3096 278 NERRELSERALELRRELFGA-----------RRQLAEEQYRLVEMAREL----------------------EELSARESD 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1397 LAQRLQAAEEHVEAVNAKCASLEKTkQRLQNEVEDLMLDVERTNAacaaldkkqrnfdkILAEWKQKYEETHAELEASQK 1476
Cdd:COG3096 325 LEQDYQAASDHLNLVQTALRQQEKI-ERYQEDLEELTERLEEQEE--------------VVEEAAEQLAEAEARLEAAEE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1477 EARSLGTELFKmknaYEESLDQLETlkrenKNLQQeisdlteqiaeggkrihelekikKQVEQEKCELQAALEEAEASLE 1556
Cdd:COG3096 390 EVDSLKSQLAD----YQQALDVQQT-----RAIQY-----------------------QQAVQALEKARALCGLPDLTPE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1557 HEEGKILRIQLELNQVKSEVdrkiaekdeeidqlkrnhiRIVESMQSTLDAEIRSRNDAIRLKKKMEGdlnemEIQLNHA 1636
Cdd:COG3096 438 NAEDYLAAFRAKEQQATEEV-------------------LELEQKLSVADAARRQFEKAYELVCKIAG-----EVERSQA 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1637 NRMAAEALRNYRNTQGILKDTQ---LHLDDA---LRTQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQEL 1710
Cdd:COG3096 494 WQTARELLRRYRSQQALAQRLQqlrAQLAELeqrLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1711 LDASERvqllhtqntsLINTKKKLEtDISQMQGEMEDILQEARNAEEKAKKAitdAAMMAEELKKEQDTSAHlermkknM 1790
Cdd:COG3096 574 AEAVEQ----------RSELRQQLE-QLRARIKELAARAPAWLAAQDALERL---REQSGEALADSQEVTAA-------M 632
|
490 500 510
....*....|....*....|....*....|....*.
gi 305632842 1791 EQTVKDLQLRLDEAEQLAlkggkKQIQKLEARVREL 1826
Cdd:COG3096 633 QQLLEREREATVERDELA-----ARKQALESQIERL 663
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
929-1075 |
4.70e-05 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 47.75 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 929 RAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETI-AKLTKEKKALQEAH 1007
Cdd:cd22656 101 DDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALkDLLTDEGGAIARKE 180
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305632842 1008 qqtLDDLQAEEDKVNT-----LTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIEN 1075
Cdd:cd22656 181 ---IKDLQKELEKLNEeyaakLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEK 250
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1455-1700 |
4.88e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1455 KILAEWKQKYEETHAEL--EASQKEARSLGTELFKMKNAYEESLDQLETLKRENK--NLQQEISDLTEQIAEggkriheL 1530
Cdd:COG3206 152 AVANALAEAYLEQNLELrrEEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSE-------L 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1531 EKIKKQVEQEKCELQAALEEAEASLEHEEGKI--LRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVEsmqstLDAE 1608
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALpeLLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA-----LRAQ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1609 IRSrndairLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRTQEDLkeqlamvERRANLLQAE 1688
Cdd:COG3206 300 IAA------LRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRL-------EREVEVAREL 366
|
250
....*....|..
gi 305632842 1689 IEELRATLEQTE 1700
Cdd:COG3206 367 YESLLQRLEEAR 378
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1224-1582 |
5.01e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.61 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1224 EKSEMKMEIDDLASNVETVskakgnlekmcRTLEDQVSELKSKeeeqqrlINDLTAQRGRlqtesgefsrqldekdalvs 1303
Cdd:pfam00038 2 EKEQLQELNDRLASYIDKV-----------RFLEQQNKLLETK-------ISELRQKKGA-------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1304 QLSRGKQAFTQQIEELKRQLEeeikaknalahalqssrhdcDLLREqyeeeqesKAELQRALSKANTEVAQWRTKYETDA 1383
Cdd:pfam00038 44 EPSRLYSLYEKEIEDLRRQLD--------------------TLTVE--------RARLQLELDNLRLAAEDFRQKYEDEL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1384 IQRTeELEEAKKKLAQRLQAA-------EEHVEAVNAKCASLEKTKQR----LQNEVEDLMLDVERTNAACAALdkkqrn 1452
Cdd:pfam00038 96 NLRT-SAENDLVGLRKDLDEAtlarvdlEAKIESLKEELAFLKKNHEEevreLQAQVSDTQVNVEMDAARKLDL------ 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1453 fDKILAEWKQKYEEtHAELeaSQKEARslgtELFKMKnaYEESLDQLETLKRENKNLQQEISDLTEQIAEggkRIHELEK 1532
Cdd:pfam00038 169 -TSALAEIRAQYEE-IAAK--NREEAE----EWYQSK--LEELQQAAARNGDALRSAKEEITELRRTIQS---LEIELQS 235
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 305632842 1533 IKKQveqeKCELQAALEEAEASLEHE----EGKILRIQLELNQVKSEVDRKIAE 1582
Cdd:pfam00038 236 LKKQ----KASLERQLAETEERYELQladyQELISELEAELQETRQEMARQLRE 285
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1465-1751 |
5.10e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.61 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1465 EETHAELEASQKEARS-LGTELFKMKNAYEESL----DQLETLKRENKNLQQEISDLTEqiaeggkrihELEKIKKQVEQ 1539
Cdd:pfam00038 24 EQQNKLLETKISELRQkKGAEPSRLYSLYEKEIedlrRQLDTLTVERARLQLELDNLRL----------AAEDFRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1540 EkcelQAALEEAEASLeheegKILRIQL-ELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRN-DAIR 1617
Cdd:pfam00038 94 E----LNLRTSAENDL-----VGLRKDLdEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEmDAAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1618 lKKKMEGDLNEMEIQL-NHANRMAAEALRNYRNTQGILKDTQLHLDDALRTQedlKEQLAMVERRANLLQAEIEELRATL 1696
Cdd:pfam00038 165 -KLDLTSALAEIRAQYeEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSA---KEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 305632842 1697 EQTERSrkIAEQElldasERVQLLHTQNTSLINtkkKLETDISQMQGEMEDILQE 1751
Cdd:pfam00038 241 ASLERQ--LAETE-----ERYELQLADYQELIS---ELEAELQETRQEMARQLRE 285
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1231-1374 |
5.66e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.65 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1231 EIDDLASNVETVSKAKGNLEKMCRTLEDQVS----ELKSKEEEQQRL---INDLTAQRGRLQTESGEFSRQLDEKDALVS 1303
Cdd:PRK09039 54 ALDRLNSQIAELADLLSLERQGNQDLQDSVAnlraSLSAAEAERSRLqalLAELAGAGAAAEGRAGELAQELDSEKQVSA 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305632842 1304 QLSRGKQAFTQQIEELKRQLeeeikakNALAHALQSSRhdcdllreqyEEEQESKAELQRALSKANTEVAQ 1374
Cdd:PRK09039 134 RALAQVELLNQQIAALRRQL-------AALEAALDASE----------KRDRESQAKIADLGRRLNVALAQ 187
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1640-1840 |
6.05e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1640 AAEALRNYRNTQGILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERV-- 1717
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELge 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1718 QLLHTQNTSLINTK-------KKLETDISQMQGeMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNM 1790
Cdd:COG3883 91 RARALYRSGGSVSYldvllgsESFSDFLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAE---LEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 305632842 1791 EQTVKDLQLRLDEAEQLaLKGGKKQIQKLEARVRELEGEVESEQKRNAEA 1840
Cdd:COG3883 167 EAAKAELEAQQAEQEAL-LAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1255-1413 |
6.62e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1255 TLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKAK--NA 1332
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1333 LAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVN 1412
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
.
gi 305632842 1413 A 1413
Cdd:COG1579 174 P 174
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1661-1939 |
6.97e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1661 LDDALRTQEDLKEQLAMVER-----RANLLQAEIEELRATLEQTERSRKIAEQELLDASERVqllhtqntslintkkkle 1735
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEkdlheRLNGLESELAELDEEIERYEEQREQARETRDEADEVL------------------ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1736 TDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTVKDLQLRLDEAEQLALkggkkQ 1815
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRER---LEELEEERDDLLAEAGLDDADAEAVEA-----R 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1816 IQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNT 1895
Cdd:PRK02224 316 REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 305632842 1896 NLAKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKVISEE 1939
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR 439
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1174-1836 |
8.58e-05 |
|
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: 47.51 E-value: 8.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1174 EFQKMRRDLEEATLQHEATAATLRKKHaDSVAELGEQIDNlQRVKQKLEKEKSEMKMEIDDLASNVetvskakGNLEKMc 1253
Cdd:pfam10174 131 ELFLLRKTLEEMELRIETQKQTLGARD-ESIKKLLEMLQS-KGLPKKSGEEDWERTRRIAEAEMQL-------GHLEVL- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1254 rtLEDQVSELKSKEEEQQRlindltaqRGRLQTESGE---FSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKAK 1330
Cdd:pfam10174 201 --LDQKEKENIHLREELHR--------RNQLQPDPAKtkaLQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1331 NALAHALQSSRHDCDLLREQYEEeqeskaeLQRALSKANTEVAQWRTKYETDAIQRTEeleeakkklaqrlqaAEEHVEA 1410
Cdd:pfam10174 271 EEEIKQMEVYKSHSKFMKNKIDQ-------LKQELSKKESELLALQTKLETLTNQNSD---------------CKQHIEV 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1411 VNAKCASLEKTKQRLQNEVEDLMLDvertnaacaaLDKKQRNFDKilaewKQKYeethaeLEASQKEARSLGTELFKMKn 1490
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEVDALRLR----------LEEKESFLNK-----KTKQ------LQDLTEEKSTLAGEIRDLK- 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1491 ayeeslDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIqleln 1570
Cdd:pfam10174 387 ------DMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERL----- 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1571 qvKSEVDRKIAEKDEEIDQLKRNhIRIVESMQSTLDAEIRSRNDAIRlkkkmegDLNEmeiqlnHANRMAAEALRNYRNT 1650
Cdd:pfam10174 456 --KEQREREDRERLEELESLKKE-NKDLKEKVSALQPELTEKESSLI-------DLKE------HASSLASSGLKKDSKL 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1651 QGILKDTQLHLDDALRTQEDLK--EQLAMVERranlLQAEIEELRATLEQtERSRKIAEQelldaservqllhtqntsli 1728
Cdd:pfam10174 520 KSLEIAVEQKKEECSKLENQLKkaHNAEEAVR----TNPEINDRIRLLEQ-EVARYKEES-------------------- 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1729 ntkkkletdiSQMQGEME---DILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQ--TVKDLQLRLDE 1803
Cdd:pfam10174 575 ----------GKAQAEVErllGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKkkGAQLLEEARRR 644
|
650 660 670
....*....|....*....|....*....|...
gi 305632842 1804 AEQLALKGGKKQIQKLEARVRELEGEVESEQKR 1836
Cdd:pfam10174 645 EDNLADNSQQLQLEELMGALEKTRQELDATKAR 677
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1245-1888 |
9.22e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.49 E-value: 9.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1245 AKGNLEKmcrtLEDQVSELKSKEEEQQRLIND----LTAQRGRLQTESGEFSRQ---LDEKDALVSQLSRGKQAFTQQIE 1317
Cdd:PRK10246 196 ARTELEK----LQAQASGVALLTPEQVQSLTAslqvLTDEEKQLLTAQQQQQQSlnwLTRLDELQQEASRRQQALQQALA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1318 ELKrqleeeiKAKNALAhALQSSrHDCDLLREQYEEEQESKAEL---QRALSKANT---EVAQWRTKYETDAIQRTEELE 1391
Cdd:PRK10246 272 AEE-------KAQPQLA-ALSLA-QPARQLRPHWERIQEQSAALahtRQQIEEVNTrlqSTMALRARIRHHAAKQSAELQ 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1392 EAKKKLAQRLQAAE------EHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNA------------ACAALDK--KQR 1451
Cdd:PRK10246 343 AQQQSLNTWLAEHDrfrqwnNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNAlpaitltltadeVAAALAQhaEQR 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1452 NFDKILAEWKQKYEETHAELEASQKEARSLGTELFKmknayeesLDQLETLKREN-KNLQQEISDLtEQIAEGGKRIHEL 1530
Cdd:PRK10246 423 PLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQ--------RNAALNEMRQRyKEKTQQLADV-KTICEQEARIKDL 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1531 EKIKKQVEQEK-CEL-----------------------QAALEEAEASLEhEEGKILRIQLE-----LNQVKSEVdRKIA 1581
Cdd:PRK10246 494 EAQRAQLQAGQpCPLcgstshpaveayqalepgvnqsrLDALEKEVKKLG-EEGAALRGQLDaltkqLQRDESEA-QSLR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1582 EKDEEIDQLKRN-------HIRIVESMQSTLDAEIRSRNDAIRLKKKMEgdlneMEIQLNHANRMAAEALRNYRNTQGIL 1654
Cdd:PRK10246 572 QEEQALTQQWQAvcaslniTLQPQDDIQPWLDAQEEHERQLRLLSQRHE-----LQGQIAAHNQQIIQYQQQIEQRQQQL 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1655 KDTQLHLddALRTQEDLKEQLAMVER------------RANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHT 1722
Cdd:PRK10246 647 LTALAGY--ALTLPQEDEEASWLATRqqeaqswqqrqnELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHE 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1723 QNTSLINTKKKLETDISQMQGEMEDILQE---ARNAEEKAKKAITDAAMMAEElkkeqdTSAHLERMKKNMEQtvkdlql 1799
Cdd:PRK10246 725 QCLSLHSQLQTLQQQDVLEAQRLQKAQAQfdtALQASVFDDQQAFLAALLDEE------TLTQLEQLKQNLEN------- 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1800 RLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNAEAV--KGLRKHERRVKELTYQTEEDRKNILRLQDLVdklqA 1877
Cdd:PRK10246 792 QRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQlaQQLRENTTRQGEIRQQLKQDADNRQQQQALM----Q 867
|
730
....*....|.
gi 305632842 1878 KVKSYKRQAEE 1888
Cdd:PRK10246 868 QIAQATQQVED 878
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
848-1006 |
9.54e-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: 47.07 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 848 ETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLL----KEKNDLQLQVQAEAEGLADA--------------EERC 909
Cdd:COG4942 73 ALEQELAALEAELAELEKEIAELRAELEAQKEELAELLralyRLGRQPPLALLLSPEDFLDAvrrlqylkylaparREQA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 910 DQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEdecselkKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL 989
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALE-------ALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
170
....*....|....*..
gi 305632842 990 DETIAKLTKEKKALQEA 1006
Cdd:COG4942 226 EALIARLEAEAAAAAER 242
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1669-1914 |
9.54e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.20 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1669 EDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQllhTQNTSLINTKKKLETDISQMQGEMEDI 1748
Cdd:pfam07888 16 EEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYK---RDREQWERQRRELESRVAELKEELRQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1749 LQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEqLALKGGKKQIQKLEARVRELEG 1828
Cdd:pfam07888 93 REKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE-TELERMKERAKKAGAQRKEEEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1829 EVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQsntnLAKFRKLQHELE 1908
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL----LEELRSLQERLN 247
|
....*.
gi 305632842 1909 EAEERA 1914
Cdd:pfam07888 248 ASERKV 253
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1491-1708 |
1.01e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 47.38 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1491 AYEESLDQLETLKRENKNLQQEISDLTEQIAEGGK---RIHELEKIKKQVEQ----EKceLQAALEEAEASLEHEEGKIL 1563
Cdd:COG0497 166 AWRALKKELEELRADEAERARELDLLRFQLEELEAaalQPGEEEELEEERRRlsnaEK--LREALQEALEALSGGEGGAL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1564 RIqleLNQVKSEVDRkIAEKDEEIDQLkrnhIRIVESMQSTLD---AEIRSRNDAIrlkkkmEGD---LNEMEIQLNHAN 1637
Cdd:COG0497 244 DL---LGQALRALER-LAEYDPSLAEL----AERLESALIELEeaaSELRRYLDSL------EFDperLEEVEERLALLR 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305632842 1638 RMAaealRNYRNTqgilkdtqlhLDDALRTQEDLKEQLAMVERRANL---LQAEIEELRATLEQ-----TERSRKIAEQ 1708
Cdd:COG0497 310 RLA----RKYGVT----------VEELLAYAEELRAELAELENSDERleeLEAELAEAEAELLEaaeklSAARKKAAKK 374
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
856-1103 |
1.04e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 47.54 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 856 MKEEFQKTKDELAKSEAKRKELEEkmvtlLKEKNDLqLQVQAEAEGLADAEERCDQLiktKIQLEAKIKEVTERAEDEEE 935
Cdd:PLN03229 509 LMEKIEKLKDEFNKRLSRAPNYLS-----LKYKLDM-LNEFSRAKALSEKKSKAEKL---KAEINKKFKEVMDRPEIKEK 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 936 INAeltakkRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMaGLDETIAKltkeKKALQEAHQQTLDDLQ 1015
Cdd:PLN03229 580 MEA------LKAEVASSGASSGDELDDDLKEKVEKMKKEIELELAGVLKSM-GLEVIGVT----KKNKDTAEQTPPPNLQ 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1016 AEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKklrmdLERAKRKLEGDLKLAQEsimdIENEKQQLDEKLKKKeFEISNLQ 1095
Cdd:PLN03229 649 EKIESLNEEINKKIERVIRSSDLKSKIELLK-----LEVAKASKTPDVTEKEK----IEALEQQIKQKIAEA-LNSSELK 718
|
....*...
gi 305632842 1096 SKIEDEQA 1103
Cdd:PLN03229 719 EKFEELEA 726
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1350-1554 |
1.25e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1350 QYEEEQESKAELQRALSKANTEVAQWRTKYEtdaiqrteELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEV 1429
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELE--------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1430 EDLMLDVERTNAA-------------------CAALDKKQRNFDKILAEwkqkYEETHAELEASQKEARSLGTELFKMKN 1490
Cdd:COG3883 89 GERARALYRSGGSvsyldvllgsesfsdfldrLSALSKIADADADLLEE----LKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305632842 1491 AYEESLDQLETLKRENknlQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEAS 1554
Cdd:COG3883 165 ELEAAKAELEAQQAEQ---EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
845-1102 |
1.27e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 845 KSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIK 924
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 925 EVTERAedeEEINAELTAKKRKLeDECSELKKDIDDLELTLAKVEKEKhatENKVKNLTEEMAgLDETIAKLTKEKKALQ 1004
Cdd:COG1340 82 ELNEKL---NELREELDELRKEL-AELNKAGGSIDKLRKEIERLEWRQ---QTEVLSPEEEKE-LVEKIKELEKELEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1005 EAHQQ------TLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQ 1078
Cdd:COG1340 154 KALEKneklkeLRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEII 233
|
250 260
....*....|....*....|....
gi 305632842 1079 QLDEKLKKKEFEISNLQSKIEDEQ 1102
Cdd:COG1340 234 ELQKELRELRKELKKLRKKQRALK 257
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
847-1154 |
1.31e-04 |
|
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: 46.81 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 847 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEV 926
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 927 TERAE-------DEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAkltkE 999
Cdd:pfam07888 156 KERAKkagaqrkEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEA----E 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1000 KKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKklrmdLERAkrklEGDLKLAQESIMDIENEKQQ 1079
Cdd:pfam07888 232 NEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQAR-----LQAA----QLTLQLADASLALREGRARW 302
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305632842 1080 LDEKlkkkefeiSNLQSKIEDE----QALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERL 1154
Cdd:pfam07888 303 AQER--------ETLQQSAEADkdriEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASL 373
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1316-1582 |
1.33e-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: 46.93 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1316 IEELKRQLEEEIKAKNaLAHALQSSRHDCDLLREQYEEEQESKAELqraLSKANTEVAQWRTKYETDAIQRTEELEEAKK 1395
Cdd:NF033838 71 LSEIQKSLDKRKHTQN-VALNKKLSDIKTEYLYELNVLKEKSEAEL---TSKTKKELDAAFEQFKKDTLEPGKKVAEATK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1396 KLAQRLQAAEEHVEA---------------------VNAKCASLEKTKQRLQNEvedlmLDVERTNAACAALDKKQRN-- 1452
Cdd:NF033838 147 KVEEAEKKAKDQKEEdrrnyptntyktleleiaesdVEVKKAELELVKEEAKEP-----RDEEKIKQAKAKVESKKAEat 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1453 -FDKILAEWKQKYEETHAELEASQKEARSLGTELFKM----KNAYEESLDQLETLKRENKNLQQEISDLTEQ-------- 1519
Cdd:NF033838 222 rLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQdkpkRRAKRGVLGEPATPDKKENDAKSSDSSVGEEtlpspslk 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1520 ----IAEGGKRIHELEK-IKKQVEQEK----------CELQAA-----LEEAEASLEHEEGKILRIQLELNQVKSEVDRK 1579
Cdd:NF033838 302 pekkVAEAEKKVEEAKKkAKDQKEEDRrnyptntyktLELEIAesdvkVKEAELELVKEEAKEPRNEEKIKQAKAKVESK 381
|
...
gi 305632842 1580 IAE 1582
Cdd:NF033838 382 KAE 384
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1311-1763 |
1.38e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1311 AFTQQIEELKRQLEEEIKAKNALAHAlqssrhdcdllREQYEEEQESKAELQRALskantevaqwrtkyetdaiqrtEEL 1390
Cdd:PRK04863 273 DYMRHANERRVHLEEALELRRELYTS-----------RRQLAAEQYRLVEMAREL----------------------AEL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1391 EEAKKKLAQRLQAAEEHVEAVNAKCASLEKTkQRLQNEVEDLMLDVERTNAACAALDKKQrnfdkilaewkqkyEETHAE 1470
Cdd:PRK04863 320 NEAESDLEQDYQAASDHLNLVQTALRQQEKI-ERYQADLEELEERLEEQNEVVEEADEQQ--------------EENEAR 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1471 LEASQKEARSLGTELFKmknaYEESLDQLETLKRENKNLQQ---------EISDLTEQIAEGgkRIHELEKIKKQVEQEK 1541
Cdd:PRK04863 385 AEAAEEEVDELKSQLAD----YQQALDVQQTRAIQYQQAVQalerakqlcGLPDLTADNAED--WLEEFQAKEQEATEEL 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1542 CELQAALEEAEASLE-HEEGKILriqleLNQVKSEVDRKIAEkdeeidqlkrnhirivESMQSTLDAEIRSRNDAIRLKK 1620
Cdd:PRK04863 459 LSLEQKLSVAQAAHSqFEQAYQL-----VRKIAGEVSRSEAW----------------DVARELLRRLREQRHLAEQLQQ 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1621 kMEGDLNEMEIQLNH---ANRMAAEALRNYRNTQGILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEELRAtle 1697
Cdd:PRK04863 518 -LRMRLSELEQRLRQqqrAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQA--- 593
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 305632842 1698 QTERSRKIAeQELLDASERVQLLHTQNTSLINTKKKLETDISQMQgEMEDILQEARNAEEKAKKAI 1763
Cdd:PRK04863 594 RIQRLAARA-PAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLL-ERERELTVERDELAARKQAL 657
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
880-1115 |
1.40e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.84 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 880 KMVTLLKEKNDL--QLQVqaeaEGLADAEERCDQLIKTKIQLEAKIKEVTERAED--EEEINAELTAKKRKLEDECSELK 955
Cdd:PRK05771 10 LIVTLKSYKDEVleALHE----LGVVHIEDLKEELSNERLRKLRSLLTKLSEALDklRSYLPKLNPLREEKKKVSVKSLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 956 KDIDDLELTLAKVEKEkhatenkVKNLTEEMAGLDETIAKLTKEKKALQ--EAHQQTLDDLQAEED---KVNTLTKAKTK 1030
Cdd:PRK05771 86 ELIKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYvsvFVGTVPEDKLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1031 LEQQVDDLEGSLE-QEKKLRM-----DLERAKRKLEGDLKLAQESIMDIENEKqQLDEKLKKKEFEISNLQSKIEDeqal 1104
Cdd:PRK05771 159 ELKLESDVENVEYiSTDKGYVyvvvvVLKELSDEVEEELKKLGFERLELEEEG-TPSELIREIKEELEEIEKERES---- 233
|
250
....*....|.
gi 305632842 1105 giqLQKKIKEL 1115
Cdd:PRK05771 234 ---LLEELKEL 241
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
865-1094 |
1.48e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 865 DELAKSeaKRKELEEKMVTLLKEKNDLQLQVQAE-----------AEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDE 933
Cdd:PHA02562 169 DKLNKD--KIRELNQQIQTLDMKIDHIQQQIKTYnknieeqrkknGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 934 EEINAELTAKKRKLEDECSELKKDIDdlelTLAKVEK--EKHATenkVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTL 1011
Cdd:PHA02562 247 VMDIEDPSAALNKLNTAAAKIKSKIE----QFQKVIKmyEKGGV---CPTCTQQISEGPDRITKIKDKLKELQHSLEKLD 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1012 DDLQAEEDKVNTLTKAKTKLEqqvdDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEI 1091
Cdd:PHA02562 320 TAIDELEEIMDEFNEQSKKLL----ELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTK 395
|
...
gi 305632842 1092 SNL 1094
Cdd:PHA02562 396 SEL 398
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
847-979 |
1.63e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 847 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTL---LKEKNDLQLQVQAEAEgLADAEERCDQLIKTKIQLEAKI 923
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVearIKKYEEQLGNVRNNKE-YEALQKEIESLKRRISDLEDEI 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 924 KEVTERAEDEE----EINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKV 979
Cdd:COG1579 113 LELMERIEELEeelaELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1256-1479 |
1.85e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1256 LEDQVSELKSKEEEQQRLINDLTAQRG--RLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNAL 1333
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1334 AHALQSSRhdcdlLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNA 1413
Cdd:COG3206 260 LQSPVIQQ-----LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQA 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 305632842 1414 KcasLEKTKQRLQ--NEVEDLMLDVERTnaacaaLDKKQRNFDKILaewkQKYEETHAELEASQKEAR 1479
Cdd:COG3206 335 Q---LAQLEARLAelPELEAELRRLERE------VEVARELYESLL----QRLEEARLAEALTVGNVR 389
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1296-1559 |
1.88e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.46 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1296 DEKDALVSQLsRGKQAFtqQIEELKRQLEEEiKAKNALAHALQSSRHdCDLLREQYEEEQESKAELQRalskantevaqw 1375
Cdd:PRK05771 16 SYKDEVLEAL-HELGVV--HIEDLKEELSNE-RLRKLRSLLTKLSEA-LDKLRSYLPKLNPLREEKKK------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1376 rtkyetdaiQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLM----LDVErtnaacaalDKKQR 1451
Cdd:PRK05771 79 ---------VSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnFDLD---------LSLLL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1452 NFD--KILAEWKQKYEETHAELEASQKEARSLGTE-------LFKMKNAYEESLDQLETLKRENKNL------QQEISDL 1516
Cdd:PRK05771 141 GFKyvSVFVGTVPEDKLEELKLESDVENVEYISTDkgyvyvvVVVLKELSDEVEEELKKLGFERLELeeegtpSELIREI 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 305632842 1517 TEQIAEGGKRIHEL-EKIKKQVEQEKCELQAALEEAEASLEHEE 1559
Cdd:PRK05771 221 KEELEEIEKERESLlEELKELAKKYLEELLALYEYLEIELERAE 264
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
839-1060 |
2.04e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 839 KIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQ 918
Cdd:PRK02224 497 RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 919 LEAKIKEVTERAEDEEEInAELTAKKRKLEDECSELKKDIDDleltLAKVEKEKhatENKVKNLTEEMAGLDETIAKLTK 998
Cdd:PRK02224 577 LNSKLAELKERIESLERI-RTLLAAIADAEDEIERLREKREA----LAELNDER---RERLAEKRERKRELEAEFDEARI 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 305632842 999 EKkaLQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLE 1060
Cdd:PRK02224 649 EE--AREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVE 708
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1669-1935 |
2.11e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1669 EDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKiaeqELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDI 1748
Cdd:PRK03918 196 KEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1749 LQEARNAEEKAKKAitdaammaEELKKEQDTSAHLERMKKNMEQtvkdlqlrldeaeqlalkgGKKQIQKLEARVRELEG 1828
Cdd:PRK03918 272 KKEIEELEEKVKEL--------KELKEKAEEYIKLSEFYEEYLD-------------------ELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1829 EVEseqkrnaEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQaKVKSYKRQAEEAEEQSNTNlaKFRKLQHELE 1908
Cdd:PRK03918 325 GIE-------ERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGL--TPEKLEKELE 394
|
250 260
....*....|....*....|....*..
gi 305632842 1909 EAEERADIAESQVNKLRVKSREVHTKV 1935
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEI 421
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
933-1325 |
2.28e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.44 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 933 EEEINAEL-TAKKRKL-EDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQT 1010
Cdd:PRK11281 38 EADVQAQLdALNKQKLlEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1011 LDDLQAEEdkvntltkaktkLEQQVDDLEGSLEQEKK-----------LRMDLERAKRKLEGDLKLAQEsimdIENekqQ 1079
Cdd:PRK11281 118 LSTLSLRQ------------LESRLAQTLDQLQNAQNdlaeynsqlvsLQTQPERAQAALYANSQRLQQ----IRN---L 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1080 LDEKLKKKEFEISNLQSKIEDEQA-LGIQLQKKIKELQARIEELEEeieaerasrakAEKQRSdlsrELEEISERLEEAg 1158
Cdd:PRK11281 179 LKGGKVGGKALRPSQRVLLQAEQAlLNAQNDLQRKSLEGNTQLQDL-----------LQKQRD----YLTARIQRLEHQ- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1159 gATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQI------------DNLqRVKQKLEkeks 1226
Cdd:PRK11281 243 -LQLLQEAINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLlkateklntltqQNL-RVKNWLD---- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1227 emkmeiddlasnvetvskakgNLEKMCRTLEDQVSELK-----SKEEEQQR-------LINDLTAQRGRLQTESGEFSRQ 1294
Cdd:PRK11281 317 ---------------------RLTQSERNIKEQISVLKgslllSRILYQQQqalpsadLIEGLADRIADLRLEQFEINQQ 375
|
410 420 430
....*....|....*....|....*....|....*
gi 305632842 1295 LDE---KDALVSQLSRG-KQAFTqqiEELKRQLEE 1325
Cdd:PRK11281 376 RDAlfqPDAYIDKLEAGhKSEVT---DEVRDALLQ 407
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
893-1017 |
2.40e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 893 LQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEI---NAELTAKKRKLEDECSELKKDIDDLELTLAKVE 969
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELrerRNELQKLEKRLLQKEENLDRKLELLEKREEELE 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 305632842 970 KEKHATENKVKNLTEEMAGLD----------ETIAKLTKEkkalqEAHQQTLDDLQAE 1017
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEelieeqlqelERISGLTAE-----EAKEILLEKVEEE 166
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1262-1848 |
2.45e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.22 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1262 ELKSKEEEQQRLINDLTAQRGRLQTESGEFSRqldEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSsr 1341
Cdd:COG5022 811 EYRSYLACIIKLQKTIKREKKLRETEEVEFSL---KAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQ-- 885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1342 hdcdllreQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAvnakcaSLEKT 1421
Cdd:COG5022 886 --------ELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGP------SIEYV 951
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1422 KQRLQNEVedlmldvertNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLgTELFKMKNAYEESLDQLET 1501
Cdd:COG5022 952 KLPELNKL----------HEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKEL-AELSKQYGALQESTKQLKE 1020
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1502 LKRENKNLQQEISDLTEQIAEGgKRIHELEKIKKQVEQEKCELQAALEEAeaSLEHEEGKILRIQLELNQVKSEVDRKIA 1581
Cdd:COG5022 1021 LPVEVAELQSASKIISSESTEL-SILKPLQKLKGLLLLENNQLQARYKAL--KLRRENSLLDDKQLYQLESTENLLKTIN 1097
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1582 EKDEEIdqLKRNHIRIVESMQSTLDAEIRSRndairLKKKMEGDLN------EMEIQLNHANRMAAEALRNYRNTQGILk 1655
Cdd:COG5022 1098 VKDLEV--TNRNLVKPANVLQFIVAQMIKLN-----LLQEISKFLSqlvntlEPVFQKLSVLQLELDGLFWEANLEALP- 1169
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1656 dtqlHLDDALRTQEDLKEQLAMVERRANLLQAEIEELRA---TLEQTERSRKIAEQELLDASERVQLLHTQNTSL----- 1727
Cdd:COG5022 1170 ----SPPPFAALSEKRLYQSALYDEKSKLSSSEVNDLKNeliALFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLkgfnn 1245
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1728 -----INTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITD-----------------AAMMAEELKKEQDTSAHLER 1785
Cdd:COG5022 1246 lnkkfDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSllqyinvglfnalrtkaSSLRWKSATEVNYNSEELDD 1325
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1786 MKKNME------------QTVKDLQLRLDEAEQLALKGGKK------QIQKLEARVRELEGEVESEQKRNAEAVKGLRKH 1847
Cdd:COG5022 1326 WCREFEisdvdeeleeliQAVKVLQLLKDDLNKLDELLDACyslnpaEIQNLKSRYDPADKENNLPKEILKKIEALLIKQ 1405
|
.
gi 305632842 1848 E 1848
Cdd:COG5022 1406 E 1406
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
857-1080 |
2.62e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.30 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 857 KEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEG--------LADAEERCDQLIKTKIQLEAKIKEVTE 928
Cdd:pfam00038 3 KEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRlyslyekeIEDLRRQLDTLTVERARLQLELDNLRL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 929 RAEDEEEINAELTAKKRKLEDECSELKKDIDdlELTLAKVEkekhaTENKVKNLTEEMAGL----DETIAKLT------- 997
Cdd:pfam00038 83 AAEDFRQKYEDELNLRTSAENDLVGLRKDLD--EATLARVD-----LEAKIESLKEELAFLkknhEEEVRELQaqvsdtq 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 998 -----------------------------KEKKALQEAHQQTLDDLQAEEDKVN-TLTKAKTKLEQ---QVDDLEGSLEQ 1044
Cdd:pfam00038 156 vnvemdaarkldltsalaeiraqyeeiaaKNREEAEEWYQSKLEELQQAAARNGdALRSAKEEITElrrTIQSLEIELQS 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 305632842 1045 EKKLRMDLERAKRKLE----GDLKLAQESIMDIENEKQQL 1080
Cdd:pfam00038 236 LKKQKASLERQLAETEeryeLQLADYQELISELEAELQET 275
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1388-1923 |
2.86e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 45.79 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1388 EELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKqrlqNEVEDLMLDVERtnaacAALDKKQRNFDKILAEWKQKYEET 1467
Cdd:pfam05701 42 LELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTK----RLIEELKLNLER-----AQTEEAQAKQDSELAKLRVEEMEQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1468 HAELEASQkearSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKR----IHELEKIKKQVEQEKCE 1543
Cdd:pfam05701 113 GIADEASV----AAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRaeeaVSASKEIEKTVEELTIE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1544 LQAALEEAE----ASLEHEEGKIlRIQLELNQVKSEVDRKIAEKDEEIDQLkRNHIRIVESMQSTLDAeirsrndAIRLK 1619
Cdd:pfam05701 189 LIATKESLEsahaAHLEAEEHRI-GAALAREQDKLNWEKELKQAEEELQRL-NQQLLSAKDLKSKLET-------ASALL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1620 KKMEGDLNE-MEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEELR---AT 1695
Cdd:pfam05701 260 LDLKAELAAyMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAASLRSELEKEKaelAS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1696 LEQTERSRKIAEQELLDASERVQllhtqntSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAitdaAMMA-EELK 1774
Cdd:pfam05701 340 LRQREGMASIAVSSLEAELNRTK-------SEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSL----AQAArEELR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1775 KEQD-----------TSAHLERMKKNMEQTvkdlqlrlDEAEQLALkggkkqiqkleARVRELEgevESEQKRNAEAVKG 1843
Cdd:pfam05701 409 KAKEeaeqakaaastVESRLEAVLKEIEAA--------KASEKLAL-----------AAIKALQ---ESESSAESTNQED 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1844 lrkherRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNK 1923
Cdd:pfam05701 467 ------SPRGVTLSLEEYYELSKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNREMEERKEALKIALEKAEK 540
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1570-1767 |
2.89e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 45.98 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1570 NQVKSEVDRKI--AEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAI---------RLKKKMEGdLNEMEIQLNHAnr 1638
Cdd:NF012221 1563 DKERAEADRQRleQEKQQQLAAISGSQSQLESTDQNALETNGQAQRDAIleesravtkELTTLAQG-LDALDSQATYA-- 1639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1639 maAEALRNYRN--TQGILKDTQLHLDDALRTqedLKEQLAMVERR--ANLLQAE--IEELRATLEQTERSRKIAEQELLD 1712
Cdd:NF012221 1640 --GESGDQWRNpfAGGLLDRVQEQLDDAKKI---SGKQLADAKQRhvDNQQKVKdaVAKSEAGVAQGEQNQANAEQDIDD 1714
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305632842 1713 ASERVQLLHTQNTSLINTKKKLETDIS------QMQGEmedilQEARNAEEKAKKAITDAA 1767
Cdd:NF012221 1715 AKADAEKRKDDALAKQNEAQQAESDANaaandaQSRGE-----QDASAAENKANQAQADAK 1770
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1108-1863 |
2.93e-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: 45.97 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1108 LQKKIKELQARIEE-LEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKM-------- 1178
Cdd:pfam10174 1 LQAQLRDLQRENELlRRELDIKESKLGSSMNSIKTFWSPELKKERALRKEEAARISVLKEQYRVTQEENQHLqltiqalq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1179 -----RRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKG----NL 1249
Cdd:pfam10174 81 delraQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGardeSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1250 EKMCRTLEDQVSELKSKEEEQQRlindlTAQRGRLQTESGEFSRQLDEKD----ALVSQLSRGKQAftQQIEELKRQLEE 1325
Cdd:pfam10174 161 KKLLEMLQSKGLPKKSGEEDWER-----TRRIAEAEMQLGHLEVLLDQKEkeniHLREELHRRNQL--QPDPAKTKALQT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1326 EIKAKNA-----------LAHALQSSRHDCDLLREQYEEE--------QESK------AELQRALSKANTEVAQWRTKYE 1380
Cdd:pfam10174 234 VIEMKDTkisslernirdLEDEVQMLKTNGLLHTEDREEEikqmevykSHSKfmknkiDQLKQELSKKESELLALQTKLE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1381 TDAIQRTEeleeakkklaqrlqaAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDvertnaacaaLDKKQRNFDKilaew 1460
Cdd:pfam10174 314 TLTNQNSD---------------CKQHIEVLKESLTAKEQRAAILQTEVDALRLR----------LEEKESFLNK----- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1461 KQKYeethaeLEASQKEARSLGTELFKMKnayeeslDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQE 1540
Cdd:pfam10174 364 KTKQ------LQDLTEEKSTLAGEIRDLK-------DMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTD 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1541 KCELQAALEEAEASLEHEEGKILRIqlelnqvKSEVDRKIAEKDEEIDQLKRN-----------HIRIVESMQSTLDAEI 1609
Cdd:pfam10174 431 SSNTDTALTTLEEALSEKERIIERL-------KEQREREDRERLEELESLKKEnkdlkekvsalQPELTEKESSLIDLKE 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1610 RSRNDAIRLKKKmEGDLNEMEIQLNHANRMAAEalrnyrnTQGILKDTQlHLDDALRTQEDLKEQLAMVERR-------A 1682
Cdd:pfam10174 504 HASSLASSGLKK-DSKLKSLEIAVEQKKEECSK-------LENQLKKAH-NAEEAVRTNPEINDRIRLLEQEvarykeeS 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1683 NLLQAEIEELRATLEQTE-----RSRKIAEQElldaSERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEE 1757
Cdd:pfam10174 575 GKAQAEVERLLGILREVEnekndKDKKIAELE----SLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLAD 650
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1758 KAKKAITDAAMMA-EELKKEQD-TSAHLERMKKNMEQTVKDL-QLRLDEAEQLALKGGKKQiQKLEARVRELEGEV---- 1830
Cdd:pfam10174 651 NSQQLQLEELMGAlEKTRQELDaTKARLSSTQQSLAEKDGHLtNLRAERRKQLEEILEMKQ-EALLAAISEKDANIalle 729
|
810 820 830
....*....|....*....|....*....|....*.
gi 305632842 1831 --ESEQKRNAEAVKGL-RKHERRVKELTYQTEEDRK 1863
Cdd:pfam10174 730 lsSSKKKKTQEEVMALkREKDRLVHQLKQQTQNRMK 765
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1315-1555 |
3.01e-04 |
|
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: 44.71 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1315 QIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQEskaELQRALSKANTEVAQwrtkyETDAIQRTEELEEAK 1394
Cdd:pfam06008 20 NLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQK---KATQTLAKAQQVNAE-----SERTLGHAKELAEAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1395 KKLAQRLQAAEEHVEAVNAKCASL-EKTKQRLQNEVEDLMLDVERTNaacaaLDKKQRNFDKILAEWKQKYEETHAELEA 1473
Cdd:pfam06008 92 KNLIDNIKEINEKVATLGENDFALpSSDLSRMLAEAQRMLGEIRSRD-----FGTQLQNAEAELKAAQDLLSRIQTWFQS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1474 SQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTeqiAEGGKRIHELEKIKKQVEQEKCELQAALEEAEA 1553
Cdd:pfam06008 167 PQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLN---LANQANLREFQRKKEEVSEQKNQLEETLKTARD 243
|
..
gi 305632842 1554 SL 1555
Cdd:pfam06008 244 SL 245
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1502-1907 |
3.06e-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: 46.12 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1502 LKRENKNLQQEISDLTE-----QIAEGGKRIHELEKIKKQVEQEKCEL--------QAALEEAEASLEHEEGKILRIQLE 1568
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPldqytQLALMEFAKKKSLHGKAELLTLRSQLltlctpcmPDTYHERKQVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1569 LNQVKSEVDRKIaEKDEEIDQLKRNHIRIVESMQS--TLDAEIRSRNDAIRLKKKMEGDLNEMEiQLNHANRMAAEALRN 1646
Cdd:TIGR00618 238 TQQSHAYLTQKR-EAQEEQLKKQQLLKQLRARIEElrAQEAVLEETQERINRARKAAPLAAHIK-AVTQIEQQAQRIHTE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1647 YRNTQGILKDTQLHLDDALRTQEDLKEQlamvERRANLLQAEIEELRATLEQTERSRKIAEQELLDaSERVQLLHTQNTS 1726
Cdd:TIGR00618 316 LQSKMRSRAKLLMKRAAHVKQQSSIEEQ----RRLLQTLHSQEIHIRDAHEVATSIREISCQQHTL-TQHIHTLQQQKTT 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1727 LINTKKKLETDISQMQGEMEDilQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVK-----DLQLRL 1801
Cdd:TIGR00618 391 LTQKLQSLCKELDILQREQAT--IDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEkihlqESAQSL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1802 DEAEQLalKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKS 1881
Cdd:TIGR00618 469 KEREQQ--LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEED 546
|
410 420
....*....|....*....|....*.
gi 305632842 1882 YKRQAEEAEEQSNTNLAKFRKLQHEL 1907
Cdd:TIGR00618 547 VYHQLTSERKQRASLKEQMQEIQQSF 572
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
847-1010 |
3.20e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 847 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKE-----KNDLQLQVQAEAEGLADAEERCDQLikTKI---- 917
Cdd:COG3883 54 NELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAlyrsgGSVSYLDVLLGSESFSDFLDRLSAL--SKIadad 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 918 -----QLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDET 992
Cdd:COG3883 132 adlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
170
....*....|....*...
gi 305632842 993 IAKLTKEKKALQEAHQQT 1010
Cdd:COG3883 212 AAAAAAAAAAAAAAAAAA 229
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1078-1240 |
3.47e-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: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1078 QQLDEKLKKKEFEISNLQSKIEDeqalgiqLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEA 1157
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1158 GG-----ATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEI 1232
Cdd:COG1579 86 RNnkeyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....*...
gi 305632842 1233 DDLASNVE 1240
Cdd:COG1579 166 EELAAKIP 173
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1494-1743 |
3.74e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1494 ESLDQLETLKRENKNLQQEISDLTEQIAEGGKrihELEKIKKQVEQEKCE---------LQAALEEAEASLEheegkilR 1564
Cdd:PRK11281 70 ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQA---ELEALKDDNDEETREtlstlslrqLESRLAQTLDQLQ-------N 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1565 IQLELNQVKSEVdrkIAEKdeeiDQLKRNHIRIVESMQSTLdaEIRSRNDAIRLKKKmegDLNEMEIQLNHANRMAAEAL 1644
Cdd:PRK11281 140 AQNDLAEYNSQL---VSLQ----TQPERAQAALYANSQRLQ--QIRNLLKGGKVGGK---ALRPSQRVLLQAEQALLNAQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1645 RNYR------NTQgilkdtqlhLDDALRTQEDLK-EQLAMVERRANLLQAEIEELR-----ATLEQTERSRKIAE----- 1707
Cdd:PRK11281 208 NDLQrkslegNTQ---------LQDLLQKQRDYLtARIQRLEHQLQLLQEAINSKRltlseKTVQEAQSQDEAARiqanp 278
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 305632842 1708 -------------QELLDASERVQLLHTQN-------TSLINTKKKLETDISQMQG 1743
Cdd:PRK11281 279 lvaqeleinlqlsQRLLKATEKLNTLTQQNlrvknwlDRLTQSERNIKEQISVLKG 334
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
964-1194 |
3.77e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 964 TLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDdlegslE 1043
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE------E 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1044 QEKKLRMDLERAKRKLEGDLKLAQ--------------ESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQAlgiQLQ 1109
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLA---ELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1110 KKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQH 1189
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
....*
gi 305632842 1190 EATAA 1194
Cdd:COG3883 241 AAAAS 245
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
952-1211 |
4.29e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 952 SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKL 1031
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1032 EQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKK 1111
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1112 IKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEA 1191
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260
....*....|....*....|
gi 305632842 1192 TAATLRKKHADSVAELGEQI 1211
Cdd:COG4372 267 ILVEKDTEEEELEIAALELE 286
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1659-1833 |
4.35e-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: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1659 LHLDDALRTQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKkkletDI 1738
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-----EY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1739 SQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQdtsAHLERMKKNMEQTVKDLQLRLDEAEqlalkggkKQIQK 1818
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELE---AELAELEAELEEKKAELDEELAELE--------AELEE 160
|
170
....*....|....*
gi 305632842 1819 LEARVRELEGEVESE 1833
Cdd:COG1579 161 LEAEREELAAKIPPE 175
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
847-1034 |
4.40e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 847 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAeglADAEERCDQLIKTKIQLEAK-IKE 925
Cdd:COG3883 40 DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA---RALYRSGGSVSYLDVLLGSEsFSD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 926 VTERA-------EDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTK 998
Cdd:COG3883 117 FLDRLsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA 196
|
170 180 190
....*....|....*....|....*....|....*.
gi 305632842 999 EKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQ 1034
Cdd:COG3883 197 QLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1654-1896 |
4.68e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1654 LKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLhtqntslintKKK 1733
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER----------REE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1734 LETDISQMQ-----GEMEDILQEARNAEEkakkAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLA 1808
Cdd:COG3883 88 LGERARALYrsggsVSYLDVLLGSESFSD----FLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1809 lkggkkqiQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEE 1888
Cdd:COG3883 164 --------AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
....*...
gi 305632842 1889 AEEQSNTN 1896
Cdd:COG3883 236 AAAAAAAA 243
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1731-1918 |
4.72e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1731 KKKLETDISQMQGEMEDILQEARN-AEEKAKKAITDAAMMAEELKKEQDtsahlermkknmeqtvKDLQLRldeaeqlal 1809
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKeAEAIKKEALLEAKEEIHKLRNEFE----------------KELRER--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1810 kggKKQIQKLEARVRELEGEVESEQKRnaeavkgLRKHERRVkeltyqtEEDRKNILRLQDLVDKLQAKVKS-YKRQAEE 1888
Cdd:PRK12704 81 ---RNELQKLEKRLLQKEENLDRKLEL-------LEKREEEL-------EKKEKELEQKQQELEKKEEELEElIEEQLQE 143
|
170 180 190
....*....|....*....|....*....|
gi 305632842 1889 AEEQSNTNLAKFRKLQHELEEAEERADIAE 1918
Cdd:PRK12704 144 LERISGLTAEEAKEILLEKVEEEARHEAAV 173
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1783-1908 |
4.73e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.57 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1783 LERMKK-NMEQTVKDLQLRLDEAEQL------ALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVkglrkheRRVKELT 1855
Cdd:PRK09039 71 LERQGNqDLQDSVANLRASLSAAEAErsrlqaLLAELAGAGAAAEGRAGELAQELDSEKQVSARAL-------AQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 305632842 1856 YQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAkfRKLQhELE 1908
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALA--QRVQ-ELN 193
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1757-1929 |
4.98e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1757 EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLalkggkKQIQKLEARVRELEGEVESEQKR 1836
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL------LQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1837 naeaVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQA-EEAEEQSNTNLAKFRKLQHELEEAEERAD 1915
Cdd:COG4717 148 ----LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....
gi 305632842 1916 IAESQVNKLRVKSR 1929
Cdd:COG4717 224 ELEEELEQLENELE 237
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1489-1939 |
5.14e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.90 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1489 KNAYEESLDQLETLKRENKNLQQEISDLTEQIAEggkRIHELEKIKKQVEQEKcelqaaLEEAEASLEHEEGKILRIQLE 1568
Cdd:COG5278 85 RAEIDELLAELRSLTADNPEQQARLDELEALIDQ---WLAELEQVIALRRAGG------LEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1569 LNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYR 1648
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1649 NTQGILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLI 1728
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1729 NTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLA 1808
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1809 LKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEE 1888
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 305632842 1889 AEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKVISEE 1939
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1470-1925 |
5.22e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.12 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1470 ELEASQKEARSLGTELFKMKNAYEESLDQLEtlkRENKNLQQEISDLTEQIAEggkrihELEKIKKQVEQEKCELQAALE 1549
Cdd:pfam05557 62 KREAEAEEALREQAELNRLKKKYLEALNKKL---NEKESQLADAREVISCLKN------ELSELRRQIQRAELELQSTNS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1550 EAEASLEHEEGKILRIQlELNQVKSEVDRKIAEKDEEIDQLKrnhirivesmqsTLDAEIRSRNDAIRLKKKMEGDL--- 1626
Cdd:pfam05557 133 ELEELQERLDLLKAKAS-EAEQLRQNLEKQQSSLAEAEQRIK------------ELEFEIQSQEQDSEIVKNSKSELari 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1627 NEMEIQLNHAnRMAAEALRNYRNTQGILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIA 1706
Cdd:pfam05557 200 PELEKELERL-REHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1707 EqellDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKakkaITDAAMMAEELK------------ 1774
Cdd:pfam05557 279 E----DLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKK----IEDLNKKLKRHKalvrrlqrrvll 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1775 --KEQD-TSAHLERMKK--NMEQTVKDLQLRLDEAEQLALKGgKKQIQKLEARVRELEGEVESEQKRNA--EAVKGLRKH 1847
Cdd:pfam05557 351 ltKERDgYRAILESYDKelTMSNYSPQLLERIEEAEDMTQKM-QAHNEEMEAQLSVAEEELGGYKQQAQtlERELQALRQ 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1848 ERRVKELTYQTEED---RKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKL 1924
Cdd:pfam05557 430 QESLADPSYSKEEVdslRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKL 509
|
.
gi 305632842 1925 R 1925
Cdd:pfam05557 510 Q 510
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1453-1625 |
6.26e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1453 FDKILAEWKQKYEETHAE--LEASQKEARSLGTElfKMKNAYEESLDQLETLKRENKnlqqeisdlteqiaeggKRIHEL 1530
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKriLEEAKKEAEAIKKE--ALLEAKEEIHKLRNEFEKELR-----------------ERRNEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1531 EKIKKQVEQEKCEL---QAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKD---EEIDQLKRNHIR--IVESMQ 1602
Cdd:PRK12704 85 QKLEKRLLQKEENLdrkLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLqelERISGLTAEEAKeiLLEKVE 164
|
170 180
....*....|....*....|...
gi 305632842 1603 STLDAEIRSRNDAIRLKKKMEGD 1625
Cdd:PRK12704 165 EEARHEAAVLIKEIEEEAKEEAD 187
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1666-1930 |
6.63e-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: 44.73 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1666 RTQEDLKEQLAMVERRANL------LQAEIEELRATLEQTERSRKIAEQELldasERVQLLHTQNTSLINTKKKLETDIS 1739
Cdd:pfam17380 300 RLRQEKEEKAREVERRRKLeeaekaRQAEMDRQAAIYAEQERMAMEREREL----ERIRQEERKRELERIRQEEIAMEIS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1740 QMQgEMEDILQEARNAEEKAKKAItDAAMMAEELKKEqdtsahleRMKKNMEQTVKDLQLRLDEAEqlalkGGKKQIQKL 1819
Cdd:pfam17380 376 RMR-ELERLQMERQQKNERVRQEL-EAARKVKILEEE--------RQRKIQQQKVEMEQIRAEQEE-----ARQREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1820 EA-RVRELEGEVESEQKRNAEaVKGLRKHE--RRVKELTYQ--------TEEDRKNILRlQDLVDKLQAKVKSYK----- 1883
Cdd:pfam17380 441 EEeRAREMERVRLEEQERQQQ-VERLRQQEeeRKRKKLELEkekrdrkrAEEQRRKILE-KELEERKQAMIEEERkrkll 518
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 305632842 1884 ------RQAEEAEEQSNTNLAKFRKLQHELEE---AEERADIAESQVNKLRVKSRE 1930
Cdd:pfam17380 519 ekemeeRQKAIYEEERRREAEEERRKQQEMEErrrIQEQMRKATEERSRLEAMERE 574
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
978-1233 |
7.24e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 978 KVKNLTEEMAGLDETIaKLTKEKKALQEAHQQTLDDLQAE-----EDKVNTLTKAKTKLEQQVDDLEgslEQEKKLRMDL 1052
Cdd:PHA02562 175 KIRELNQQIQTLDMKI-DHIQQQIKTYNKNIEEQRKKNGEniarkQNKYDELVEEAKTIKAEIEELT---DELLNLVMDI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1053 ErakrKLEGDLKLAQESIMDIENEKQQL--DEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQarieeleeeieaer 1130
Cdd:PHA02562 251 E----DPSAALNKLNTAAAKIKSKIEQFqkVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQ-------------- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1131 asrakaeKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEAtLQHEATAATLRKKHADSVAELGEQ 1210
Cdd:PHA02562 313 -------HSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKA-KKVKAAIEELQAEFVDNAEELAKL 384
|
250 260
....*....|....*....|...
gi 305632842 1211 IDNLQrvkqKLEKEKSEMKMEID 1233
Cdd:PHA02562 385 QDELD----KIVKTKSELVKEKY 403
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
985-1156 |
7.35e-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: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 985 EMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAK--RKLEGD 1062
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEALQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1063 LKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQAlgiQLQKKIKELQARieeleeeieaerasRAKAEKQRSD 1142
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA---ELEEKKAELDEE--------------LAELEAELEE 160
|
170
....*....|....
gi 305632842 1143 LSRELEEISERLEE 1156
Cdd:COG1579 161 LEAEREELAAKIPP 174
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
865-1069 |
8.00e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 8.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 865 DELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKK 944
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 945 RKLEDECSELK-----KDIDDLeltLAKVEKEKHATENKvknlTEEMAGLDETIAKLTKEKKALQEAhQQTLDDLQAE-E 1018
Cdd:COG3883 96 YRSGGSVSYLDvllgsESFSDF---LDRLSALSKIADAD----ADLLEELKADKAELEAKKAELEAK-LAELEALKAElE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 305632842 1019 DKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQES 1069
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1454-1767 |
9.65e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.12 E-value: 9.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1454 DKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKI 1533
Cdd:PLN02939 113 NEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1534 KKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEvdrKIAEKDeEIDQLKRNHIRIVESMQSTLDAEirsrn 1613
Cdd:PLN02939 193 KIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEE---NMLLKD-DIQFLKAELIEVAETEERVFKLE----- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1614 daiRLKKKMEGDLNEMEIQLNHANrmaAEALRNYRNTQGILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEELR 1693
Cdd:PLN02939 264 ---KERSLLDASLRELESKFIVAQ---EDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1694 ATLEQTERSR------KIAEQELLDASERVQLLHTQntslINTKKKLETDISQmqgEMEDILQEARnaEEKAKKAITDAA 1767
Cdd:PLN02939 338 ASLKEANVSKfssykvELLQQKLKLLEERLQASDHE----IHSYIQLYQESIK---EFQDTLSKLK--EESKKRSLEHPA 408
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
875-1227 |
1.01e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 875 KELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSEL 954
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 955 KKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQ 1034
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1035 VDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKE 1114
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1115 LQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAA 1194
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350
....*....|....*....|....*....|...
gi 305632842 1195 TLRKKHADSVAELGEQIDNLQRVKQKLEKEKSE 1227
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1444-1833 |
1.05e-03 |
|
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: 43.73 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1444 AALDKKQRNFDKILAEWKQKYEETHAELEASQKEARS----LGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQ 1519
Cdd:pfam07888 44 AELLQAQEAANRQREKEKERYKRDREQWERQRRELESrvaeLKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1520 IAEGGKRIHELEKIKKQVEQEKCELQAALE-------EAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKdeeidQLKR 1592
Cdd:pfam07888 124 RAAHEARIRELEEDIKTLTQRVLERETELErmkerakKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF-----QELR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1593 NHIRIVESMQSTLDAEIrsrndairlkkkmegdlNEMEIQLNHANRMAAE---ALRNYRNTQGILKDTQlhlddalRTQE 1669
Cdd:pfam07888 199 NSLAQRDTQVLQLQDTI-----------------TTLTQKLTTAHRKEAEneaLLEELRSLQERLNASE-------RKVE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1670 DLKEQLA-MVERR----ANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLhtQNTSLinTKKKLETDISQMQgE 1744
Cdd:pfam07888 255 GLGEELSsMAAQRdrtqAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQ--QSAEA--DKDRIEKLSAELQ-R 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1745 MEDILQEARNAEEKAKKaitdaammaeELKKEQDTS-AHLERMKKNMEQTVKDLQLRLDEAEQLALkggkkQIQKLEARV 1823
Cdd:pfam07888 330 LEERLQEERMEREKLEV----------ELGREKDCNrVQLSESRRELQELKASLRVAQKEKEQLQA-----EKQELLEYI 394
|
410
....*....|
gi 305632842 1824 RELEGEVESE 1833
Cdd:pfam07888 395 RQLEQRLETV 404
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1671-1939 |
1.11e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1671 LKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKklETDISQMQGEMEDILQ 1750
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQ--ERMAMERERELERIRQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1751 EARNAEEKAKKAitdaammaEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQiQKLEARVRELEgEV 1830
Cdd:pfam17380 356 EERKRELERIRQ--------EEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQ-RKIQQQKVEME-QI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1831 ESEQKrNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEa 1910
Cdd:pfam17380 426 RAEQE-EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEE- 503
|
250 260
....*....|....*....|....*....
gi 305632842 1911 EERADIAESQVNKLRVKSREVHTKVISEE 1939
Cdd:pfam17380 504 RKQAMIEEERKRKLLEKEMEERQKAIYEE 532
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1534-1811 |
1.17e-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: 43.60 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1534 KKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVksevDRKIAEKDEEIDQLkrnhirivESMQSTLDAEIRsrn 1613
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRAL--------EQELAALEAELA--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1614 daiRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRTqedlkeqLAMVERRANLLQAEIEELR 1693
Cdd:COG4942 87 ---ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRR-------LQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1694 ATLEQTERSRKIAEQElldaservqllhtqntslintKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEEL 1773
Cdd:COG4942 157 ADLAELAALRAELEAE---------------------RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
250 260 270
....*....|....*....|....*....|....*...
gi 305632842 1774 KKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKG 1811
Cdd:COG4942 216 AELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
968-1279 |
1.60e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 968 VEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKK 1047
Cdd:COG4372 15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1048 LRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQarIEELEEEIE 1127
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ--EELAALEQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1128 AERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAEL 1207
Cdd:COG4372 173 LQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 305632842 1208 GEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTA 1279
Cdd:COG4372 253 EEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1196-1411 |
1.65e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.38 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1196 LRKKHADSvAELGEQIDNLQRVKQKLEKEKSE-MKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLI 1274
Cdd:PRK05771 45 LRKLRSLL-TKLSEALDKLRSYLPKLNPLREEkKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1275 NDLTaqrgRLQTESGEFSRQLDEK--DALVSQLSRGKQAFTQQIEElKRQLEEEIKAKN-----ALAHALQSSRHDCDLL 1347
Cdd:PRK05771 124 ERLE----PWGNFDLDLSLLLGFKyvSVFVGTVPEDKLEELKLESD-VENVEYISTDKGyvyvvVVVLKELSDEVEEELK 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305632842 1348 REQYEEEQ-ESKAELQRALSKANTEVAQWRTKYEtdaiQRTEELEEAKKKLAQRLQAAEEHVEAV 1411
Cdd:PRK05771 199 KLGFERLElEEEGTPSELIREIKEELEEIEKERE----SLLEELKELAKKYLEELLALYEYLEIE 259
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
906-1047 |
1.72e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.70 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 906 EERCDQLIKTKIQLEAKIKEVTEraeDEEEINAELTakkrkledECSELKKDIDDLELTL-AKVEKEKHATENKVKNLTE 984
Cdd:smart00787 136 EWRMKLLEGLKEGLDENLEGLKE---DYKLLMKELE--------LLNSIKPKLRDRKDALeEELRQLKQLEDELEDCDPT 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 305632842 985 EMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKK 1047
Cdd:smart00787 205 ELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1257-1483 |
2.02e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1257 EDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHA 1336
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1337 LQSSRHDCDLL---------------REQYEEEQESKAELQRALSKANTEVAQwrtkYETDAIQRTEELEEAKKKLAQRL 1401
Cdd:COG3883 95 LYRSGGSVSYLdvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEA----KKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1402 QAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSL 1481
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
..
gi 305632842 1482 GT 1483
Cdd:COG3883 251 AA 252
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1626-1925 |
2.03e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1626 LNEMEIQLnHANRMAAEALRNYRNTQGILK-------------------DTQLHLDDALRTQEDL---KEQLAMVERRAN 1683
Cdd:PRK04863 232 FQDMEAAL-RENRMTLEAIRVTQSDRDLFKhlitestnyvaadymrhanERRVHLEEALELRRELytsRRQLAAEQYRLV 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1684 LLQAEIEELratleqtERSRKIAEQELLDASERVQLLhtqNTSLINTKKkletdISQMQGEMEDI---LQEARNAEEKAK 1760
Cdd:PRK04863 311 EMARELAEL-------NEAESDLEQDYQAASDHLNLV---QTALRQQEK-----IERYQADLEELeerLEEQNEVVEEAD 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1761 KAITDAAMMAEELKKEQDtsahleRMKKNM--------EQTVKDLQLR-----LDEAEQ------LALKGGKKQIQKLEA 1821
Cdd:PRK04863 376 EQQEENEARAEAAEEEVD------ELKSQLadyqqaldVQQTRAIQYQqavqaLERAKQlcglpdLTADNAEDWLEEFQA 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1822 RVRELEGEV-ESEQK-RNAEAVKglRKHE------RRV-------------KELTYQTEEDRKNILRLQDLVDKLQA--- 1877
Cdd:PRK04863 450 KEQEATEELlSLEQKlSVAQAAH--SQFEqayqlvRKIagevsrseawdvaRELLRRLREQRHLAEQLQQLRMRLSEleq 527
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 305632842 1878 ---KVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLR 1925
Cdd:PRK04863 528 rlrQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEAR 578
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1422-1778 |
2.07e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1422 KQRLQNEVEDLMLDVERTNAACAALDKKQRNFDK---ILAEWKQKYEETHAELEASQKEARslgtelfkmknayeesldq 1498
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaIYAEQERMAMERERELERIRQEER------------------- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1499 letlKRENKNLQQEisdlteQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEgkilriqlelnqvksEVDR 1578
Cdd:pfam17380 359 ----KRELERIRQE------EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEE---------------ERQR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1579 KIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKkkmegdlnEMEIQlnhanrMAAEALRNYRNTQgilKDTQ 1658
Cdd:pfam17380 414 KIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE--------EQERQ------QQVERLRQQEEER---KRKK 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1659 LHLDDALRTQEDLKEQlamverRANLLQAEIEELRATLEQTERSRKIAEQELLDaservqllhTQNTSLINTKKKLETDI 1738
Cdd:pfam17380 477 LELEKEKRDRKRAEEQ------RRKILEKELEERKQAMIEEERKRKLLEKEMEE---------RQKAIYEEERRREAEEE 541
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 305632842 1739 SQMQGEMEdilqEARNAEEKAKKAITDAAMMaEELKKEQD 1778
Cdd:pfam17380 542 RRKQQEME----ERRRIQEQMRKATEERSRL-EAMERERE 576
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
916-1101 |
2.07e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 916 KIQLEAKIKEVTERAE---DEEEINAELTAKKRKLEdecseLKKDIDDLEltlAKVEKEKHATENKVKNLteemagldet 992
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKrilEEAKKEAEAIKKEALLE-----AKEEIHKLR---NEFEKELRERRNELQKL---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 993 iakltkEKKALQeaHQQTLDDlqaeedKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgdLKLAQESIMD 1072
Cdd:PRK12704 88 ------EKRLLQ--KEENLDR------KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQL--QELERISGLT 151
|
170 180 190
....*....|....*....|....*....|
gi 305632842 1073 IENEKQQLDEKLKKK-EFEISNLQSKIEDE 1101
Cdd:PRK12704 152 AEEAKEILLEKVEEEaRHEAAVLIKEIEEE 181
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1680-1918 |
2.09e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.73 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1680 RRANLLQAEIEELratLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDIlqearnaEEKA 1759
Cdd:COG1842 5 RLSDIIRANINAL---LDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW-------EEKA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1760 KKAitdaammaeeLKKEQDTSAH--LERmKKNMEQTVKDLQLRLDEAEQLALKGgKKQIQKLEARVRELEGEVES--EQK 1835
Cdd:COG1842 75 RLA----------LEKGREDLAReaLER-KAELEAQAEALEAQLAQLEEQVEKL-KEALRQLESKLEELKAKKDTlkARA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1836 RNAEAVKGLRKHERRVkeltyQTEEDRKNILRLQDLVDKLQAKVKSYkrqAEEAEEQSntnlakfrkLQHELEEAEERAD 1915
Cdd:COG1842 143 KAAKAQEKVNEALSGI-----DSDDATSALERMEEKIEEMEARAEAA---AELAAGDS---------LDDELAELEADSE 205
|
...
gi 305632842 1916 IAE 1918
Cdd:COG1842 206 VED 208
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1087-1324 |
2.10e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1087 KEFEISNLQSKIEDEQALGIQLQKKIKELQARIeeleeeieaerasrAKAEKQRSDLSRELEEISerLEEAGGATSAQIe 1166
Cdd:COG3206 159 EAYLEQNLELRREEARKALEFLEEQLPELRKEL--------------EEAEAALEEFRQKNGLVD--LSEEAKLLLQQL- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1167 mnkkreAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNlqRVKQKLEKEKSEMKMEIDDLAsnvetvSKAK 1246
Cdd:COG3206 222 ------SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELS------ARYT 287
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305632842 1247 GNLEKMcRTLEDQVSELKSK-EEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRgKQaftQQIEELKRQLE 1324
Cdd:COG3206 288 PNHPDV-IALRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE-LE---AELRRLEREVE 361
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1239-1326 |
2.11e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 41.07 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1239 VETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQ--- 1315
Cdd:pfam08614 66 LAELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQlnm 145
|
90
....*....|.
gi 305632842 1316 IEELKRQLEEE 1326
Cdd:pfam08614 146 AEEKLRKLEKE 156
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1484-1877 |
2.14e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1484 ELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEqEKCELQAALEEAEASLEheegkil 1563
Cdd:PRK04863 301 QLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQA-DLEELEERLEEQNEVVE------- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1564 riqlELNQVKSEVDRKIAEKDEEIDQLKRNhiriVESMQSTLDAEIR---SRNDAIRLKKKMEGDLNEMEIQLNHANRMA 1640
Cdd:PRK04863 373 ----EADEQQEENEARAEAAEEEVDELKSQ----LADYQQALDVQQTraiQYQQAVQALERAKQLCGLPDLTADNAEDWL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1641 AEalrnYRNTQGILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDasERVQLL 1720
Cdd:PRK04863 445 EE----FQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLA--EQLQQL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1721 HTQntslintkkkletdisqmQGEMEDILQEARNAEEKAKKAitdaammAEELKKEQDTSAHLERMKKNMEQTVKDLQLR 1800
Cdd:PRK04863 519 RMR------------------LSELEQRLRQQQRAERLLAEF-------CKRLGKNLDDEDELEQLQEELEARLESLSES 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1801 LDEAEQLALkGGKKQIQKLEARVRELE----------------GEVESEQKRNAEAVKGLRK-HERRVKELTYQTEEDRK 1863
Cdd:PRK04863 574 VSEARERRM-ALRQQLEQLQARIQRLAarapawlaaqdalarlREQSGEEFEDSQDVTEYMQqLLERERELTVERDELAA 652
|
410
....*....|....
gi 305632842 1864 NILRLQDLVDKLQA 1877
Cdd:PRK04863 653 RKQALDEEIERLSQ 666
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
847-972 |
2.26e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.08 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 847 AETEKEMATMKEEFQKTKDELAKSEAKRKELEekmvtLLKEKNDLQLQVQAEAEGLADAEERCdqliktkIQLEAKIKEV 926
Cdd:PTZ00491 672 AELLEQEARGRLERQKMHDKAKAEEQRTKLLE-----LQAESAAVESSGQSRAEALAEAEARL-------IEAEAEVEQA 739
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 305632842 927 TERAEDEE-EINAELTAKKRKLEDECsELKKDIDDLELT----LAKVEKEK 972
Cdd:PTZ00491 740 ELRAKALRiEAEAELEKLRKRQELEL-EYEQAQNELEIAkakeLADIEATK 789
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
911-1540 |
2.31e-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: 42.81 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 911 QLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL- 989
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 990 --DETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNT-LTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgDLKLA 1066
Cdd:pfam05557 83 kyLEALNKKLNEKESQLADAREVISCLKNELSELRRqIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQ-NLEKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1067 QESIMDIEnekqqldEKLKKKEFEISnlqskiedEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSD---L 1143
Cdd:pfam05557 162 QSSLAEAE-------QRIKELEFEIQ--------SQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENkllL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1144 SRELEEISERLEEAGGATSAQIEMnkkrEAEFQKMRRDLEEATLQHEATAATLRKKHAdsvaeLGEQIDNLQRVKQKLEK 1223
Cdd:pfam05557 227 KEEVEDLKRKLEREEKYREEAATL----ELEKEKLEQELQSWVKLAQDTGLNLRSPED-----LSRRIEQLQQREIVLKE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1224 EKSemkmeidDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQqrlindltaqrgrlqtesgefsrqldekDALVS 1303
Cdd:pfam05557 298 ENS-------SLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRH----------------------------KALVR 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1304 QLSRGKQAFTQQIEELKRQLE---EEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRT-KY 1379
Cdd:pfam05557 343 RLQRRVLLLTKERDGYRAILEsydKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTlER 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1380 ETDAIQRTEELEEAkkklaqrlQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAE 1459
Cdd:pfam05557 423 ELQALRQQESLADP--------SYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNP 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1460 WKQKYEETHAELEASQKEARSLGTELFKMknayEESLDQLETLKRENKNLQ-QEISDLTEQIAEGGKRIHELEKIKKQVE 1538
Cdd:pfam05557 495 AAEAYQQRKNQLEKLQAEIERLKRLLKKL----EDDLEQVLRLPETTSTMNfKEVLDLRKELESAELKNQRLKEVFQAKI 570
|
..
gi 305632842 1539 QE 1540
Cdd:pfam05557 571 QE 572
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1813-1921 |
2.57e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1813 KKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKEL---TYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEA 1889
Cdd:COG2433 412 EEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArseERREIRKDREISRLDREIERLERELEEERERIEEL 491
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 305632842 1890 EEQSNTnLAKFRKLQH----------------ELEEAEERADIAESQV 1921
Cdd:COG2433 492 KRKLER-LKELWKLEHsgelvpvkvvekftkeAIRRLEEEYGLKEGDV 538
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1425-1738 |
2.64e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1425 LQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKR 1504
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1505 ENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQvksevdRKIAEKD 1584
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA------LSEAEAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1585 EEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNhanrmAAEALRNYRNTQGILKDTQLHLDDA 1664
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG-----LALSALLDALELEEDKEELLEEVIL 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 305632842 1665 LRTQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDI 1738
Cdd:COG4372 258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELA 331
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
847-1177 |
2.64e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 847 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEV 926
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 927 TERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKalqea 1006
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA----- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1007 hQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKK 1086
Cdd:COG4372 182 -EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1087 KEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIE 1166
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
330
....*....|.
gi 305632842 1167 MNKKREAEFQK 1177
Cdd:COG4372 341 DLLQLLLVGLL 351
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
1166-1577 |
2.77e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 42.63 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1166 EMNKKREAEFQ-----------KMRRDLEEATLQHEATaaTLRKKHADSVAELGEQidnLQRVKQKLEKEKSEMKM---- 1230
Cdd:pfam15818 15 ELRMRREAETQyeeqigkiiveTQELKWQKETLQNQKE--TLAKQHKEAMAVFKKQ---LQMKMCALEEEKGKYQLatei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1231 ---EIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLIND-------LTAQRGRLQTESGEFSRQLDEKDA 1300
Cdd:pfam15818 90 kekEIEGLKETLKALQVSKYSLQKKVSEMEQKLQLHLLAKEDHHKQLNEiekyyatITGQFGLVKENHGKLEQNVQEAIQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1301 LVSQLSRGKQAFTQQI----EELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQEsKAELQRALSKANTEvaqwr 1376
Cdd:pfam15818 170 LNKRLSALNKKQESEIcslkKELKKVTSDLIKSKVTCQYKMGEENINLTIKEQKFQELQE-RLNMELELNKKINE----- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1377 tkyETDAIQrtEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKI 1456
Cdd:pfam15818 244 ---EITHIQ--EEKQDIIISFQHMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQREKVKENEEKFLNLQNEHEKA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1457 LAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEK---- 1532
Cdd:pfam15818 319 LGTWKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQKKFEEDKKFQNVPEVNNENSEMSTEKSENLIIQKynse 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 305632842 1533 --IKKQVEQEKCELQAALE-EAEASLEHEEGKILRIQLELNQVKSEVD 1577
Cdd:pfam15818 399 qeIREENTKSFCSDTEYREtEKKKGPPVEEIIIEDLQVLEKSFKNEID 446
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1438-1582 |
3.12e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1438 RTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEarslgtELFKMKNAYE-ESLDQLETLKRENKNLQQEISDL 1516
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKE------EIHKLRNEFEkELRERRNELQKLEKRLLQKEENL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 305632842 1517 TEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRI---------QLELNQVKSEVDRKIAE 1582
Cdd:PRK12704 99 DRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsgltaeeakEILLEKVEEEARHEAAV 173
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1551-1781 |
3.16e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1551 AEASLEHEEGKILRIQLELNQVKSEVDrkiaEKDEEIDQLKRNHIRIVESMQsTLDAEIrsrndairlkKKMEGDLNEME 1630
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELD----ALQAELEELNEEYNELQAELE-ALQAEI----------DKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1631 IQLNHANRMAAEALRNYRNTQGILKDTqlhldDALRTQEDLKEQLamveRRANLLQAEIEELRATLEQTERSRKIAEQEL 1710
Cdd:COG3883 79 AEIEERREELGERARALYRSGGSVSYL-----DVLLGSESFSDFL----DRLSALSKIADADADLLEELKADKAELEAKK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305632842 1711 LDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSA 1781
Cdd:COG3883 150 AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
844-974 |
3.18e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 844 LKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVqaeaegladaeERCDQLIKtkiQLEAKI 923
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAEL-----------EEKDERIE---RLEREL 450
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 305632842 924 KEVTERAEDEEEINAELTAKKRK---LEDECSELKKDIDDLEltlAKVEKEKHA 974
Cdd:COG2433 451 SEARSEERREIRKDREISRLDREierLERELEEERERIEELK---RKLERLKEL 501
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1706-1892 |
3.29e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1706 AEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEmediLQEARNAEEKAKKAITDAAMMAEELKKE-QDTSAHLE 1784
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDE----LAALEARLEAAKTELEDLEKEIKRLELEiEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1785 RMKKNMEQ--TVKDLQLRLDEAEQLalkggKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELtyqteedr 1862
Cdd:COG1579 77 KYEEQLGNvrNNKEYEALQKEIESL-----KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK-------- 143
|
170 180 190
....*....|....*....|....*....|
gi 305632842 1863 knILRLQDLVDKLQAKVKSYKRQAEEAEEQ 1892
Cdd:COG1579 144 --KAELDEELAELEAELEELEAEREELAAK 171
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1210-1401 |
3.74e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1210 QIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTAQRgrlqtesg 1289
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1290 EFsrqldekdalvsqlsrgkQAFTQQIEELKRQ---LEEEIKAKNALAHALQssrhdcdllrEQYEEEQESKAELQRALS 1366
Cdd:COG1579 90 EY------------------EALQKEIESLKRRisdLEDEILELMERIEELE----------EELAELEAELAELEAELE 141
|
170 180 190
....*....|....*....|....*....|....*
gi 305632842 1367 KANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRL 1401
Cdd:COG1579 142 EKKAELDEELAELEAELEELEAEREELAAKIPPEL 176
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1776-1939 |
3.79e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1776 EQDTSAHLERMKKNMEQtvkdlqlrLDEAEQLALKGgKKQIQKLEaRVRELEGEVEsEQKRNAEAVKGLR------KHER 1849
Cdd:COG4913 220 EPDTFEAADALVEHFDD--------LERAHEALEDA-REQIELLE-PIRELAERYA-AARERLAELEYLRaalrlwFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1850 RVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTN-LAKFRKLQHELEEAEERADIAESQVNKLRVKS 1928
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALL 368
|
170
....*....|.
gi 305632842 1929 REVHTKVISEE 1939
Cdd:COG4913 369 AALGLPLPASA 379
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
902-1180 |
4.07e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 902 LADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKN 981
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 982 LTEEMAGLDETIAKLTKEKKALQEAHQQtLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRmDLERAKRKLEG 1061
Cdd:COG1340 90 LREELDELRKELAELNKAGGSIDKLRKE-IERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKAL-EKNEKLKELRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1062 DLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRS 1141
Cdd:COG1340 168 ELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247
|
250 260 270
....*....|....*....|....*....|....*....
gi 305632842 1142 DLSRELEEISERLEEAggatsaqiEMNKKREAEFQKMRR 1180
Cdd:COG1340 248 KLRKKQRALKREKEKE--------ELEEKAEEIFEKLKK 278
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1382-1676 |
4.11e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1382 DAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNevedlmldvertnaACAALDKKQRNFDKILAEWK 1461
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQ--------------APAKLRQAQAELEALKDDND 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1462 QKYEETHAELEASQKEARSlgtelfkmknayEESLDQLETLKRE----NKNL--QQEISDLTE-QIAEGGKRIHELEKIK 1534
Cdd:PRK11281 112 EETRETLSTLSLRQLESRL------------AQTLDQLQNAQNDlaeyNSQLvsLQTQPERAQaALYANSQRLQQIRNLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1535 KQVEQEKCEL---QAALEEAEASLeheegkiLRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRS 1611
Cdd:PRK11281 180 KGGKVGGKALrpsQRVLLQAEQAL-------LNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAINS 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 305632842 1612 RNdAIRLKKKMEGDLNEMEIQLNHANRM-AAEALRNYRNTQGILKDTQL-------------HLDDALRTQEDLKEQLA 1676
Cdd:PRK11281 253 KR-LTLSEKTVQEAQSQDEAARIQANPLvAQELEINLQLSQRLLKATEKlntltqqnlrvknWLDRLTQSERNIKEQIS 330
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
957-1059 |
4.47e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 957 DIDDLELTLAKVEKEKHATENkvknltEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVD 1036
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKK------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100
....*....|....*....|...
gi 305632842 1037 DLEGSLEQEKKLRMDLERAKRKL 1059
Cdd:COG0542 486 KIPELEKELAELEEELAELAPLL 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
842-1006 |
4.52e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 842 PLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEA 921
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 922 KIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLE---LT----LAKVEKEKHATENKVKNLTEEMAGLDETIA 994
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGpvnLLaieeYEELEERYDFLSEQREDLEEARETLEEAIE 819
|
170
....*....|...
gi 305632842 995 KLTKEKK-ALQEA 1006
Cdd:COG1196 820 EIDRETReRFLET 832
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1610-1927 |
4.57e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 42.23 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1610 RSRNDAI-RLKKKMEGDL------NEMEIQLNHANRMAAEAlrnYRNTQGILKdTQLHLDdalRTQEDL---KEQLAMVE 1679
Cdd:PLN03188 915 QTREDKIiRLESLMDGVLskedflEEELASLMHEHKLLKEK---YENHPEVLR-TKIELK---RVQDELehyRNFYDMGE 987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1680 RraNLLQAEIEELRATLEQTERSrkiaeqELLDASERVQLLHTQNTSLINTKKKLETdISQMQGEM--EDILQEARNAEE 1757
Cdd:PLN03188 988 R--EVLLEEIQDLRSQLQYYIDS------SLPSARKRNSLLKLTYSCEPSQAPPLNT-IPESTDESpeKKLEQERLRWTE 1058
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1758 KAKKAITdaamMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQK----------LEARVRELE 1827
Cdd:PLN03188 1059 AESKWIS----LAEELRTELDASRALAEKQKHELDTEKRCAEELKEAMQMAMEGHARMLEQyadleekhiqLLARHRRIQ 1134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1828 GEVESEQKRNAEA-VKGLR--------------KHERRvKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRqAEEAEEQ 1892
Cdd:PLN03188 1135 EGIDDVKKAAARAgVRGAEskfinalaaeisalKVERE-KERRYLRDENKSLQAQLRDTAEAVQAAGELLVR-LKEAEEA 1212
|
330 340 350
....*....|....*....|....*....|....*
gi 305632842 1893 SNTnlakfrkLQHELEEAEERADIAESQVNKLRVK 1927
Cdd:PLN03188 1213 LTV-------AQKRAMDAEQEAAEAYKQIDKLKRK 1240
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1172-1432 |
4.79e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1172 EAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEK 1251
Cdd:pfam00038 24 EQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAEN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1252 MCRTLEDQVSEL---KSKEEEQ-QRLINDLTAQRGRLQTESGEFSRQLDEKDALVSQLSRGKQAFTQQIEELKRQLeEEI 1327
Cdd:pfam00038 104 DLVGLRKDLDEAtlaRVDLEAKiESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQY-EEI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1328 KAKNalahalqssrhdcdllREQYEEEQESK-AELQRALSKantevaqwrtkyETDAIQRT-EELEEAKKklaqRLQAAE 1405
Cdd:pfam00038 183 AAKN----------------REEAEEWYQSKlEELQQAAAR------------NGDALRSAkEEITELRR----TIQSLE 230
|
250 260 270
....*....|....*....|....*....|.
gi 305632842 1406 EHVEAVNAKCASLEK----TKQRLQNEVEDL 1432
Cdd:pfam00038 231 IELQSLKKQKASLERqlaeTEERYELQLADY 261
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
769-1114 |
4.88e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 41.86 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 769 FKAGLLGLLEEMR---------DDKLAQLITRTQarcrgflaRVEYQRMVERREAIFCIQYNIRAFMNVKHWPWMKLFF- 838
Cdd:pfam15818 5 FKTSLLEALEELRmrreaetqyEEQIGKIIVETQ--------ELKWQKETLQNQKETLAKQHKEAMAVFKKQLQMKMCAl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 839 ---KIKPLLKSAETEKEMATMKE---EFQKTKDELAKseaKRKELEEKMVTLLKEKNDLQLQVqaeaeglaDAEERCDQL 912
Cdd:pfam15818 77 eeeKGKYQLATEIKEKEIEGLKEtlkALQVSKYSLQK---KVSEMEQKLQLHLLAKEDHHKQL--------NEIEKYYAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 913 IKTKIQLEAKIKEVTERAEDEE-EINAELTAKKRKLEDECSELKKDIDDL--ELTLAKVE-KEKHATEN--------KVK 980
Cdd:pfam15818 146 ITGQFGLVKENHGKLEQNVQEAiQLNKRLSALNKKQESEICSLKKELKKVtsDLIKSKVTcQYKMGEENinltikeqKFQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 981 NLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEgslEQEKKLRMDLERAKRKLe 1060
Cdd:pfam15818 226 ELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALK---ENNQTLERDNELQREKV- 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 305632842 1061 gdlKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKE 1114
Cdd:pfam15818 302 ---KENEEKFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQE 352
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
929-1116 |
4.91e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 41.97 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 929 RAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKV---EKEKHATENKVKNLTEEMAGLDETIAKLTK--EKKAL 1003
Cdd:pfam13166 270 KAALEAHFDDEFTEFQNRLQKLIEKVESAISSLLAQLPAVsdlASLLSAFELDVEDIESEAEVLNSQLDGLRRalEAKRK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1004 QEAHQQTLDDLQAEEDKVNTLTKAKTKL----EQQVDDLEgsleqEKKlrmdlERAKRKLEGDLklaqesIMDIENEKQQ 1079
Cdd:pfam13166 350 DPFKSIELDSVDAKIESINDLVASINELiakhNEITDNFE-----EEK-----NKAKKKLRLHL------VEEFKSEIDE 413
|
170 180 190
....*....|....*....|....*....|....*..
gi 305632842 1080 LDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQ 1116
Cdd:pfam13166 414 YKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELE 450
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
952-1098 |
5.17e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.60 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 952 SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDL----------------- 1014
Cdd:PRK11637 71 ASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAQLDAAfrqgehtglqlilsgee 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1015 ---------------QAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIEN---- 1075
Cdd:PRK11637 151 sqrgerilayfgylnQARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESslqk 230
|
170 180
....*....|....*....|...
gi 305632842 1076 EKQQLDEkLKKKEfeiSNLQSKI 1098
Cdd:PRK11637 231 DQQQLSE-LRANE---SRLRDSI 249
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
910-1182 |
5.28e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 910 DQLIKTKIQ---------------LEAKIKEVTERAEDEEEINAELTAKKR----KLEDECSELKKDIDDLELTLAKVEK 970
Cdd:PHA02562 169 DKLNKDKIRelnqqiqtldmkidhIQQQIKTYNKNIEEQRKKNGENIARKQnkydELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 971 EKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQ-----QTLDDlqaEEDKVntltkakTKLEQQVDDLEGSLEQE 1045
Cdd:PHA02562 249 DIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGVcptctQQISE---GPDRI-------TKIKDKLKELQHSLEKL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1046 KKlrmdlerakrklegdlklaqesimDIENEKQQLDEkLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEeleee 1125
Cdd:PHA02562 319 DT------------------------AIDELEEIMDE-FNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIE----- 368
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 305632842 1126 ieaerasraKAEKQRSDLSRELEEISERLEEAGgatsaqiemNKKREAEFQKMRRDL 1182
Cdd:PHA02562 369 ---------ELQAEFVDNAEELAKLQDELDKIV---------KTKSELVKEKYHRGI 407
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
1004-1098 |
5.70e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 39.22 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1004 QEAHQQTLDDLQAE-EDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDE 1082
Cdd:pfam11559 54 RESLNETIRTLEAEiERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQIKTQFAH 133
|
90
....*....|....*.
gi 305632842 1083 KLKKKEFEISNLQSKI 1098
Cdd:pfam11559 134 EVKKRDREIEKLKERL 149
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
989-1115 |
6.39e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 989 LDETIAK-LTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEqekklrmDLERAKRKLEGDLKLAQ 1067
Cdd:COG2433 382 LEELIEKeLPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELE-------EKDERIERLERELSEAR 454
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 305632842 1068 ESimdiENEKQQLDEKLKKKEFEISNLQSKIEDEQalgiqlqKKIKEL 1115
Cdd:COG2433 455 SE----ERREIRKDREISRLDREIERLERELEEER-------ERIEEL 491
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
876-1002 |
6.47e-03 |
|
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.
Pssm-ID: 462986 [Multi-domain] Cd Length: 347 Bit Score: 40.90 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 876 ELEEKMVTLLKEKNDLQLQVQAEAEG-----LADAEERCD----QLIKTKI-QLEAKIKEVTERAEdeeEINAELTAKKR 945
Cdd:pfam10186 23 ELRVDLARLLSEKDSLKKKVEEALEGkeegeQLEDNIGNKklklRLLKSEVaISNERLNEIKDKLD---QLRREIAEKKK 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 305632842 946 KLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKA 1002
Cdd:pfam10186 100 KIEKLRSSLKQRRSDLESASYQLEERRASQLAKLQNSIKRIKQKWTALHSKTAESRS 156
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1678-1917 |
6.73e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.67 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1678 VERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLhtqntslintKKKLETDISQMQgEMEDILQEARNAEE 1757
Cdd:pfam00038 45 PSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDF----------RQKYEDELNLRT-SAENDLVGLRKDLD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1758 KAKKAITDAAMMAEELKKEqdtsahLERMKKNMEQTVKDLQLRLDEAEQL-------------ALKGGKKQIQKLEARVR 1824
Cdd:pfam00038 114 EATLARVDLEAKIESLKEE------LAFLKKNHEEEVRELQAQVSDTQVNvemdaarkldltsALAEIRAQYEEIAAKNR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1825 -ELE-------GEVESEQKRNAEAVKGLRKherrvkELTyqteEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTN 1896
Cdd:pfam00038 188 eEAEewyqsklEELQQAAARNGDALRSAKE------EIT----ELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQ 257
|
250 260
....*....|....*....|...
gi 305632842 1897 LAKFRKLQHELEEA--EERADIA 1917
Cdd:pfam00038 258 LADYQELISELEAElqETRQEMA 280
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1664-1859 |
6.83e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1664 ALRTQEDLKEQLAMVERRAN------LLQAEIEELRATLEQTERSRKI----------AEQELLDASERVQLLHTQNTSL 1727
Cdd:PRK11281 34 DLPTEADVQAQLDALNKQKLleaedkLVQQDLEQTLALLDKIDRQKEEteqlkqqlaqAPAKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1728 INTK------KKLETDISQMQGEMEDiLQEA-----------RNAEEKAKKAITDAAMMAEE----LKKEQDTSAHL--- 1783
Cdd:PRK11281 114 TRETlstlslRQLESRLAQTLDQLQN-AQNDlaeynsqlvslQTQPERAQAALYANSQRLQQirnlLKGGKVGGKALrps 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1784 ERMKKNMEQTVKDLQLRLdeaEQLALKG-------GKKQIQKLEARVRELEGEVESEQkrnaEAV--KGLRKHERRVKEL 1854
Cdd:PRK11281 193 QRVLLQAEQALLNAQNDL---QRKSLEGntqlqdlLQKQRDYLTARIQRLEHQLQLLQ----EAInsKRLTLSEKTVQEA 265
|
....*
gi 305632842 1855 TYQTE 1859
Cdd:PRK11281 266 QSQDE 270
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1008-1101 |
6.86e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 40.99 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1008 QQTLDDLQAEEDKVNT--------LTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQ------------ 1067
Cdd:pfam03148 232 EQTANDLRAQADAVNFalrkrieeTEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKLAQtrlenrtyrpnv 311
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 305632842 1068 ------------ESIMDIENEKQQLDEKLKKKEFEISNL---QSKIEDE 1101
Cdd:pfam03148 312 elcrdeaqyglvDEVKELEETIEALKQKLAEAEASLQALertRLRLEED 360
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1294-1524 |
6.88e-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: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1294 QLDEKDALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANteVA 1373
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA--RA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1374 QWRTKYE-------------TDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTN 1440
Cdd:COG3883 95 LYRSGGSvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1441 AACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQI 1520
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
....
gi 305632842 1521 AEGG 1524
Cdd:COG3883 255 AGAA 258
|
|
| PRK15374 |
PRK15374 |
type III secretion system needle tip complex protein SipB; |
1147-1365 |
7.12e-03 |
|
type III secretion system needle tip complex protein SipB;
Pssm-ID: 185272 [Multi-domain] Cd Length: 593 Bit Score: 41.10 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1147 LEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLrkKHADSVAE-LGEQIDNLQRVKQKLEKEK 1225
Cdd:PRK15374 101 LSQLESRLAVWQAMIESQKEMGIQVSKEFQTALGEAQEATDLYEASIKKT--DTAKSVYDaAEKKLTQAQNKLQSLDPAD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1226 SEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQqrlINDLTAQRGRLQTESGEFSRQLDEKDalVSQL 1305
Cdd:PRK15374 179 PGYAQAEAAVEQAGKEATEAKEALDKATDATVKAGTDAKAKAEKA---DNILTKFQGTANAASQNQVSQGEQDN--LSNV 253
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 305632842 1306 SRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRH-DCDLLREQYEEEQESKAELQRAL 1365
Cdd:PRK15374 254 ARLTMLMAMFIEIVGKNTEESLQNDLALFNALQEGRQaEMEKKSAEFQEETRKAEETNRIM 314
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1420-1822 |
7.43e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 41.43 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1420 KTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLD-Q 1498
Cdd:pfam15964 300 QTIERLTKERDDLMSALVSVRSSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKELAsQ 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1499 LETLKRENKNLQQEISDLTEQIAEG----GKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKS 1574
Cdd:pfam15964 380 QEKRAQEKEALRKEMKKEREELGATmlalSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQLN 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1575 EVDRKIAEKDEEIDQLKRNHIRIVEsmqsTLDAEIrsrndairlkKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGIL 1654
Cdd:pfam15964 460 QTKMKKDEAEKEHREYRTKTGRQLE----IKDQEI----------EKLGLELSESKQRLEQAQQDAARAREECLKLTELL 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1655 KDT--QLHLDdalRTQEDLKEQLAMVERRANLLQAEIEElratLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTK- 1731
Cdd:pfam15964 526 GESehQLHLT---RLEKESIQQSFSNEAKAQALQAQQRE----QELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKe 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1732 ------KKLETDISQMQGEMEDILQEARNAEEKAKKaitdaamMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAE 1805
Cdd:pfam15964 599 ecctlaKKLEEITQKSRSEVEQLSQEKEYLQDRLEK-------LQKRNEELEEQCVQHGRMHERMKQRLRQLDKHCQATA 671
|
410
....*....|....*..
gi 305632842 1806 QLALKGGKKQIQKLEAR 1822
Cdd:pfam15964 672 QQLVQLLSKQNQLFKER 688
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1258-1636 |
8.01e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 8.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1258 DQVSELKSKEEEQQRLINDLT-AQRGRLQTEsgefsRQLDEKDALVSQLSrgkQAfTQQIEELKRQLEEeIKAKNALAHA 1336
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEqTLALLDKID-----RQKEETEQLKQQLA---QA-PAKLRQAQAELEA-LKDDNDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1337 LQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYE------TDAIQRTEELEEAKK--KLAQRLQAAEEHV 1408
Cdd:PRK11281 116 ETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPEraqaalYANSQRLQQIRNLLKggKVGGKALRPSQRV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1409 EaVNAKCASLE-KTKQR---LQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKY----EETHAELEASQKEARS 1480
Cdd:PRK11281 196 L-LQAEQALLNaQNDLQrksLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAINSKRltlsEKTVQEAQSQDEAARI 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1481 LGTELFKMKNAYE--------ESLDQLETLKREN---KN----LQQEISDLTEQIA--EGG---KRIhelekikkqVEQE 1540
Cdd:PRK11281 275 QANPLVAQELEINlqlsqrllKATEKLNTLTQQNlrvKNwldrLTQSERNIKEQISvlKGSlllSRI---------LYQQ 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1541 KCELQAALEEAEASleheeGKI--LRI-QLELNQVKSevdrKIAEKDEEIDQLKRNHirivesmQSTLDAEIR-SRNDAI 1616
Cdd:PRK11281 346 QQALPSADLIEGLA-----DRIadLRLeQFEINQQRD----ALFQPDAYIDKLEAGH-------KSEVTDEVRdALLQLL 409
|
410 420
....*....|....*....|.
gi 305632842 1617 RLKKKMEGDLN-EMEIQLNHA 1636
Cdd:PRK11281 410 DERRELLDQLNkQLNNQLNLA 430
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1623-1924 |
9.04e-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: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1623 EGDLnEMEIQL--NHANRM-----AAEALRNYrntQGILKDTQLHLDDALRTQEDLKEQLAMVERRANLLQAEIEELR-- 1693
Cdd:COG3096 322 ESDL-EQDYQAasDHLNLVqtalrQQEKIERY---QEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKsq 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1694 -ATLEQ---TERSRKIAEQELLDASERVQLLhTQNTSLinTKKKLETDISQMQGEMEDILQEARNAEEK-----AKKAIT 1764
Cdd:COG3096 398 lADYQQaldVQQTRAIQYQQAVQALEKARAL-CGLPDL--TPENAEDYLAAFRAKEQQATEEVLELEQKlsvadAARRQF 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1765 DAAM-----MAEELKKEQDTSAHLE-----RMKKNMEQTVKDLQLRLDEAEQLA---------LKGGKKQI--------- 1816
Cdd:COG3096 475 EKAYelvckIAGEVERSQAWQTAREllrryRSQQALAQRLQQLRAQLAELEQRLrqqqnaerlLEEFCQRIgqqldaaee 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1817 -----QKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKnilrLQDLVDKLQAKVKSYKRQAEEAEE 1891
Cdd:COG3096 555 leellAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLA----AQDALERLREQSGEALADSQEVTA 630
|
330 340 350
....*....|....*....|....*....|...
gi 305632842 1892 QSNTNLAKFRKLQHELEEAEERADIAESQVNKL 1924
Cdd:COG3096 631 AMQQLLEREREATVERDELAARKQALESQIERL 663
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
915-1110 |
9.06e-03 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 40.97 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 915 TKIQLEAKIKEVTERaedeeeinaelTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIA 994
Cdd:pfam15066 340 SNLYLEKKVKELQMK-----------ITKQQVFVDIINKLKENVEELIEDKYNVILEKNDINKTLQNLQEILANTQKHLQ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 995 KLTKEKKALQeahqqtlddLQAEEDKVNTL---TKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKR--KLEGDLKLAQES 1069
Cdd:pfam15066 409 ESRKEKETLQ---------LELKKIKVNYVhlqERYITEMQQKNKSVSQCLEMDKTLSKKEEEVERlqQLKGELEKATTS 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 305632842 1070 IMDI--------ENEKQQLDEKLKKKEFEisnlqsKIEDEQALGIQLQK 1110
Cdd:pfam15066 480 ALDLlkreketrEQEFLSLQEEFQKHEKE------NLEERQKLKSRLEK 522
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1686-1892 |
9.56e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1686 QAEIEELRATLEQTERSRKIAEQELLDASERVQllhtqntSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITD 1765
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELE-------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 305632842 1766 AAMMAEELKKEQDTSAHLERMK--KNMEQTVKDLQL--RLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNAEAv 1841
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLLgsESFSDFLDRLSAlsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 305632842 1842 kglrkhERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQ 1892
Cdd:COG3883 167 ------EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| |
