|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
83-751 |
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: 1316.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd01380 1 PAVLHNLKVRFCQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 163 GESGAGKTVSAKYAMRYFATVSGSAS-EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATVGGSSSgETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 242 YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESH 321
Cdd:cd01380 161 YLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 322 QMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARD 401
Cdd:cd01380 241 QMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 402 ALAKHIYAKLFNWIVDNVNQALHSAV--KQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 479
Cdd:cd01380 321 ALAKHIYAQLFDWIVDRINKALASPVkeKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 480 EQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNK-CALFEKPRLSNKAFIIQHFADKVE 558
Cdd:cd01380 401 EEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTAFIVKHFADDVE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 559 YQCEGFLEKNKDTVFEEQIKVLKSSKFkmlpelfqddekaisptsatssgrtpltrtpakptkgrpgqmakeHKKTVGHQ 638
Cdd:cd01380 481 YQVEGFLEKNRDTVSEEHLNVLKASKN---------------------------------------------RKKTVGSQ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 639 FRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKD 718
Cdd:cd01380 516 FRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKE 595
|
650 660 670
....*....|....*....|....*....|....
gi 2462544153 719 VL-SDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01380 596 WLrDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
72-751 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1076.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 72 NDLTALSYLHEPAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMA 151
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRY-KSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 152 RDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEAN---VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGF 228
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNvgrLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 229 DKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHT 308
Cdd:pfam00063 161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 309 RQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYI 388
Cdd:pfam00063 241 DKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETVS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 389 KPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHS-AVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNM 467
Cdd:pfam00063 321 KPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVkTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 468 HVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKPRL-SN 545
Cdd:pfam00063 401 HMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKpLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHFQKPRLqGE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 546 KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPltrtpaKPTKgrpg 625
Cdd:pfam00063 480 THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTP------KRTK---- 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 626 qmaKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:pfam00063 550 ---KKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQE 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2462544153 706 FFSRYRVLMKQKDV--LSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:pfam00063 627 FVQRYRILAPKTWPkwKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
64-762 |
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: 1015.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 64 NPDILVGENDLTALSYLHEPAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVA 143
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRY-LKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 144 EEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEAN-VEEKVLASNPIMESIGNAKTTRNDNSSRFGK 222
Cdd:smart00242 80 DNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGsVEDQILESNPILEAFGNAKTLRNNNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 223 YIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDA 302
Cdd:smart00242 160 FIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 303 KEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDAD-SCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRKLA 381
Cdd:smart00242 240 EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDnAASTVKDKEELSNAAELLGVDPEELEKALTKRKIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 382 TATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKL 461
Cdd:smart00242 320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 462 QQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEK 540
Cdd:smart00242 400 QQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKpPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFSKP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 541 PRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkaispTSATSSGRtpltrtpakpt 620
Cdd:smart00242 480 KKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGV-----SNAGSKKR----------- 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 621 kgrpgqmakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSR 700
Cdd:smart00242 544 -----------FQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYR 612
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462544153 701 WTYQEFFSRYRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLR 762
Cdd:smart00242 613 LPFDEFLQRYRVLLPDTwpPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
7-1291 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 968.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 7 YTKFARVWIPDPEEVWKSAELLK-DYKPGDKVLLLHLEEGK--DLEYHLDPKTKelphlRNPDILVGENDLTALSYLHEP 83
Cdd:COG5022 6 AEVGSGCWIPDEEKGWIWAEIIKeAFNKGKVTEEGKKEDGEsvSVKKKVLGNDR-----IKLPKFDGVDDLTELSYLNEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:COG5022 81 AVLHNLEKRY-NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 164 ESGAGKTVSAKYAMRYFATVSGSASE--ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:COG5022 160 ESGAGKTENAKRIMQYLASVTSSSTVeiSSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 242 YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESH 321
Cdd:COG5022 240 YLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 322 QMGIFRILAGILHLGNVGFTSrDADSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARD 401
Cdd:COG5022 320 QDQIFKILAAILHIGNIEFKE-DRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 402 ALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQ 481
Cdd:COG5022 399 SLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 482 IPWTLIDFYDNQPCINLIESK--LGILDLLDEECKMPKGTDDTWAQKLYNT-HLNKCALFEKPRLSNKAFIIQHFADKVE 558
Cdd:COG5022 479 IEWSFIDYFDNQPCIDLIEKKnpLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNKFVVKHYAGDVE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 559 YQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKaisptsatssgrtpltrtpaKPTKGRPgqmakehkKTVGHQ 638
Cdd:COG5022 559 YDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEEN--------------------IESKGRF--------PTLGSR 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 639 FRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQK- 717
Cdd:COG5022 611 FKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKs 690
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 718 -----DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLRADKLRAACIRIQKTIRGWLLRKKYLRMRKA 792
Cdd:COG5022 691 wtgeyTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKR 770
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 793 AITMQRYVRGYQARCYAKFLRRTKAATIIQKYWRMYVVRRRYKIRRAATIVLQSYL-RGFLARNRYRKILREHKAVIIQK 871
Cdd:COG5022 771 IKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIkREKKLRETEEVEFSLKAEVLIQK 850
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 872 RVRGWLARTHYKRSMHAIIYLQCCFRRMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQ-NKDYKCLVEKL 950
Cdd:COG5022 851 FGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDlIENLEFKTELI 930
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 951 TNLEGIYNSETEKLRSDLERLQLSEeeakvatgrVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEE 1030
Cdd:COG5022 931 ARLKKLLNNIDLEEGPSIEYVKLPE---------LNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKEL 1001
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1031 NTLLKQ------EKEALNHRIVQQAKEMTETMEKKLVEETKQLELDLNDERlryQNLLNEFSRLEERYDDLKeemtlmvh 1104
Cdd:COG5022 1002 AELSKQygalqeSTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLK---GLLLLENNQLQARYKALK-------- 1070
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1105 VPKPGHKRTDSTHSSNESEYIFSSEI----AEMEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQ-----EKQVMQDE 1175
Cdd:COG5022 1071 LRRENSLLDDKQLYQLESTENLLKTInvkdLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQlvntlEPVFQKLS 1150
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1176 LDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQ---------ELESENKKLKNEL-NELRKALSEKSAPEVTAPGAPAY 1245
Cdd:COG5022 1151 VLQLELDGLFWEANLEALPSPPPFAALSEKRLYQsalydekskLSSSEVNDLKNELiALFSKIFSGWPRGDKLKKLISEG 1230
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462544153 1246 RVLMEQLTSVSEELDVRK----------EEVLILRSQLVSQKEAIQPKNTMTDSTI 1291
Cdd:COG5022 1231 WVPTEYSTSLKGFNNLNKkfdtpasmsnEKLLSLLNSIDNLLSSYKLEEEVLPATI 1286
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
83-751 |
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: 878.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMG-DMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd00124 1 AAILHNLRERY-ARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 162 SGESGAGKTVSAKYAMRYFATVSGSAS------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRII 235
Cdd:cd00124 80 SGESGAGKTETTKLVLKYLAALSGSGSskssssASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 236 GANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADN----FNYTKQGGSPVIEGVDDAKEMAHTRQA 311
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSyyylNDYLNSSGCDRIDGVDDAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 312 CTLLGISESHQMGIFRILAGILHLGNVGFTSR--DADSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIK 389
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDeeDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 390 PISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQH--SFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNM 467
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 468 HVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNK 546
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKpLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAKL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 547 AFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKfkmlpelfqddekaisptsatssgrtpltrtpakptkgrpgq 626
Cdd:cd00124 480 EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS------------------------------------------ 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 627 makehkktvghQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEF 706
Cdd:cd00124 518 -----------QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEF 586
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2462544153 707 FSRYRVLMKQKDVLSDR--KQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd00124 587 LKRYRILAPGATEKASDskKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
83-751 |
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: 796.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd01377 1 ASVLHNLRERY-YSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 163 GESGAGKTVSAKYAMRYFATVSGSA--------SEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRI 234
Cdd:cd01377 80 GESGAGKTENTKKVIQYLASVAASSkkkkesgkKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 235 IGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTL 314
Cdd:cd01377 160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 315 LGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKL 394
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 395 QATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 474
Cdd:cd01377 320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 475 EEYMKEQIPWTLIDF-YDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR--LSNKAFII 550
Cdd:cd01377 400 EEYKKEGIEWTFIDFgLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKpkKSEAHFIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 551 QHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLtrtpakptkgrpgqmake 630
Cdd:cd01377 480 KHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGGGKKKKKGGSF------------------ 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 631 hkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRY 710
Cdd:cd01377 542 --RTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRY 619
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 2462544153 711 RVLMKQ--KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01377 620 SILAPNaiPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
83-751 |
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: 762.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd01384 1 PGVLHNLKVRY-ELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 162 SGESGAGKTVSAKYAMRYFATVSGSAS--EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANM 239
Cdd:cd01384 80 SGESGAGKTETTKMLMQYLAYMGGRAVteGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 240 RTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISE 319
Cdd:cd01384 160 RTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 320 SHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEP---LCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQA 396
Cdd:cd01384 240 EEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSefhLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 397 TNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:cd01384 320 TLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 477 YMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNThLNKCALFEKPRLSNKAFIIQHFAD 555
Cdd:cd01384 400 YTKEEIDWSYIEFVDNQDVLDLIEKKpGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKPKLSRTDFTIDHYAG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELF--QDDEKAISPTSATSsgrtpltrtpakptkgrpgqmakehkk 633
Cdd:cd01384 479 DVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFppLPREGTSSSSKFSS--------------------------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 634 tVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVL 713
Cdd:cd01384 532 -IGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLL 610
|
650 660 670
....*....|....*....|....*....|....*....
gi 2462544153 714 MKQKDVLS-DRKQTCKNVLEKLILdkDKYQFGKTKIFFR 751
Cdd:cd01384 611 APEVLKGSdDEKAACKKILEKAGL--KGYQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
84-751 |
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: 753.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 84 AVLHNLRVRFIDsKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd01381 2 GILRNLLIRYRE-KLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 164 ESGAGKTVSAKYAMRYFATVSGSASEanVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYL 243
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHSW--IEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 244 LEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQM 323
Cdd:cd01381 159 LEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 324 GIFRILAGILHLGNVGFTSRDA---DSCTIpPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNAR 400
Cdd:cd01381 239 DIFKLLAAILHLGNIKFEATVVdnlDASEV-RDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 401 DALAKHIYAKLFNWIVDNVNQALHSAVKQHSF---IGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEY 477
Cdd:cd01381 318 DAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 478 MKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPR-LSNKAFIIQHFAD 555
Cdd:cd01381 398 DKEGINWQHIEFVDNQDVLDLIALKpMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNN-KNYLKPKsDLNTSFGINHFAG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkaisPTSATSSGRTPltrtpakptkgrpgqmakehkkTV 635
Cdd:cd01381 477 VVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDI----SMGSETRKKSP----------------------TL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK 715
Cdd:cd01381 531 SSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP 610
|
650 660 670
....*....|....*....|....*....|....*...
gi 2462544153 716 --QKDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01381 611 giPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
83-751 |
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: 731.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDmdPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd01383 1 PSVLHNLEYRY-SQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKLLDS--PHVYAVADTAYREMMRDEINQSIIIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 163 GESGAGKTVSAKYAMRYFATVSGSASeaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTY 242
Cdd:cd01383 78 GESGAGKTETAKIAMQYLAALGGGSS--GIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 243 LLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQ 322
Cdd:cd01383 156 LLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKEDQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 323 MGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDA 402
Cdd:cd01383 236 EHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 403 LAKHIYAKLFNWIVDNVNQALHSAVKQHS-FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQ 481
Cdd:cd01383 316 LAKAIYASLFDWLVEQINKSLEVGKRRTGrSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 482 IPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLyNTHLNKCALFEKPRlsNKAFIIQHFADKVEYQ 560
Cdd:cd01383 396 IDWTKVDFEDNQECLDLIEKKpLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCFKGER--GGAFTIRHYAGEVTYD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 561 CEGFLEKNKDTVFEEQIKVLKSSKFKmLPELFQddekaispTSATSSGRTPLTRTPAkptkGRPGQMakehKKTVGHQFR 640
Cdd:cd01383 473 TSGFLEKNRDLLHSDLIQLLSSCSCQ-LPQLFA--------SKMLDASRKALPLTKA----SGSDSQ----KQSVATKFK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 641 NSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLM-KQKDV 719
Cdd:cd01383 536 GQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLpEDVSA 615
|
650 660 670
....*....|....*....|....*....|..
gi 2462544153 720 LSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01383 616 SQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| Myo5a_CBD |
cd15478 |
Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, ... |
1476-1850 |
0e+00 |
|
Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. They interact with several adaptor proteins, in case of Myo5a-CBD, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin. Mutations in human Myo5a (many of which map to the cargo binding domain) lead to Griscelli syndrome, a severe neurological disease.
Pssm-ID: 271262 Cd Length: 375 Bit Score: 721.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1476 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 1555
Cdd:cd15478 1 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1556 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 1635
Cdd:cd15478 81 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1636 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIR 1715
Cdd:cd15478 161 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1716 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 1795
Cdd:cd15478 241 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2462544153 1796 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 1850
Cdd:cd15478 321 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 375
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
84-751 |
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: 718.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14883 2 GINTNLKVRY-KKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 164 ESGAGKTVSAKYAMRYFATVSGSASEanVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYL 243
Cdd:cd14883 81 ESGAGKTETTKLILQYLCAVTNNHSW--VEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 244 LEKSRVVFQAEEERNYHIFYQLCASAKL-PEFK-MLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESH 321
Cdd:cd14883 159 LEQSRITFQAPGERNYHVFYQLLAGAKHsKELKeKLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPEEM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 322 QMGIFRILAGILHLGNVGFTSRDADSCTIPPKH-EPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNAR 400
Cdd:cd14883 239 QEGIFSVLSAILHLGNLTFEDIDGETGALTVEDkEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 401 DALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKE 480
Cdd:cd14883 319 DAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 481 QIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKP--RLSNKAFIIQHFADKV 557
Cdd:cd14883 399 GINWSHIVFTDNQECLDLIEKPpLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPdrRRWKTEFGVKHYAGEV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 558 EYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQ-DDEKAISPTSATSSGRTPLTRTpakpTKGRPgqmakehkkTVG 636
Cdd:cd14883 478 TYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTyPDLLALTGLSISLGGDTTSRGT----SKGKP---------TVG 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 637 HQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQ 716
Cdd:cd14883 545 DTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPR 624
|
650 660 670
....*....|....*....|....*....|....*..
gi 2462544153 717 KDVLSDRKQ--TCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14883 625 ARSADHKETcgAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
84-751 |
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: 715.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd01378 2 AINENLKKRF-ENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 164 ESGAGKTVSAKYAMRYFATVSGSaSEANVE---EKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMR 240
Cdd:cd01378 81 ESGAGKTEASKRIMQYIAAVSGG-SESEVErvkDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHIT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 241 TYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISES 320
Cdd:cd01378 160 NYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 321 HQMGIFRILAGILHLGNVGFTSRDADSCTIPPKhEPLCIFCDLMGVDYEEMCHWLCHRKLATATE---TYIKPISKLQAT 397
Cdd:cd01378 240 EQDSIFRILAAILHLGNIQFAEDEEGNAAISDT-SVLDFVAYLLGVDPDQLEKALTHRTIETGGGgrsVYEVPLNVEQAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 398 NARDALAKHIYAKLFNWIVDNVNQALHSAVKQHS-FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:cd01378 319 YARDALAKAIYSRLFDWIVERINKSLAAKSGGKKkVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 477 YMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECK-MPKGTDDTWAQKLyNTHLNKCALFEKP----RLSNKAFII 550
Cdd:cd01378 399 YVREGIEWTPIKYFNNKIICDLIEEKpPGIFAILDDACLtAGDATDQTFLQKL-NQLFSNHPHFECPsghfELRRGEFRI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 551 QHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaisptsatssgrtpltrtPAKPTKGRPgqmake 630
Cdd:cd01378 478 KHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEG--------------------VDLDSKKRP------ 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 631 hkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRY 710
Cdd:cd01378 532 --PTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERY 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 2462544153 711 RVLMK----------QKDVLSDRKQTCknvlekliLDKDKYQFGKTKIFFR 751
Cdd:cd01378 610 KLLSPktwpawdgtwQGGVESILKDLN--------IPPEEYQMGKTKIFIR 652
|
|
| Myo5b_CBD |
cd15477 |
Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, ... |
1476-1847 |
0e+00 |
|
Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. They interact with several adaptor proteins, in case of Myo5b-CBD, Rab11-family interacting protein 2.
Pssm-ID: 271261 Cd Length: 372 Bit Score: 647.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1476 KEDEQKLVKNLILELKPRGVAVNlIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 1555
Cdd:cd15477 1 KEDEALLIRNLVTDLKPQAVSAT-VPCLPAYILYMCIRHADYINDDQKVHSLLTSTINGIKKVLKKHNDDFEMTSFWLAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1556 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 1635
Cdd:cd15477 80 TCRLLHCLKQYSGDEGFMTQNTAKQNEHCLKNFDLTEYRQVLSDLSIQIYQQLIKIAEGILQPMIVSAMLENESIQGLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1636 VKPTGLRKRTSSIAD-EGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQI 1714
Cdd:cd15477 160 VKPMGYRKRSSSMADgDNSYTLEALIRQLNTFHSIMCDQGLDPEIIQQVFKQLFYMINAVTLNNLLLRKDVCSWSTGMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1715 RYNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVS 1794
Cdd:cd15477 240 RYNISQLEEWLRGRNLHQSGAAQTMEPLIQAAQLLQLKKKTSEDAEAICSLCTALSTQQIVKILNLYTPLNEFEERVTVS 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2462544153 1795 FIRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFI 1847
Cdd:cd15477 320 FIRTIQAQLQERNDPPQLLLDTKHMFPVLFPFNPSALTLDSIHIPASLNLDFL 372
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
83-751 |
0e+00 |
|
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: 640.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14903 1 AAILYNVKKRFL-RKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 162 SGESGAGKTVSAKYAMRYFATVSGSASEANVEeKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:cd14903 80 SGESGAGKTETTKILMNHLATIAGGLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 242 YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEfkMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESH 321
Cdd:cd14903 159 YLLEKTRVISHERPERNYHIFYQLLASPDVEE--RLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 322 QMGIFRILAGILHLGNVGFTSRDAD--SCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNA 399
Cdd:cd14903 237 QEVLFEVLAGILHLGQLQIQSKPNDdeKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDC 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 400 RDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 479
Cdd:cd14903 317 RDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 480 EQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKAFIIQHFADKVEY 559
Cdd:cd14903 397 EGIRWAHIDFADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSRTQFTIKHYAGPVTY 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 560 QCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqdDEKAISPTSATSSGRTPltrtpakptkGRPGQMAKEHKKTVGHQF 639
Cdd:cd14903 477 ESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLF--KEKVESPAAASTSLARG----------ARRRRGGALTTTTVGTQF 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 640 RNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQK-D 718
Cdd:cd14903 545 KDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGrN 624
|
650 660 670
....*....|....*....|....*....|....
gi 2462544153 719 VLSDRKQTCKNVLEKLILDK-DKYQFGKTKIFFR 751
Cdd:cd14903 625 TDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
86-751 |
0e+00 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 627.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 86 LHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 164
Cdd:cd01382 4 LNNIRVRYSKDK-IYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 165 SGAGKTVSAKYAMRYFATVSGSASeANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 244
Cdd:cd01382 83 SGAGKTESTKYILRYLTESWGSGA-GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 245 EKSRVVFQAEEERNYHIFYQLCASAklPE---FKMLRLGNadnfnytkqggspviegVDDAKEMAHTRQACTLLGISESH 321
Cdd:cd01382 162 EKSRICVQSKEERNYHIFYRLCAGA--PEdlrEKLLKDPL-----------------LDDVGDFIRMDKAMKKIGLSDEE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 322 QMGIFRILAGILHLGNVGFTSRDADS---CTIPPKHEPLCIFC-DLMGVDYEEMCHWLCHRKLATATE----TYIK-PIS 392
Cdd:cd01382 223 KLDIFRVVAAVLHLGNIEFEENGSDSgggCNVKPKSEQSLEYAaELLGLDQDELRVSLTTRVMQTTRGgakgTVIKvPLK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 393 KLQATNARDALAKHIYAKLFNWIVDNVNQAL---HSAvkqhSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHV 469
Cdd:cd01382 303 VEEANNARDALAKAIYSKLFDHIVNRINQCIpfeTSS----YFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 470 FKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPRLS---- 544
Cdd:cd01382 379 LKEEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLvGILDLLDEESKLPKPSDQHFTSAVHQKHKNH-FRLSIPRKSklki 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 545 ------NKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAiSPTSATSSGRTPLtrtpak 618
Cdd:cd01382 458 hrnlrdDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNN-NKDSKQKAGKLSF------ 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 619 ptkgrpgqmakehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFP 698
Cdd:cd01382 531 --------------ISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFP 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 2462544153 699 SRWTYQEFFSRYRVLMKQKDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01382 597 SRTSFHDLYNMYKKYLPPKLARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
83-751 |
0e+00 |
|
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: 624.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14872 1 AMIVHNLRKRFKNDQ-IYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 163 GESGAGKTVSAKYAMRYFATVSGSASeaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTY 242
Cdd:cd14872 80 GESGAGKTEATKQCLSFFAEVAGSTN--GVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 243 LLEKSRVVFQAEEERNYHIFYQLCASAklPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQ 322
Cdd:cd14872 158 LLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFDDADI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 323 MGIFRILAGILHLGNVGFTS----RDADSCTIPPKHEpLCIFCDLMGVDYEEMCHWLCHRKLAT-ATETYIKPISKLQAT 397
Cdd:cd14872 236 NNVMSLIAAILKLGNIEFASgggkSLVSGSTVANRDV-LKEVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLTPAQAT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 398 NARDALAKHIYAKLFNWIVDNVNQALHSA-VKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:cd14872 315 DACDALAKAAYSRLFDWLVKKINESMRPQkGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEAL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 477 YMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTH-LNKCALFEKPRLSNKAFIIQHFA 554
Cdd:cd14872 395 YQSEGVKFEHIDFIDNQPVLDLIEKKQpGLMLALDDQVKIPKGSDATFMIAANQTHaAKSTFVYAEVRTSRTEFIVKHYA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 555 DKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkaisptsatssgrtpltrtPAKPTKgrpgqmakehKKT 634
Cdd:cd14872 475 GDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSE-------------------GDQKTS----------KVT 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 635 VGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLM 714
Cdd:cd14872 526 LGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLV 605
|
650 660 670
....*....|....*....|....*....|....*....
gi 2462544153 715 K--QKDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14872 606 KtiAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
86-751 |
0e+00 |
|
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: 618.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 86 LHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGES 165
Cdd:cd01385 4 LENLRARFKHGK-IYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 166 GAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLE 245
Cdd:cd01385 83 GSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 246 KSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQMGI 325
Cdd:cd01385 163 KSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQRQI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 326 FRILAGILHLGNVGFTSRDA---DSCTIPPKhEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDA 402
Cdd:cd01385 243 FSVLSAVLHLGNIEYKKKAYhrdESVTVGNP-EVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 403 LAKHIYAKLFNWIVDNVNQAL----HSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYM 478
Cdd:cd01385 322 MAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 479 KEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKlYNTHLNKCALFEKPRLSNKAFIIQHFADKV 557
Cdd:cd01385 402 KEGISWHNIEYTDNTGCLQLISKKpTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQVMEPAFIIAHYAGKV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 558 EYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAI-----------------SPTSATSSGRT-PLTRTPAKP 619
Cdd:cd01385 481 KYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVAVfrwavlrafframaafrEAGRRRAQRTAgHSLTLHDRT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 620 TKGRPGQMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPS 699
Cdd:cd01385 561 TKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSV 640
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2462544153 700 RWTYQEFFSRYRVLMKqKDVLSdRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01385 641 RYTFQEFITQFQVLLP-KGLIS-SKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| Myo5_CBD |
cd15470 |
Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, ... |
1477-1843 |
0e+00 |
|
Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. The MyoV-CBDs directly interact with several adaptor proteins, in case of Myo5a, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin, and in case of Myo5b, Rab11-family interacting protein 2.
Pssm-ID: 271254 [Multi-domain] Cd Length: 332 Bit Score: 615.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1477 EDEQKLVKNLILELKPRGvAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNT 1556
Cdd:cd15470 1 EDESRLIKNLITDLKPRG-AVGLLPGLPAYILFMCIRHADYVNDEAKVRSLLTATINAIKKVLKKHSEDFEMLSFWLVNT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1557 CRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmivsgmlehetiqgvsgv 1636
Cdd:cd15470 80 CRLLNCLKQYSGEEEFMKHNTPKQNEHCLKNFDLSEYRQVLSDLAIQIYQQLIKRAEEILQP------------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1637 kptglrkrtssiadegtyTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRY 1716
Cdd:cd15470 142 ------------------TLDSLLQQLNSFHTTLTQHGLDPELIKQVFRQLFYLICASTLNNLLLRKDLCSWSKGMQIRY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1717 NVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFI 1796
Cdd:cd15470 204 NVSQLEEWLRDKGLQDSGARETLEPLIQAAQLLQVKKTTEEDAQSICEMCTKLTTAQIVKILNLYTPVDDFEERVTPSFI 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2462544153 1797 RTIQMRLRDRKDSP--QLLMDAKHIFPVTFPFNPSSLALETIQIPASLG 1843
Cdd:cd15470 284 RKVQARLNERADSNqlQLLMDTKYIFPVTFPFNPSPVALEELQIPPSLH 332
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
84-751 |
0e+00 |
|
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: 604.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd01387 2 TVLWNLKTRY-ERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 164 ESGAGKTVSAKYAMRYFATVSGSAsEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMRTYL 243
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRR-NNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAITSQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 244 LEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQM 323
Cdd:cd01387 159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 324 GIFRILAGILHLGNVGFTSRDADSctippKHEPLCIFCD--------LMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd01387 239 SIFRILASVLHLGNVYFHKRQLRH-----GQEGVSVGSDaeiqwvahLLQISPEGLQKALTFKVTETRRERIFTPLTIDQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 396 ATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQE 475
Cdd:cd01387 314 ALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 476 EYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKL-YNTHLNKcaLFEKPRLSNKAFIIQHF 553
Cdd:cd01387 394 EYIREQIDWTEIAFADNQPVINLISKKpVGILHILDDECNFPQATDHSFLEKChYHHALNE--LYSKPRMPLPEFTIKHY 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 554 ADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaisptsatssgRTPLTRTPAKPTKGRPGQMaKEHKK 633
Cdd:cd01387 472 AGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSH-------------RAQTDKAPPRLGKGRFVTM-KPRTP 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 634 TVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVL 713
Cdd:cd01387 538 TVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 2462544153 714 MKQKDVLSDRKQTCKNVLEKL--ILDKDKYQFGKTKIFFR 751
Cdd:cd01387 618 VALKLPRPAPGDMCVSLLSRLctVTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
84-751 |
0e+00 |
|
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: 597.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMAR----DERNQS 158
Cdd:cd14890 2 SLLHTLRLRY-ERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 159 IIVSGESGAGKTVSAKYAMRYFATVS-----------------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFG 221
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITsgfaqgasgegeaaseaIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 222 KYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNA-DNFNYTKQGGSpvIEGVD 300
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPvEYFYLRGECSS--IPSCD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 301 DAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTS-RDADSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRK 379
Cdd:cd14890 239 DAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESeNDTTVLEDATTLQSLKLAAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 380 LATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANE 459
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 460 KLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL----GILDLLDeECKMPKGTDdtwAQKLYNTHLNkc 535
Cdd:cd14890 399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVngkpGIFITLD-DCWRFKGEE---ANKKFVSQLH-- 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 536 ALFEKPRLSNKA--------------------FIIQHFADKVEYQCEGFLEKNKDTVFEEqikvlksskfkmLPELFQDD 595
Cdd:cd14890 473 ASFGRKSGSGGTrrgssqhphfvhpkfdadkqFGIKHYAGDVIYDASGFNEKNNETLNAE------------MKELIKQS 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 596 EKAISPTSatssgrtpltrtpakptkgrpgqmakehkktVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEK 675
Cdd:cd14890 541 RRSIREVS-------------------------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGL 589
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462544153 676 RAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLsdrKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14890 590 DCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTAENI---EQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
84-751 |
0e+00 |
|
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: 593.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 84 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14873 2 SIMYNLFQRYKRNQ-IYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 163 GESGAGKTVSAKYAMRYFATVS-------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRII 235
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISqqslelsLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 236 GANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLL 315
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 316 GISESHQMGIFRILAGILHLGNVGFTSrdADSCTIPPKhEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEFIT--AGGAQVSFK-TALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 396 ATNARDALAKHIYAKLFNWIVDNVNQALHSAvKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQE 475
Cdd:cd14873 318 AVDSRDSLAMALYARCFEWVIKKINSRIKGK-EDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 476 EYMKEQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPRLSNKAFIIQHFAD 555
Cdd:cd14873 397 EYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANN-HFYVKPRVAVNNFGVKHYAG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaisptSATSSGRTPltrtpakptkgrpgQMAKEHKK-T 634
Cdd:cd14873 476 EVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHV-------SSRNNQDTL--------------KCGSKHRRpT 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 635 VGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLM 714
Cdd:cd14873 535 VSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLM 614
|
650 660 670
....*....|....*....|....*....|....*..
gi 2462544153 715 KQKDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14873 615 RNLALPEDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
83-749 |
0e+00 |
|
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: 587.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAY---SGQNMGD---MDPHIFAVAEEAYKQMARDER- 155
Cdd:cd14901 1 PSILHVLRRRF-AHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehGERRAAGerkLPPHVYAVADKAFRAMLFASRg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 156 ---NQSIIVSGESGAGKTVSAKYAMRYFATVS-------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIE 225
Cdd:cd14901 80 qkcDQSILVSGESGAGKTETTKIIMNYLASVSsatthgqNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 226 IGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPV-IEGVDDAKE 304
Cdd:cd14901 160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDrRDGVDDSVQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 305 MAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEP-LCIFCDLMGVDYEEMCHWLCHRKLATA 383
Cdd:cd14901 240 YAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLAnVRAACDLLGLDMDVLEKTLCTREIRAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 384 TETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQAL--HSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKL 461
Cdd:cd14901 320 GEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIaySESTGASRFIGIVDIFGFEIFATNSLEQLCINFANEKL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 462 QQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNThLNKCALFEK 540
Cdd:cd14901 400 QQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARpTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHASFSV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 541 PRLSN--KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPelfqddekaisptsatssgrtpltrtpak 618
Cdd:cd14901 479 SKLQQgkRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS----------------------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 619 ptkgrpgqmakehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFP 698
Cdd:cd14901 530 --------------STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYP 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462544153 699 SRWTYQEFFSRYRVLMKQK-------DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIF 749
Cdd:cd14901 596 VRFPHDAFVHTYSCLAPDGasdtwkvNELAERLMSQLQHSELNIEHLPPFQVGKTKVF 653
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
83-751 |
0e+00 |
|
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: 567.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSgQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14888 1 ASILHSLNLRF-DIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 162 SGESGAGKTVSAKYAMRYFATVsGSASE---ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDK-------- 230
Cdd:cd14888 79 SGESGAGKTESTKYVMKFLACA-GSEDIkkrSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskrmsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 231 -RYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCA-----------------------SAKLPEFKMLRLGNADNFN 286
Cdd:cd14888 158 dRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMSSFEPHLKFR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 287 YTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGF-TSRDADSCTI--PPKHEPLCIFCDL 363
Cdd:cd14888 238 YLTKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFeNNEACSEGAVvsASCTDDLEKVASL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 364 MGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQAL-HSAVKQHSFIGVLDIYGFE 442
Cdd:cd14888 318 LGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIgYSKDNSLLFCGVLDIFGFE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 443 TFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDD 521
Cdd:cd14888 398 CFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKpLGIFCMLDEECFVPGGKDQ 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 522 TWAQKLYNTHLNKcALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQddekaisp 601
Cdd:cd14888 478 GLCNKLCQKHKGH-KRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFS-------- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 602 tsatssgrtpltrtpAKPTKGRPGQMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQL 681
Cdd:cd14888 549 ---------------AYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQL 613
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 682 RACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkqkdvlsdRKQTCKNVLEklildkdkYQFGKTKIFFR 751
Cdd:cd14888 614 KYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILL--------NGEGKKQLSI--------WAVGKTLCFFK 667
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
83-751 |
0e+00 |
|
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: 562.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFIDSkLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd01379 1 DTIVSQLQKRYSRD-QIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 163 GESGAGKTVSAKYAMRYFaTVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTY 242
Cdd:cd01379 80 GESGAGKTESANLLVQQL-TVLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 243 LLEKSRVVFQAEEERNYHIFYQLCA----SAKLPEFKmlrLGNADNFNYTKQGGspviEGVDDAKEMAHTR------QAC 312
Cdd:cd01379 159 LLEKSRVVHQAIGERNFHIFYYIYAglaeDKKLAKYK---LPENKPPRYLQNDG----LTVQDIVNNSGNRekfeeiEQC 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 313 -TLLGISESHQMGIFRILAGILHLGNVGFTS-----RDADSCTIpPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATET 386
Cdd:cd01379 232 fKVIGFTKEEVDSVYSILAAILHIGDIEFTEvesnhQTDKSSRI-SNPEALNNVAKLLGIEADELQEALTSHSVVTRGET 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 387 YIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQAL----HSAVKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQ 462
Cdd:cd01379 311 IIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpdrSASDEPLS-IGILDIFGFENFQKNSFEQLCINIANEQIQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 463 QQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNthlN-KCALFEK 540
Cdd:cd01379 390 YYFNQHIFAWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKpMGLLALLDEESRFPKATDQTLVEKFHN---NiKSKYYWR 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 541 PRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLpelfqddekaisptsatssgrtpltrtpakpt 620
Cdd:cd01379 467 PKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV-------------------------------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 621 kgrpgqmakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSR 700
Cdd:cd01379 515 -----------RQTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHR 583
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 2462544153 701 WTYQEFFSRYRVL---MKQKDVLSdrKQTCKNVLEKLILdkDKYQFGKTKIFFR 751
Cdd:cd01379 584 ILFADFLKRYYFLafkWNEEVVAN--RENCRLILERLKL--DNWALGKTKVFLK 633
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
89-751 |
6.27e-180 |
|
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: 558.99 E-value: 6.27e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 89 LRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGE--DIINAYSGQNMGDMD-PHIFAVAEEAYKQMARD----ERNQSIIV 161
Cdd:cd14892 7 LRRRY-ERDAIYTFTADILISINPYKSIPLLYDvpGFDSQRKEEATASSPpPHVFSIAERAYRAMKGVgkgqGTPQSIVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 162 SGESGAGKTVSAKYAMRYFATVSGSASEA-----------NVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDK 230
Cdd:cd14892 86 SGESGAGKTEASKYIMKYLATASKLAKGAstskgaanaheSIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 231 RYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQ 310
Cdd:cd14892 166 DGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVDGVDDATEFKQLRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 311 ACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEP--LCIFCDLMGVDYEEMCHWLCHRKLATATETYI 388
Cdd:cd14892 246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGvnVAKAAGLLGVDAAELMFKLVTQTTSTARGSVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 389 K-PISKLQATNARDALAKHIYAKLFNWIVDNVNqALHSAV-----------KQHSFIGVLDIYGFETFEINSFEQFCINY 456
Cdd:cd14892 326 EiKLTAREAKNALDALCKYLYGELFDWLISRIN-ACHKQQtsgvtggaaspTFSPFIGILDIFGFEIMPTNSFEQLCINF 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 457 ANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMP-KGTDDTWAQKLYNTHLNK 534
Cdd:cd14892 405 TNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKpLGLLPLLEEQMLLKrKTTDKQLLTIYHQTHLDK 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 535 CALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKfkmlpelfqddekaisptsatssgrtpltr 614
Cdd:cd14892 485 HPHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS------------------------------ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 615 tpakptkgrpgqmakehkktvghQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISA 694
Cdd:cd14892 535 -----------------------KFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRR 591
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462544153 695 AGFPSRWTYQEFFSRYRVLMKQKDVLSDRKQTCKNVLE--------KLILDKDKYQFGKTKIFFR 751
Cdd:cd14892 592 EGFPIRRQFEEFYEKFWPLARNKAGVAASPDACDATTArkkceeivARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
83-751 |
2.08e-179 |
|
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: 557.67 E-value: 2.08e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14929 1 ASVLHTLRRRY-DHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 163 GESGAGKTVSAKYAMRYFATVSGSASE----ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGAN 238
Cdd:cd14929 80 GESGAGKTVNTKHIIQYFATIAAMIESkkklGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 239 MRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPViEGVDDAKEMAHTRQACTLLGIS 318
Cdd:cd14929 160 IDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAV-ESLDDAEELLATEQAMDILGFL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 319 ESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATN 398
Cdd:cd14929 239 PDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVTY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 399 ARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYM 478
Cdd:cd14929 319 AVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEYR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 479 KEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKAFIIQ----HF 553
Cdd:cd14929 399 KEGIDWVSIDFgLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHfelvHY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 554 ADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaISPTSATSSGRtpltrtpakptkgrpgqmaKEHKK 633
Cdd:cd14929 479 AGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENY---ISTDSAIQFGE-------------------KKRKK 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 634 TVGHQFRNSLH-----LLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 708
Cdd:cd14929 537 GASFQTVASLHkenlnKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQ 616
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2462544153 709 RY-----RVLMKQKDVlSDRKQTcKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14929 617 RYcilnpRTFPKSKFV-SSRKAA-EELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
83-751 |
1.41e-178 |
|
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: 555.82 E-value: 1.41e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14913 1 PAVLYNLKDRY-TSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 163 GESGAGKTVSAKYAMRYFATVSG---------SASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14913 80 GESGAGKTVNTKRVIQYFATIAAtgdlakkkdSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG-NADNFNYTKQGgSPVIEGVDDAKEMAHTRQAC 312
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITtNPYDYPFISQG-EILVASIDDAEELLATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 313 TLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPIS 392
Cdd:cd14913 239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 393 KLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKL 472
Cdd:cd14913 319 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 473 EQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR-LSNKA--- 547
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKvVKGRAeah 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 548 FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaisPTSATSSGrtPLTRTPAKPTKGRPGQm 627
Cdd:cd14913 479 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY--------ATFATADA--DSGKKKVAKKKGSSFQ- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 628 akehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFF 707
Cdd:cd14913 548 ------TVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFK 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2462544153 708 SRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14913 622 QRYRVLNASaipEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
83-751 |
5.98e-176 |
|
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: 548.00 E-value: 5.98e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14904 1 PSILFNLKKRFAASK-PYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 162 SGESGAGKTVSAKYAMRYFATVSGSASEANVEeKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:cd14904 80 SGESGAGKTETTKIVMNHLASVAGGRKDKTIA-KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 242 YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQG-GSPVIEGVDDAKEMAHTRQACTLLGISES 320
Cdd:cd14904 159 YLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSlAQMQIPGLDDAKLFASTQKSLSLIGLDND 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 321 HQMGIFRILAGILHLGNVGFTSRDADSCTIPpKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNAR 400
Cdd:cd14904 239 AQRTLFKILSGVLHLGEVMFDKSDENGSRIS-NGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEENR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 401 DALAKHIYAKLFNWIVDNVNQAL---HSAVKQHsfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEY 477
Cdd:cd14904 318 DALAKAIYSKLFDWMVVKINAAIstdDDRIKGQ--IGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 478 MKEQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHL----NKCALFekPRLSNKAFIIQHF 553
Cdd:cd14904 396 IREGLQWDHIEYQDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQtkkdNESIDF--PKVKRTQFIINHY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 554 ADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkAISPTSATSSGRtpltrtpakptkgrpgqmAKEHKK 633
Cdd:cd14904 474 AGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE-APSETKEGKSGK------------------GTKAPK 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 634 TVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVL 713
Cdd:cd14904 535 SLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIM 614
|
650 660 670
....*....|....*....|....*....|....*....
gi 2462544153 714 MKQKDVLSDRKQTCKNVLEKLILDKD-KYQFGKTKIFFR 751
Cdd:cd14904 615 FPPSMHSKDVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
84-751 |
2.29e-175 |
|
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: 547.25 E-value: 2.29e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14927 2 SVLHNLRRRY-SRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 164 ESGAGKTVSAKYAMRYFATVS-------------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDK 230
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAalgdgpgkkaqflATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 231 RYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKlPEFK--MLRLGNADNFNYTKQGGSPViEGVDDAKEMAHT 308
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKK-PELQdmLLVSMNPYDYHFCSQGVTTV-DNMDDGEELMAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 309 RQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYI 388
Cdd:cd14927 239 DHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 389 KPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMH 468
Cdd:cd14927 319 KGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 469 VFKLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKA 547
Cdd:cd14927 399 MFILEQEEYKREGIEWVFIDFgLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 548 -----FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddEKAISPTSATSsgrtPLTRTPAKPTKG 622
Cdd:cd14927 479 kyeahFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY---ENYVGSDSTED----PKSGVKEKRKKA 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 623 RPGQmakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWT 702
Cdd:cd14927 552 ASFQ-------TVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRIL 624
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2462544153 703 YQEFFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14927 625 YADFKQRYRILNPSaipDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
84-751 |
3.03e-173 |
|
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: 541.52 E-value: 3.03e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14920 2 SVLHNLKDRYY-SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 164 ESGAGKTVSAKYAMRYFATVSGS-------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIG 236
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASShkgrkdhNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 237 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPvIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIP-IPGQQDKDNFQETMEAMHIMG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 317 ISESHQMGIFRILAGILHLGNVGF-TSRDADSCTIpPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14920 240 FSHEEILSMLKVVSSVLQFGNISFkKERNTDQASM-PENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 396 ATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 474
Cdd:cd14920 319 ADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 475 EEYMKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKA-FI 549
Cdd:cd14920 399 EEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAdFC 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 550 IQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKaISPTSATSSGRTPLTRTPAKPTKGRpgqmak 629
Cdd:cd14920 479 IIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDR-IVGLDQVTGMTETAFGSAYKTKKGM------ 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 630 ehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSR 709
Cdd:cd14920 552 --FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2462544153 710 YRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14920 630 YEILTPNAipKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
85-751 |
1.62e-170 |
|
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: 533.84 E-value: 1.62e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 85 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP---------IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDER 155
Cdd:cd14907 3 LLINLKKRYQQDK-IFTYVGPTLIVMNPYKQIDnlfseevmqMYKEQIIQNGEYFDIKKEPPHIYAIAALAFKQLFENNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 156 NQSIIVSGESGAGKTVSAKYAMRYFATVSG------------------SASEANVEEKVLASNPIMESIGNAKTTRNDNS 217
Cdd:cd14907 82 KQAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevltltssiratSKSTKSIEQKILSCNPILEAFGNAKTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 218 SRFGKYIEIGFDKRYR-IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAK---LPEFKMLRLGNADNFNYTKQGGS 293
Cdd:cd14907 162 SRFGKYVSILVDKKKRkILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADqqlLQQLGLKNQLSGDRYDYLKKSNC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 294 PVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSR--DADSCTIPPKHEPLCIFCDLMGVDYEEM 371
Cdd:cd14907 242 YEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDStlDDNSPCCVKNKETLQIIAKLLGIDEEEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 372 CHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQAL--HSAVKQHSF------IGVLDIYGFET 443
Cdd:cd14907 322 KEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpKDEKDQQLFqnkylsIGLLDIFGFEV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 444 FEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTL--IDFYDNQPCINLIES-KLGILDLLDEECKMPKGTD 520
Cdd:cd14907 402 FQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSYTDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 521 DTWAQKLYNTHLNKCALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAis 600
Cdd:cd14907 482 EKLLNKIKKQHKNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGEDGS-- 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 601 ptsaTSSGRTPLTRTPAKptkgrpgqmakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQ 680
Cdd:cd14907 560 ----QQQNQSKQKKSQKK-------------DKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQ 622
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462544153 681 LRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkqkdvlsdrkqtcKNVLeklildkdkyqFGKTKIFFR 751
Cdd:cd14907 623 IRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLK-------------KNVL-----------FGKTKIFMK 669
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
83-751 |
2.53e-170 |
|
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: 533.26 E-value: 2.53e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14909 1 ASVLHNLRQRYY-AKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 163 GESGAGKTVSAKYAMRYFATVSGS-------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRII 235
Cdd:cd14909 80 GESGAGKTENTKKVIAYFATVGASkktdeaaKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 236 GANMRTYLLEKSRVVFQAEEERNYHIFYQLcASAKLPEFKMLRL--GNADNFNYTKQGGSpVIEGVDDAKEMAHTRQACT 313
Cdd:cd14909 160 GADIETYLLEKARVISQQSLERSYHIFYQI-MSGSVPGVKEMCLlsDNIYDYYIVSQGKV-TVPNVDDGEEFSLTDQAFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 314 LLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISK 393
Cdd:cd14909 238 ILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 394 LQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLE 473
Cdd:cd14909 318 QQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 474 QEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKA----- 547
Cdd:cd14909 398 QEEYKREGIDWAFIDFgMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGqqaah 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 548 FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTpltrtpakpTKGrpGQM 627
Cdd:cd14909 478 FAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRG---------KKG--GGF 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 628 AkehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFF 707
Cdd:cd14909 547 A-----TVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFK 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2462544153 708 SRYRVLM-KQKDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14909 622 MRYKILNpAGIQGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| Myo5c_CBD |
cd15476 |
Cargo binding domain of myosin 5C; Class V myosins are well studied unconventional myosins, ... |
1477-1844 |
3.41e-169 |
|
Cargo binding domain of myosin 5C; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. The MyoV-CBDs directly interact with several adaptor proteins.MyoVb and myoVc areprimarily expressed in epithelial cells, and have been implicated as motors involved in recycling endosomes.
Pssm-ID: 271260 [Multi-domain] Cd Length: 332 Bit Score: 517.03 E-value: 3.41e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1477 EDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNT 1556
Cdd:cd15476 1 EDEAKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRHADYLNDANKLKSLMNAIITGVKQVIKEHQEDFEMLSFWLSNT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1557 CRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmivsgmlehetiqgvsgv 1636
Cdd:cd15476 81 YHFLNCLKQYSGEEEFMKHNTPRQNKNCLKNFDLSEHRQILSDLAIRIYHQFISVMENNLQP------------------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1637 kptglrkrtssiadegtyTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRY 1716
Cdd:cd15476 143 ------------------TISSILQQLSYFYSTMCQHGMDPELIKQAVKQLFFLIGAVTLNSIFLRKDMCSCRKGMQIRC 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1717 NVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFI 1796
Cdd:cd15476 205 NISYLEEWLKEKNLQNSNAKETLEPLSQAAWLLQVNKTTDDDAKEICERCTELSAVQIVKILNSYTPIDDFEKRVTPSFV 284
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2462544153 1797 RTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGL 1844
Cdd:cd15476 285 RKVQSLLQNREGSSQLMLDTKYRFQVTFPFCPSPQALEMLQVPSSLKL 332
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
84-751 |
8.03e-167 |
|
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: 524.16 E-value: 8.03e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14911 2 SVLHNIKDRYY-SGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 164 ESGAGKTVSAKYAMRYFATVSGSASEAN----------------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIG 227
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASKPKGSgavphpavnpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 228 FDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPViEGVDDAKEMAH 307
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPV-PGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 308 TRQACTLLGISESHQMGIFRILAGILHLGNVGF-TSRDADSCTIPPKHEPLCIfCDLMGVDYEEMCHWLCHRKLATATET 386
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFrQERNNDQATLPDNTVAQKI-AHLLGLSVTDMTRAFLTPRIKVGRDF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 387 YIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQF 465
Cdd:cd14911 319 VTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 466 NMHVFKLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKPRLS 544
Cdd:cd14911 399 NHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFMKTDFR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 545 NKA-FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSgrtplTRTPAKPTKGR 623
Cdd:cd14911 478 GVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTD-----TQFGARTRKGM 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 624 pgqmakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTY 703
Cdd:cd14911 553 --------FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPF 624
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 2462544153 704 QEFFSRYRVLMKQ--KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14911 625 QEFRQRYELLTPNviPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
83-751 |
2.30e-166 |
|
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: 523.32 E-value: 2.30e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAY------SGQNM---GDMDPHIFAVAEEAYKQMARD 153
Cdd:cd14908 1 PAILHSLSRRF-FRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYrqegllRSQGIespQALGPHVFAIADRSYRQMMSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 154 ER-NQSIIVSGESGAGKTVSAKYAMRYFATV----------SGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGK 222
Cdd:cd14908 80 IRaSQSILISGESGAGKTESTKIVMLYLTTLgngeegapneGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 223 YIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASA--------KLPEFKMLRLGNADNFNYTKQGGSP 294
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGdeeehekyEFHDGITGGLQLPNEFHYTGQGGAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 295 VIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPK---HEPLCIFCDLMGVDYEEM 371
Cdd:cd14908 240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEegnEKCLARVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 372 CHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ--HSFIGVLDIYGFETFEINSF 449
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKdiRSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 450 EQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIES-KLGILDLLDEECKMP-KGTDDTWAQKL 527
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAkKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 528 YNTHLNKC--ALFEKPRLSNKA-------FIIQHFADKVEYQCE-GFLEKNKDtvfeeqiKVLKSSKfkmlpELFQDdek 597
Cdd:cd14908 480 YETYLPEKnqTHSENTRFEATSiqktkliFAVRHFAGQVQYTVEtTFCEKNKD-------EIPLTAD-----SLFES--- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 598 aisptsatssgrtpltrtpakptkgrpgqmakehkktvGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRA 677
Cdd:cd14908 545 --------------------------------------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRV 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 678 VQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK--QKDVLS------DRKQTCKNVLEKLI-------------- 735
Cdd:cd14908 587 TEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPliPEVVLSwsmerlDPQKLCVKKMCKDLvkgvlspamvsmkn 666
|
730
....*....|....*.
gi 2462544153 736 LDKDKYQFGKTKIFFR 751
Cdd:cd14908 667 IPEDTMQLGKSKVFMR 682
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
83-751 |
2.89e-164 |
|
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: 517.35 E-value: 2.89e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14917 1 PAVLYNLKERY-ASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 163 GESGAGKTVSAKYAMRYFATVSG---------SASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14917 80 GESGAGKTVNTKRVIQYFAVIAAigdrskkdqTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRL-GNADNFNYTKQGGSPViEGVDDAKEMAHTRQAC 312
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGETTV-ASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 313 TLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPIS 392
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 393 KLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKL 472
Cdd:cd14917 319 VQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 473 EQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR-LSNKA--- 547
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRnIKGKPeah 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 548 FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekaisptsaTSSGRTPLTRTPAKPTKGRPGQm 627
Cdd:cd14917 479 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN----------YAGADAPIEKGKGKAKKGSSFQ- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 628 akehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFF 707
Cdd:cd14917 548 ------TVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFR 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2462544153 708 SRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14917 622 QRYRILNPAaipEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
83-751 |
6.37e-162 |
|
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: 510.76 E-value: 6.37e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14916 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 163 GESGAGKTVSAKYAMRYFATVSG----------SASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd14916 80 GESGAGKTVNTKRVIQYFASIAAigdrskkenpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRL-GNADNFNYTKQGgSPVIEGVDDAKEMAHTRQA 311
Cdd:cd14916 160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVSQG-EVSVASIDDSEELLATDSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 312 CTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPI 391
Cdd:cd14916 239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 392 SKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFK 471
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 472 LEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR----LSNK 546
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRnvkgKQEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 547 AFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAisptSATSSGrtpltrtpakptKGRPGQ 626
Cdd:cd14916 479 HFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASA----DTGDSG------------KGKGGK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 627 MAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEF 706
Cdd:cd14916 543 KKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2462544153 707 FSRYRVL----MKQKDVLSDRKQTCKnVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14916 623 RQRYRILnpaaIPEGQFIDSRKGAEK-LLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
84-751 |
3.58e-161 |
|
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: 508.41 E-value: 3.58e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 84 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14934 2 SVLDNLRQRYTNMR-IYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 164 ESGAGKTVSAKYAMRYFATVSGSASEA-----NVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGAN 238
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSsdgkgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 239 MRTYLLEKSRVVFQAEEERNYHIFYQLCASAKlPEF--KMLRLGNADNFNYTKQGGSpVIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14934 161 IESYLLEKSRVISQQAAERGYHIFYQILSNKK-PELieSLLLVPNPKEYHWVSQGVT-VVDNMDDGEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 317 ISESHQMGIFRILAGILHLGNVGFTSR------DADSCTIPPKheplciFCDLMGVDYEEMCHWLCHRKLATATETYIKP 390
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFGNMKFKQKpreeqaEVDTTEVADK------VAHLMGLNSGELQKGITRPRVKVGNEFVQKG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 391 ISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14934 313 QNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKP-----RLS 544
Cdd:cd14934 393 VLEQEEYKREGIEWVFIDFgLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPkggkgKGP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 545 NKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFkMLPELFQDDEKAISPTSATSSGRTPLtrtpakptkgrp 624
Cdd:cd14934 473 EAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSL-GLLALLFKEEEAPAGSKKQKRGSSFM------------ 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 625 gqmakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQ 704
Cdd:cd14934 540 ---------TVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYP 610
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 2462544153 705 EFFSRYRVLmkQKDVLS----DRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14934 611 EFKQRYQVL--NPNVIPqgfvDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
83-751 |
1.54e-159 |
|
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: 504.65 E-value: 1.54e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14912 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 163 GESGAGKTVSAKYAMRYFATVSGSAS-----------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR 231
Cdd:cd14912 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 232 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG-NADNFNYTKQGGSPViEGVDDAKEMAHTRQ 310
Cdd:cd14912 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITtNPYDYPFVSQGEISV-ASIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 311 ACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKP 390
Cdd:cd14912 239 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 391 ISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14912 319 QTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRL----SN 545
Cdd:cd14912 399 VLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVvkgkAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 546 KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSgrtpltrtpakpTKGrpG 625
Cdd:cd14912 479 AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGA------------KKG--G 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 626 QMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14912 545 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2462544153 706 FFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14912 625 FKQRYKVLNASaipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
85-751 |
2.18e-159 |
|
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: 503.67 E-value: 2.18e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 85 VLHNLRVRFIDSkLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQM----ARDERNQSII 160
Cdd:cd14889 3 LLEVLKVRFMQS-NIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMlgrlARGPKNQCIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 161 VSGESGAGKTVSAKYAMRYFATVSGSASEanVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMR 240
Cdd:cd14889 82 ISGESGAGKTESTKLLLRQIMELCRGNSQ--LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 241 TYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISES 320
Cdd:cd14889 159 EYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYDEVCNAMDMVGFTEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 321 HQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHE-PLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNA 399
Cdd:cd14889 239 EEVDMFTILAGILSLGNITFEMDDDEALKVENDSNgWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAEDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 400 RDALAKHIYAKLFNWIVDNVNQALHSAVK---QHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:cd14889 319 RDSIAKVAYGRVFGWIVSKINQLLAPKDDssvELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLMEQKE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 477 YMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLyNTHLNKCALFEKPRLSNKAFIIQHFAD 555
Cdd:cd14889 399 YKKEGIDWKEITYKDNKPILDLFLNKpIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYGKSRSKSPKFTVNHYAG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaisptsATSSGRTPLTRTPAKPTKGRPGQMAKEHKKTV 635
Cdd:cd14889 478 KVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLF-----------TATRSRTGTLMPRAKLPQAGSDNFNSTRKQSV 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK 715
Cdd:cd14889 547 GAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILLC 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 2462544153 716 QKDvLSDRKQTCKNVLEKliLDKDKYQFGKTKIFFR 751
Cdd:cd14889 627 EPA-LPGTKQSCLRILKA--TKLVGWKCGKTRLFFK 659
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
83-751 |
4.33e-159 |
|
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: 503.45 E-value: 4.33e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14923 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 163 GESGAGKTVSAKYAMRYFATVS----------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd14923 80 GESGAGKTVNTKRVIQYFATIAvtgdkkkeqqPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKlPEFKMLRL--GNADNFNYTKQGgSPVIEGVDDAKEMAHTRQ 310
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKK-PELIDLLLisTNPFDFPFVSQG-EVTVASIDDSEELLATDN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 311 ACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKP 390
Cdd:cd14923 238 AIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 391 ISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14923 318 QNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR-LSNKA- 547
Cdd:cd14923 398 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKpAKGKAe 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 548 --FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaiSPTSATSSGRTPLTRTPAKpTKGRPG 625
Cdd:cd14923 478 ahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLF-------SNYAGAEAGDSGGSKKGGK-KKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 626 QmakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14923 550 Q-------TVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYAD 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2462544153 706 FFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14923 623 FKQRYRILNASaipEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
83-751 |
1.51e-158 |
|
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: 501.57 E-value: 1.51e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14918 1 PGVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 163 GESGAGKTVSAKYAMRYFATVSGSAS---------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14918 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG-NADNFNYTKQGgSPVIEGVDDAKEMAHTRQAC 312
Cdd:cd14918 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITtNPYDYAFVSQG-EITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 313 TLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPIS 392
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 393 KLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKL 472
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 473 EQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRL----SNKA 547
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVvkgkAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 548 FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRtpltrtpakpTKGRPGQm 627
Cdd:cd14918 479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAK----------KKGSSFQ- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 628 akehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFF 707
Cdd:cd14918 548 ------TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFK 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2462544153 708 SRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14918 622 QRYKVLNASaipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
85-751 |
2.76e-158 |
|
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: 499.60 E-value: 2.76e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 85 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDM-DPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14897 3 IVQTLKSRYNKDK-FYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVRSQrPPHLFWIADQAYRRLLETGRNQCILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 164 ESGAGKTVSAKYAMRYFATVSGSASEaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYL 243
Cdd:cd14897 82 ESGAGKTESTKYMIKHLMKLSPSDDS-DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 244 LEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNyTKQGGSPVIEGVDDAKEMAHTRQACT-------LLG 316
Cdd:cd14897 161 LEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHR-ILRDDNRNRPVFNDSEELEYYRQMFHdltnimkLIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 317 ISESHQMGIFRILAGILHLGNVGF-TSRDADSCTIPPKHePLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14897 240 FSEEDISVIFTILAAILHLTNIVFiPDEDTDGVTVADEY-PLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 396 ATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQH-----SFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14897 319 ANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQimtrgPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 471 KLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLyNTHLNKCALFEKPRLSNKAFI 549
Cdd:cd14897 399 PRERSEYEIEGIEWRDIEYHDNDDVLELFFKKpLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESPRYVASPGNRVAFG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 550 IQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaispTSatssgrtpltrtpakptkgrpgqmak 629
Cdd:cd14897 478 IRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF---------TS-------------------------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 630 ehkktvghQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSR 709
Cdd:cd14897 523 --------YFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKR 594
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 2462544153 710 YRVLM-KQKDVLSDRKQTCKNVLEklILDKDKYQFGKTKIFFR 751
Cdd:cd14897 595 YKEICdFSNKVRSDDLGKCQKILK--TAGIKGYQFGKTKVFLK 635
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
83-751 |
7.29e-157 |
|
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: 497.33 E-value: 7.29e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14910 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 163 GESGAGKTVSAKYAMRYFATVSGSAS-----------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR 231
Cdd:cd14910 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 232 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG-NADNFNYTKQGgSPVIEGVDDAKEMAHTRQ 310
Cdd:cd14910 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITtNPYDYAFVSQG-EITVPSIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 311 ACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKP 390
Cdd:cd14910 239 AIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 391 ISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14910 319 QTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKA-- 547
Cdd:cd14910 399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKve 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 548 --FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaisptsatsSGRTPLTRTPAKPTKGrpG 625
Cdd:cd14910 479 ahFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLF--------------SGAAAAEAEEGGGKKG--G 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 626 QMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14910 543 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2462544153 706 FFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14910 623 FKQRYKVLNASaipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
83-751 |
2.74e-156 |
|
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: 495.79 E-value: 2.74e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14915 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 163 GESGAGKTVSAKYAMRYFATVSGSAS-----------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR 231
Cdd:cd14915 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeaasgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 232 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG-NADNFNYTKQGgSPVIEGVDDAKEMAHTRQ 310
Cdd:cd14915 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITtNPYDFAFVSQG-EITVPSIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 311 ACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKP 390
Cdd:cd14915 239 AVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 391 ISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14915 319 QTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSN-KA- 547
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKgKAe 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 548 --FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGrtpltrtpakptkgrpG 625
Cdd:cd14915 479 ahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGGGKKG----------------G 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 626 QMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14915 543 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2462544153 706 FFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14915 623 FKQRYKVLNASaipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
84-751 |
3.48e-156 |
|
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: 495.70 E-value: 3.48e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14932 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 164 ESGAGKTVSAKYAMRYFATVSGSA-----------SEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQgGSPVIEGVDDAKEMAHTRQAC 312
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSN-GNVTIPGQQDKELFAETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 313 TLLGISESHQMGIFRILAGILHLGNVGF-TSRDADSCTIPPKHEPLCIfCDLMGVDYEEMCHWLCHRKLATATETYIKPI 391
Cdd:cd14932 240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFkKERNSDQASMPDDTAAQKV-CHLLGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 392 SKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14932 319 TQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKP-RLSN 545
Cdd:cd14932 399 ILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQGNN-PKFQKPkKLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 546 KA-FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSsgrtpLTRTPAKPTKGRP 624
Cdd:cd14932 478 DAdFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAG-----MGESLHGAFKTRK 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 625 GQMakehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQ 704
Cdd:cd14932 553 GMF-----RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2462544153 705 EFFSRYRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14932 628 EFRQRYEILTPNAipKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
84-751 |
5.36e-156 |
|
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: 494.92 E-value: 5.36e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14921 2 SVLHNLRERYF-SGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 164 ESGAGKTVSAKYAMRYFATVSGS-------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIG 236
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASShkgkkdtSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 237 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPvIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVP-IPAAQDDEMFQETLEAMSIMG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 317 ISESHQMGIFRILAGILHLGNVGF-TSRDADSCTIPPKHEPLCIfCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14921 240 FSEEEQLSILKVVSSVLQLGNIVFkKERNTDQASMPDNTAAQKV-CHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 396 ATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 474
Cdd:cd14921 319 ADFAIEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 475 EEYMKEQIPWTLIDF-YDNQPCINLIE---SKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPR-LSNKA-F 548
Cdd:cd14921 399 EEYQREGIEWNFIDFgLDLQPCIELIErpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNH-PKFQKPKqLKDKTeF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 549 IIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLTrTPAKPTKGRpgqma 628
Cdd:cd14921 478 SIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLP-SASKTKKGM----- 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 629 kehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 708
Cdd:cd14921 552 ---FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2462544153 709 RYRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14921 629 RYEILAANAipKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
83-751 |
5.84e-155 |
|
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: 491.10 E-value: 5.84e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRF-IDSKLIYTYCGIVLVAINPYEQLPiygEDIINAYSGQNMGDMDPHIFAVAEEAYKQM---ARDERNQS 158
Cdd:cd14891 1 AGILHNLEERSkLDNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMclgSGRMQNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 159 IIVSGESGAGKTVSAKYAMRYFATVS-----------------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFG 221
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAvggkkasgqdieqsskkRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 222 KYIEIGFDKR-YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVD 300
Cdd:cd14891 158 KFMKLQFTKDkFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 301 DAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRD-----ADSCTIPPKhEPLCIFCDLMGVDYEEMCHWL 375
Cdd:cd14891 238 DAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDtsegeAEIASESDK-EALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 376 CHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEI-NSFEQFCI 454
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFETkNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 455 NYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTHL- 532
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPnGILPLLDNEARNPNPSDAKLNETLHKTHKr 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 533 NKCALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVfeeqikvlksskfkmlPELFQDdekaisptsatssgrtpL 612
Cdd:cd14891 477 HPCFPRPHPKDMREMFIVKHYAGTVSYTIGSFIDKNNDII----------------PEDFED-----------------L 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 613 TRTPAKptkgrpgqmakehkktvghqFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRI 692
Cdd:cd14891 524 LASSAK--------------------FSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEV 583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462544153 693 SAAGFPSRWTYQEFFSRYRVLM----KQKDVLSDRKQTcKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14891 584 LKVGLPTRVTYAELVDVYKPVLppsvTRLFAENDRTLT-QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
85-749 |
1.51e-154 |
|
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: 490.52 E-value: 1.51e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 85 VLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAY-SGQNMGDMDPHIFAVAEEAYK--QMARDERNQSII 160
Cdd:cd14880 3 VLRCLQARYT-ADTFYTNAGCTLVALNPFKPVPqLYSPELMREYhAAPQPQKLKPHIFTVGEQTYRnvKSLIEPVNQSIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 161 VSGESGAGKTVSAKYAMRYFATVSGSAS--EAN-----VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14880 82 VSGESGAGKTWTSRCLMKFYAVVAASPTswESHkiaerIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTkqggsPVIEGVDDAKEMAHTRQACT 313
Cdd:cd14880 162 MTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWL-----PNPERNLEEDCFEVTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 314 LLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLC---IFCDLMGVDYEEMCHWLCHRKLATATE--TYI 388
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKEsvrTSALLLKLPEDHLLETLQIRTIRAGKQqqVFK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 389 KPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNM 467
Cdd:cd14880 317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 468 HVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIE-SKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNK 546
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKLSRE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 547 -AFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLTrtpakptkgrpg 625
Cdd:cd14880 477 pSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQSRAPVL------------ 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 626 qmakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14880 545 --------TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQN 616
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2462544153 706 FFSRYRVLMKqkdvLSDRKQTCKNVLEKLILDKDKYQFGKTKIF 749
Cdd:cd14880 617 FVERYKLLRR----LRPHTSSGPHSPYPAKGLSEPVHCGRTKVF 656
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
84-751 |
4.21e-151 |
|
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: 481.51 E-value: 4.21e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14919 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 164 ESGAGKTVSAKYAMRYFATVSGS----ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANM 239
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASShkskKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 240 RTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQgGSPVIEGVDDAKEMAHTRQACTLLGISE 319
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSN-GHVTIPGQQDKDMFQETMEAMRIMGIPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 320 SHQMGIFRILAGILHLGNVGF-TSRDADSCTIPPKHEPLCIfCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATN 398
Cdd:cd14919 240 EEQMGLLRVISGVLQLGNIVFkKERNTDQASMPDNTAAQKV-SHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 399 ARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEY 477
Cdd:cd14919 319 AIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 478 MKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYN---THLNkcalFEKPR-LSNKA-F 548
Cdd:cd14919 399 QREGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQeqgTHPK----FQKPKqLKDKAdF 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 549 IIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLtrtpAKPTKGRPGQMa 628
Cdd:cd14919 475 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETAL----PGAFKTRKGMF- 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 629 kehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 708
Cdd:cd14919 550 ----RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2462544153 709 RYRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14919 626 RYEILTPNSipKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
83-751 |
3.64e-150 |
|
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: 480.54 E-value: 3.64e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAY--------SGQNMGDMDPHIFAVAEEAYKQMARD 153
Cdd:cd14902 1 AALLQALSERF-EHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFGGLLKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 154 ER-NQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEANVE--------EKVLASNPIMESIGNAKTTRNDNSSRFGKYI 224
Cdd:cd14902 80 ERrNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEgsdaveigKRILQTNPILESFGNAQTIRNDNSSRFGKFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 225 EIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGS----PVIEGVD 300
Cdd:cd14902 160 KIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGPsfarKRAVADK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 301 DAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFT---SRDADSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCH 377
Cdd:cd14902 240 YAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTaenGQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 378 RKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSF---------IGVLDIYGFETFEINS 448
Cdd:cd14902 320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSIsdedeelatIGILDIFGFESLNRNG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 449 FEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKL 527
Cdd:cd14902 400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSnGLFSLLDQECLMPKGSNQALSTKF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 528 YNTHLNKcalfekprlsnKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEK--AISPTSAT 605
Cdd:cd14902 480 YRYHGGL-----------GQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRdsPGADNGAA 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 606 SSGRTPLTRTPakptkgrpgqmakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACG 685
Cdd:cd14902 549 GRRRYSMLRAP-----------------SVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVG 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 686 VLETIRISAAGFPSRWTYQEF---FSRYRVLMKQKD----------------------VLSDRKQTCKNVLEKLILDKDK 740
Cdd:cd14902 612 VLEAVRIARHGYSVRLAHASFielFSGFKCFLSTRDraakmnnhdlaqalvtvlmdrvLLEDGVEREEKNPGALTAVTGD 691
|
730 740
....*....|....*....|....*
gi 2462544153 741 Y--------------QFGKTKIFFR 751
Cdd:cd14902 692 GsgtafendcrrkdvQVGRTLVFCK 716
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
83-751 |
2.59e-149 |
|
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: 477.91 E-value: 2.59e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGediINAYSGQNMGDMD--PHIFAVAEEAYKQMAR------- 152
Cdd:cd14895 1 PAFVDYLAQRYGVDQ-VYCRSGAVLIAVNPFKHIPgLYD---LHKYREEMPGWTAlpPHVFSIAEGAYRSLRRrlhepga 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 153 DERNQSIIVSGESGAGKTVSAKYAMRYFA--------TVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYI 224
Cdd:cd14895 77 SKKNQTILVSGESGAGKTETTKFIMNYLAesskhttaTSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 225 EIGF-----DKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG--NADNFNYTKQGGSPVI- 296
Cdd:cd14895 157 RMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLEllSAQEFQYISGGQCYQRn 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 297 EGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTS-------RDADSCTIPPK-----------HEPLC 358
Cdd:cd14895 237 DGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVAssedegeEDNGAASAPCRlasaspssltvQQHLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 359 IFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQAlhSAVKQHS------- 431
Cdd:cd14895 317 IVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSA--SPQRQFAlnpnkaa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 432 ------FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LG 504
Cdd:cd14895 395 nkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRpSG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 505 ILDLLDEECKMPKGTDDTWAQKLYNThLNKCALFEKPRL--SNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKS 582
Cdd:cd14895 475 IFSLLDEECVVPKGSDAGFARKLYQR-LQEHSNFSASRTdqADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGK 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 583 SKFKMLPELFqdDEKAISPTSATSSGRTPLTRtpakptkgRPGQMAkehKKTVGHQFRNSLHLLMETLNATTPHYVRCIK 662
Cdd:cd14895 554 TSDAHLRELF--EFFKASESAELSLGQPKLRR--------RSSVLS---SVGIGSQFKQQLASLLDVVQQTQTHYIRCIK 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 663 PNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLSdrkQTCKNVLEKliLDKDKYQ 742
Cdd:cd14895 621 PNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASD---ATASALIET--LKVDHAE 695
|
....*....
gi 2462544153 743 FGKTKIFFR 751
Cdd:cd14895 696 LGKTRVFLR 704
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
85-725 |
3.24e-149 |
|
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: 474.79 E-value: 3.24e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 85 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAY---------SGQNMGD--MDPHIFAVAEEAYKQMAR 152
Cdd:cd14900 3 ILSALETRFYAQK-IYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssSTRNKGSdpMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 153 ----DERNQSIIVSGESGAGKTVSAKYAMRYFA---------TVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSR 219
Cdd:cd14900 82 glngVMSDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaaSVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 220 FGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKmlrlgnADNFNYtkqggspviegV 299
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK------RDMYRR-----------V 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 300 DDAKEMahtrqactlLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHE--PLCIF-----CDLMGVDYEEMC 372
Cdd:cd14900 225 MDAMDI---------IGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDlaPSSIWsrdaaATLLSVDATKLE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 373 HWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALH--SAVKQHS---FIGVLDIYGFETFEIN 447
Cdd:cd14900 296 KALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKmdDSSKSHGglhFIGILDIFGFEVFPKN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 448 SFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQK 526
Cdd:cd14900 376 SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRpTGILSLIDEECVMPKGSDTTLASK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 527 LYnTHLNKCALFEKPRLSNKA--FIIQHFADKVEYQCEGFLEKNKDTVFEEQIkvlksskfkmlpELFQDdekaisptsa 604
Cdd:cd14900 456 LY-RACGSHPRFSASRIQRARglFTIVHYAGHVEYSTDGFLEKNKDVLHQEAV------------DLFVY---------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 605 tssgrtpltrtpakptkgrpgqmakehkktvGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRAC 684
Cdd:cd14900 513 -------------------------------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCN 561
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2462544153 685 GVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLSDRKQ 725
Cdd:cd14900 562 GVMEAVRVARAGFPIRLLHDEFVARYFSLARAKNRLLAKKQ 602
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
84-751 |
5.96e-149 |
|
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: 475.71 E-value: 5.96e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd15896 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 164 ESGAGKTVSAKYAMRYFATVSGS-----------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQgGSPVIEGVDDAKEMAHTRQAC 312
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSN-GNVTIPGQQDKDLFTETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 313 TLLGISESHQMGIFRILAGILHLGNVGF-TSRDADSCTIPPKHEPLCIfCDLMGVDYEEMCHWLCHRKLATATETYIKPI 391
Cdd:cd15896 240 RIMGIPEDEQIGMLKVVASVLQLGNMSFkKERHTDQASMPDNTAAQKV-CHLMGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 392 SKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd15896 319 TQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIE---SKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNK 546
Cdd:cd15896 399 ILEQEEYQREGIEWSFIDFgLDLQPCIDLIEkpaSPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 547 A-FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPltrtpaKPTKGRPG 625
Cdd:cd15896 479 AdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSEMP------GAFKTRKG 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 626 QMakehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd15896 553 MF-----RTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2462544153 706 FFSRYRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd15896 628 FRQRYEILTPNAipKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
84-751 |
7.76e-147 |
|
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: 469.96 E-value: 7.76e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14930 2 SVLHNLRERYY-SGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 164 ESGAGKTVSAKYAMRYFATVSGSAS-------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIG 236
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKgrkepgvPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 237 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGgsPVIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG--PSSSPGQERELFQETLESLRVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 317 ISESHQMGIFRILAGILHLGNVGF-TSRDADSCTIpPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14930 239 FSHEEITSMLRMVSAVLQFGNIVLkRERNTDQATM-PDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 396 ATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 474
Cdd:cd14930 318 ADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 475 EEYMKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKPR-LSNKA-F 548
Cdd:cd14930 398 EEYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRhLRDQAdF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 549 IIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRtpltrtpaKPTKGRPgqmA 628
Cdd:cd14930 477 SVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGD--------GPPGGRP---R 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 629 KEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 708
Cdd:cd14930 546 RGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2462544153 709 RYRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14930 626 RYEILTPNAipKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
34-798 |
3.17e-141 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 459.50 E-value: 3.17e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 34 GDKVLLLHLEEGKDLEYHLDPKtkelpHLRNPDILVGEN---DLTALSYLHEPAVLHNLRVRFIdSKLIYTYCGIVLVAI 110
Cdd:PTZ00014 63 GEKLTLKQIDPPTNSTFEVKPE-----HAFNANSQIDPMtygDIGLLPHTNIPCVLDFLKHRYL-KNQIYTTADPLLVAI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 111 NPYEQLPIYGEDIINAY-SGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASE 189
Cdd:PTZ00014 137 NPFKDLGNTTNDWIRRYrDAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMD 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 190 ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLC--A 267
Cdd:PTZ00014 217 LKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLkgA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 268 SAKLPE-FKMLRLGNADNFNytkqGGSPVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDAD 346
Cdd:PTZ00014 297 NDEMKEkYKLKSLEEYKYIN----PKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEG 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 347 -----SCTIPPKHEPLCIFCDLMGVDYEEMCHWLchrklaTATETYI------KPISKLQATNARDALAKHIYAKLFNWI 415
Cdd:PTZ00014 373 gltdaAAISDESLEVFNEACELLFLDYESLKKEL------TVKVTYAgnqkieGPWSKDESEMLKDSLSKAVYEKLFLWI 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 416 VDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPC 495
Cdd:PTZ00014 447 IRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESV 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 496 INLIESKL-GILDLLDEECKMPKGTDD----TWAQKLYNthlNKCALFEKpRLSNKAFIIQHFADKVEYQCEGFLEKNKD 570
Cdd:PTZ00014 527 IDLLCGKGkSVLSILEDQCLAPGGTDEkfvsSCNTNLKN---NPKYKPAK-VDSNKNFVIKHTIGDIQYCASGFLFKNKD 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 571 TVFEEQIKVLKSSKFKMLPELFQDDEkaisptsatssgrtpLTRtpakptkgrpGQMAKehKKTVGHQFRNSLHLLMETL 650
Cdd:PTZ00014 603 VLRPELVEVVKASPNPLVRDLFEGVE---------------VEK----------GKLAK--GQLIGSQFLNQLDSLMSLI 655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 651 NATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRV--LMKQKDVLSDRKQTCK 728
Cdd:PTZ00014 656 NSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYldLAVSNDSSLDPKEKAE 735
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462544153 729 NVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLRADKLRA--ACIRIqktIRGWLLRKKYLR-MRKAAITMQR 798
Cdd:PTZ00014 736 KLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAAwePLVSV---LEALILKIKKKRkVRKNIKSLVR 805
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
83-751 |
1.21e-139 |
|
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: 448.85 E-value: 1.21e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14896 1 SSVLLCLKKRF-HLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 163 GESGAGKTVSAKYAMRYFATVSGSASEANVE--EKVLasnPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMR 240
Cdd:cd14896 80 GHSGSGKTEAAKKIVQFLSSLYQDQTEDRLRqpEDVL---PILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 241 TYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISES 320
Cdd:cd14896 156 HYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 321 HQMGIFRILAGILHLGNVGFTSRDADSctippkHEPLCIFCD--------LMGVDYEEMCHWLCHRKLATATETYIKPIS 392
Cdd:cd14896 236 ELTAIWAVLAAILQLGNICFSSSERES------QEVAAVSSWaeihtaarLLQVPPERLEGAVTHRVTETPYGRVSRPLP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 393 KLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSF--IGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14896 310 VEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 471 KLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPRLSNKAFI 549
Cdd:cd14896 390 AQEEEECQRELLPWVPIPQPPRESCLDLLVDQPhSLLSILDDQTWLSQATDHTFLQKCHYHHGDH-PSYAKPQLPLPVFT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 550 IQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekaisptsatssgrtpltrtpAKPTKGRpgqmaK 629
Cdd:cd14896 469 VRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQE----------------------AEPQYGL-----G 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 630 EHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSR 709
Cdd:cd14896 522 QGKPTLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLAR 601
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2462544153 710 YRVLMKQK-DVLSDRKQtCKNVLEKLI-LDKDKYQFGKTKIFFR 751
Cdd:cd14896 602 FGALGSERqEALSDRER-CGAILSQVLgAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
85-749 |
4.29e-137 |
|
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: 444.42 E-value: 4.29e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 85 VLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQN-MGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14906 3 ILNNLGKRYK-SDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINqNKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 163 GESGAGKTVSAKYAMRYFATVSGSASEAN---------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR-Y 232
Cdd:cd14906 82 GESGSGKTEASKTILQYLINTSSSNQQQNnnnnnnnnsIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 233 RIIGANMRTYLLEKSRVVFQAEEER-NYHIFYQLCASAKLPEFKMLRLGN--------------ADNFNYTKQGGSPVIE 297
Cdd:cd14906 162 KIDGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNdpskyryldarddvISSFKSQSSNKNSNHN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 298 GVDDAKE-MAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTI---PPKHEPLCIFCDLMGVDYEEMCH 373
Cdd:cd14906 242 NKTESIEsFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqkDKVTASLESVSKLLGYIESVFKQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 374 WLCHRKLATATE--TYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQ-----------ALHSAVKQHSFIGVLDIYG 440
Cdd:cd14906 322 ALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRkfnqntqsndlAGGSNKKNNLFIGVLDIFG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 441 FETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGT 519
Cdd:cd14906 402 FENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKsDGILSLLDDECIMPKGS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 520 DDTWAQKlYNTHLNKCALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAI 599
Cdd:cd14906 482 EQSLLEK-YNKQYHNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQITST 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 600 SPTSATSSGRTpltrtpakptkgrpgqmakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQ 679
Cdd:cd14906 561 TNTTKKQTQSN-----------------------TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLS 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 680 QLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLSDRKQTCKNVLEKLIL----------------------- 736
Cdd:cd14906 618 QLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIqsklktmgisnnkkknnsnsnsn 697
|
730
....*....|....*.
gi 2462544153 737 ---DKDKYQFGKTKIF 749
Cdd:cd14906 698 ttnDKPLFQIGKTKIF 713
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
83-749 |
7.31e-137 |
|
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: 441.35 E-value: 7.31e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSG-QNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14876 1 PCVLDFLKHRYLKNQ-IYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 162 SGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:cd14876 80 SGESGAGKTEATKQIMRYFASAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 242 YLLEKSRVVFQAEEERNYHIFYQLC--ASAKLPE-FKMLRLGNADNFNytkqGGSPVIEGVDDAKEMAHTRQACTLLGIS 318
Cdd:cd14876 160 FLLEKSRIVTQDDNERSYHIFYQLLkgADSEMKSkYHLLGLKEYKFLN----PKCLDVPGIDDVADFEEVLESLKSMGLT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 319 ESHQMGIFRILAGILHLGNVGFTSRDA----DSCTIPPkhEPLCIF---CDLMGVDYEEMCHWLChRKLATATETYIK-P 390
Cdd:cd14876 236 EEQIDTVFSIVSGVLLLGNVKITGKTEqgvdDAAAISN--ESLEVFkeaCSLLFLDPEALKRELT-VKVTKAGGQEIEgR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 391 ISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14876 313 WTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 471 KLEQEEYMKEQIPWTLIDFYDNQPCIN-LIESKLGILDLLDEECKMPKGTDD----TWAQKLYNthlNKCALFEKpRLSN 545
Cdd:cd14876 393 ERESKLYKDEGIPTAELEYTSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEkfvsACVSKLKS---NGKFKPAK-VDSN 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 546 KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekaisptsatssgrTPLTRtpakptkgrpG 625
Cdd:cd14876 469 INFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEG---------------VVVEK----------G 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 626 QMAKehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14876 524 KIAK--GSLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEE 601
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2462544153 706 FFSRYRVL-MKQKDVLSDRKQT-CKNVLEKLILDKDKYQFGKTKIF 749
Cdd:cd14876 602 FLYQFKFLdLGIANDKSLDPKVaALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
84-736 |
2.89e-128 |
|
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: 419.89 E-value: 2.89e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYS---GQNMGDM-------DPHIFAVAEEAYKQMAR 152
Cdd:cd14899 2 SILNALRLRY-ERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhNSQFGDRvtstdprEPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 153 DERNQSIIVSGESGAGKTVSAKYAMRYFATVSG----------------SASEANVEEKVLASNPIMESIGNAKTTRNDN 216
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGtgnnnltnsesisppaSPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 217 SSRFGKYIEIGF-DKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQL------CASAKLPEFKMLRlGNADNFNYTK 289
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELlsadnnCVSKEQKQVLALS-GGPQSFRLLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 290 QG-GSPVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFT--------------SRDADSCTIPPKH 354
Cdd:cd14899 240 QSlCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEqiphkgddtvfadeARVMSSTTGAFDH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 355 epLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVK------ 428
Cdd:cd14899 320 --FTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASapwgad 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 429 ---------QHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLI 499
Cdd:cd14899 398 esdvddeedATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 500 ESK-LGILDLLDEECKMPKGTDDTWAQKLY--------NTHLNKCALFEKprlsNKAFIIQHFADKVEYQCEGFLEKNKD 570
Cdd:cd14899 478 EHRpIGIFSLTDQECVFPQGTDRALVAKYYlefekknsHPHFRSAPLIQR----TTQFVVAHYAGCVTYTIDGFLAKNKD 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 571 TVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLTRTPAKPTKGrpgqmakehKKTVGHQFRNSLHLLMETL 650
Cdd:cd14899 554 SFCESAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIA---------AVSVGTQFKIQLNELLSTV 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 651 NATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYR----VLMKQKDVLSDRKQT 726
Cdd:cd14899 625 RATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYRrvllSLYKWGDNDFERQMR 704
|
730
....*....|
gi 2462544153 727 CKNVLEKLIL 736
Cdd:cd14899 705 CGVSLGKTRV 714
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
85-751 |
6.00e-124 |
|
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: 405.42 E-value: 6.00e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 85 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMG-----DMDPHIFAVAEEAYKQMARDERNQS 158
Cdd:cd14886 3 VIDILRDRFAKDK-IYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 159 IIVSGESGAGKTVSAKYAMRYFAtVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGAN 238
Cdd:cd14886 82 CIVSGESGAGKTETAKQLMNFFA-YGHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 239 MRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLgIS 318
Cdd:cd14886 161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKL-FS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 319 ESHQMGIFRILAGILHLGNVGF---TSRDADSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14886 240 KNEIDSFYKCISGILLAGNIEFseeGDMGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 396 ATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQE 475
Cdd:cd14886 320 AEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEIQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 476 EYMKEQIPWTLIDFYDNQPCINLIES-KLGILDLLDEECKMPKGTDDTWAQKLyNTHLNKcALFEKPRLSNKAFIIQHFA 554
Cdd:cd14886 400 EYEIEGIDHSMITFTDNSNVLAVFDKpNLSIFSFLEEQCLIQTGSSEKFTSSC-KSKIKN-NSFIPGKGSQCNFTIVHTA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 555 DKVEYQCEGFLEKNKDTVFEEQIKVLKSSKfkmlpelfqddekaisptsatssgrTPLTRTPAKPTKGRPGQMAKehkKT 634
Cdd:cd14886 478 ATVTYNTEEFVDKNKHKLSVDILELLMGST-------------------------NPIVNKAFSDIPNEDGNMKG---KF 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 635 VGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLM 714
Cdd:cd14886 530 LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILI 609
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2462544153 715 KQKDVL----SDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14886 610 SHNSSSqnagEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
85-751 |
1.04e-121 |
|
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: 399.57 E-value: 1.04e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 85 VLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAY-SGQNMGDMDPHIFAVAEEAYKQM-ARDERNQSIIVS 162
Cdd:cd14875 3 LLHCIKERFEKLHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 163 GESGAGKTVSAKYAMRYFATVS----GSASEANVEEKVLA----SNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRI 234
Cdd:cd14875 83 GESGSGKTENAKMLIAYLGQLSymhsSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPTSGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 235 -IGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKML-RLGNADNFNYTKQGGSPVIEGVD-----DAKEMAH 307
Cdd:cd14875 163 mVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTFVRRGVDgktldDAHEFQN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 308 TRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPpKHEPLCIFCDLMGVDYEEM--CHWLchrKLATATE 385
Cdd:cd14875 243 VRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIA-DETPFLTACRLLQLDPAKLreCFLV---KSKTSLV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 386 TYIKpiSKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHS--FIGVLDIYGFETFEINSFEQFCINYANEKLQQ 463
Cdd:cd14875 319 TILA--NKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCSGckYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 464 QFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR 542
Cdd:cd14875 397 HYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKrTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPYFVLPK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 543 --LSNKaFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaisptsatssgrtpltrtpakpt 620
Cdd:cd14875 477 stIPNQ-FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTE------------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 621 kgrpgQMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSR 700
Cdd:cd14875 531 -----KGLARRKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVR 605
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 701 WTYQEFFSRYRVLM--------KQKDvLSDRKQTCKNVLEKLI-LDKDKYQFGKTKIFFR 751
Cdd:cd14875 606 RPIEQFCRYFYLIMprstaslfKQEK-YSEAAKDFLAYYQRLYgWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
84-713 |
7.16e-114 |
|
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: 374.23 E-value: 7.16e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 84 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQlpIYGEDIINAYSgQNMGDMDPHIFAVAEEAYKQMARdERNQSIIVSG 163
Cdd:cd14898 2 ATLEILEKRYASGK-IYTKSGLVFLALNPYET--IYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 164 ESGAGKTVSAKYAMRYFatVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRyrIIGANMRTYL 243
Cdd:cd14898 77 ESGSGKTENAKLVIKYL--VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFDGK--ITGAKFETYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 244 LEKSRVVFQAEEERNYHIFYQLCASaklpefKMLRLGNaDNFNYTKQGGSPViEGVDDAKEMAHTRQACTLLGISESHQm 323
Cdd:cd14898 153 LEKSRVTHHEKGERNFHIFYQFCAS------KRLNIKN-DFIDTSSTAGNKE-SIVQLSEKYKMTCSAMKSLGIANFKS- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 324 gIFRILAGILHLGNVGFTSrdaDSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATEtYIKPISKL-QATNARDA 402
Cdd:cd14898 224 -IEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGE-TIEVFNTLkQARTIRNS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 403 LAKHIYAKLFNWIVDNVNQALhSAVKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQI 482
Cdd:cd14898 299 MARLLYSNVFNYITASINNCL-EGSGERS-ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEGI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 483 PWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKL--YNTHlnkcalFEKPRLSNKaFIIQHFADKVEYQ 560
Cdd:cd14898 377 EWPDVEFFDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIkkYLNG------FINTKARDK-IKVSHYAGDVEYD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 561 CEGFLEKNKDtvfEEQIKVLKSskfkmlpelfqddekaisptsatssgrtpltrtpakptkgrPGQMAKEHKKTVGHQFR 640
Cdd:cd14898 450 LRDFLDKNRE---KGQLLIFKN-----------------------------------------LLINDEGSKEDLVKYFK 485
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462544153 641 NSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVL 713
Cdd:cd14898 486 DSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRIL 558
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
84-750 |
1.87e-106 |
|
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: 355.70 E-value: 1.87e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 84 AVLHNLRVRFIdSKLIYTYCGI-VLVAINPYEQLPI--------YGEDIINAYSGQNMGDMdPHIFAVAEEAYKQMARDE 154
Cdd:cd14879 5 AITSHLASRFR-SDLPYTRLGSsALVAVNPYKYLSSnsdaslgeYGSEYYDTTSGSKEPLP-PHAYDLAARAYLRMRRRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 155 RNQSIIVSGESGAGKTVSAKYAMRYFATVSGSAS-EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14879 83 EDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKkGTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGG---SPVIEGVDDAKEMAHTRQ 310
Cdd:cd14879 163 LIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYGchpLPLGPGSDDAEGFQELKT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 311 ACTLLGISESHQMGIFRILAGILHLGNVGFT---SRDADSCTIPPKHEpLCIFCDLMGVDYEEmchwlchrkLATATeTY 387
Cdd:cd14879 243 ALKTLGFKRKHVAQICQLLAAILHLGNLEFTydhEGGEESAVVKNTDV-LDIVAAFLGVSPED---------LETSL-TY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 388 iKpiSKL-------------QATNARDALAKHIYAKLFNWIVDNVNQALhSAVKQ--HSFIGVLDIYGFETF---EINSF 449
Cdd:cd14879 312 -K--TKLvrkelctvfldpeGAAAQRDELARTLYSLLFAWVVETINQKL-CAPEDdfATFISLLDFPGFQNRsstGGNSL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 450 EQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECK-MPKGTDDTWAQKL 527
Cdd:cd14879 388 DQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKpGGLLGILDDQTRrMPKKTDEQMLEAL 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 528 YNTHLNKCALFEKPRLSNK----AFIIQHFADKVEYQCEGFLEKNKDTVfeeqikvlkSSKFKMLpelfqddekaISPTs 603
Cdd:cd14879 468 RKRFGNHSSFIAVGNFATRsgsaSFTVNHYAGEVTYSVEGFLERNGDVL---------SPDFVNL----------LRGA- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 604 atssgrtpltrtpakptkgrpgqmakehkktvgHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRA 683
Cdd:cd14879 528 ---------------------------------TQLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRS 574
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462544153 684 CGVLETIRISAAGFPSRWTYQEFFSRYrvlmKQKDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFF 750
Cdd:cd14879 575 LGLPELAARLRVEYVVSLEHAEFCERY----KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
84-751 |
4.91e-98 |
|
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: 331.39 E-value: 4.91e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 84 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAY---SGQNMGDMDPHIFAVAEEAYKQMARDERNQSII 160
Cdd:cd14878 2 SLLYEIQKRFGNNQ-IYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 161 VSGESGAGKTVSAKYAMRYFATVSGSaSEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGF-DKRYRIIGANM 239
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASS-SRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 240 RTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQG---GSPVIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14878 160 YTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmreDVSTAERSLNREKLAVLKQALNVVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 317 ISESHQMGIFRILAGILHLGNVGFTS-RDADSCTIpPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14878 240 FSSLEVENLFVILSAILHLGDIRFTAlTEADSAFV-SDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 396 ATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSF----IGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFK 471
Cdd:cd14878 319 AEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 472 LEQEEYMKEQIPW----------TLIDFYDNQPcinlieskLGILDLLDEECKMPKGTDDTWAQKLY----NTHLNKCAL 537
Cdd:cd14878 399 QEQTECVQEGVTMetayspgnqtGVLDFFFQKP--------SGFLSLLDEESQMIWSVEPNLPKKLQslleSSNTNAVYS 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 538 FEK-------PRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQddekaisptsatssgrT 610
Cdd:cd14878 471 PMKdgngnvaLKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ----------------S 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 611 PLTrtpakptkgrpgqmakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETI 690
Cdd:cd14878 535 KLV--------------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMV 594
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462544153 691 RISAAGFPSRWTYQEFFSRYRVLMKQkdVLSDRKQT-----CKNVLEKLILdkDKYQFGKTKIFFR 751
Cdd:cd14878 595 KIFRYGYPVRLSFSDFLSRYKPLADT--LLGEKKKQsaeerCRLVLQQCKL--QGWQMGVRKVFLK 656
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
85-751 |
2.01e-96 |
|
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: 327.73 E-value: 2.01e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 85 VLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 164
Cdd:cd01386 3 VLHTLRQRY-GANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 165 SGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 244
Cdd:cd01386 82 SGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 245 EKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGN-ADNFNYtkqGGSPVIEGVD---DAKEMAHTRQACTLLGISES 320
Cdd:cd01386 162 ERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQlAESNSF---GIVPLQKPEDkqkAAAAFSKLQAAMKTLGISEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 321 HQMGIFRILAGILHLGNVGftsrdadSCTIPP-------KHEPLCIFCDLMGVDYEEMCHWLCHRKL------ATATETY 387
Cdd:cd01386 239 EQRAIWSILAAIYHLGAAG-------ATKAASagrkqfaRPEWAQRAAYLLGCTLEELSSAIFKHHLsggpqqSTTSSGQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 388 IKPIS------KLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFE------INSFEQFCIN 455
Cdd:cd01386 312 ESPARsssggpKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAhsgsqrGATFEDLCHN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 456 YANEKLQQQFNMHVFKLEQEEYMKEQIPwtlIDFYDNQPC----INLI---------------ESKLGILDLLDEECKMP 516
Cdd:cd01386 392 YAQERLQLLFHERTFVAPLERYKQENVE---VDFDLPELSpgalVALIdqapqqalvrsdlrdEDRRGLLWLLDEEALYP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 517 KGTDDTWAQKLYnTHLNKCALFEKPRLSNKA-----FIIQHF--ADKVEYQCEGFLEKNKDTVFEEQikvlksskfkmLP 589
Cdd:cd01386 469 GSSDDTFLERLF-SHYGDKEGGKGHSLLRRSegplqFVLGHLlgTNPVEYDVSGWLKAAKENPSAQN-----------AT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 590 ELFQDDEKaisptsatssgrtpltrtpakptkgrpgQMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPN----- 664
Cdd:cd01386 537 QLLQESQK----------------------------ETAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagk 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 665 -DFKFPFTFDEKRAVQ------QLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK-------QKDVLSDRKQTCKNV 730
Cdd:cd01386 589 dERSTSSPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPpltkklgLNSEVADERKAVEEL 668
|
730 740
....*....|....*....|.
gi 2462544153 731 LEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01386 669 LEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
83-751 |
2.40e-94 |
|
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: 323.14 E-value: 2.40e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFI-------DSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDER 155
Cdd:cd14887 1 PNLLENLYQRYNkayinkeNRNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 156 NQSIIVSGESGAGKTVSAKYAMRYFATVS---GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSdrrHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYtkqggspviegvddakEMAHTRQAC 312
Cdd:cd14887 161 KLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPEST----------------DLRRITAAM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 313 TLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHR---KLATATETYIK 389
Cdd:cd14887 225 KTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSVSVGCEETAADRSHSSEVKCLSsglKVTEASRKHLK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 390 PISKL--------------------------------QATNARDALAKHIYAKLFNWIVDNVNQALHSAVK--------- 428
Cdd:cd14887 305 TVARLlglppgvegeemlrlalvsrsvretrsffdldGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsded 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 429 -----QHSFIGVLDIYGFETFE---INSFEQFCINYANEKLqqqfnmHVFKLEQ-----------EEYMKEQI------- 482
Cdd:cd14887 385 tpsttGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERL------HCFLLEQlilnehmlytqEGVFQNQDcsafpfs 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 483 ----------PWTLIDF-----------YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKP 541
Cdd:cd14887 459 fplastltssPSSTSPFsptpsfrsssaFATSPSLPSSLSSLSSSLSSSPPVWEGRDNSDLFYEKLNKNIINSAKYKNIT 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 542 R---LSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEqikvlksskfkmLPELFqddekaisptsatSSGRTPLTRTPAK 618
Cdd:cd14887 539 PalsRENLEFTVSHFACDVTYDARDFCRANREATSDE------------LERLF-------------LACSTYTRLVGSK 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 619 PTKGRpgQMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFP 698
Cdd:cd14887 594 KNSGV--RAISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFP 671
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 2462544153 699 SRWTYQEFFSRY--RVLMKQKDVLSDrKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14887 672 CRLPYVELWRRYetKLPMALREALTP-KMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
85-751 |
2.63e-94 |
|
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: 320.04 E-value: 2.63e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 85 VLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYgediINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 164
Cdd:cd14937 3 VLNMLALRY-KKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 165 SGAGKTVSAKYAMRYFatVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 244
Cdd:cd14937 78 SGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 245 EKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGgSPVIEGVDDAKEMAHTRQACTLLGISESHQmG 324
Cdd:cd14937 156 ENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNK-NVVIPEIDDAKDFGNLMISFDKMNMHDMKD-D 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 325 IFRILAGILHLGNVGFTSRDA---DSCTIPPKH--EPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNA 399
Cdd:cd14937 234 LFLTLSGLLLLGNVEYQEIEKggkTNCSELDKNnlELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 400 RDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 479
Cdd:cd14937 314 CKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYKA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 480 EQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTwaqkLYNTHLNKCALFEK----PRLSNKAFIIQHFAD 555
Cdd:cd14937 394 EDILIESVKYTTNESIIDLLRGKTSIISILEDSCLGPVKNDES----IVSVYTNKFSKHEKyastKKDINKNFVIKHTVS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkaisptSATSSGRtpltrtpakptkgrpgqmakehKKTV 635
Cdd:cd14937 470 DVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE------VSESLGR----------------------KNLI 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAgFPSRWTYQEFFSRYRVL-- 713
Cdd:cd14937 522 TFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNISFF-FQYKYTFDVFLSYFEYLdy 600
|
650 660 670
....*....|....*....|....*....|....*...
gi 2462544153 714 MKQKDVLSDRKQTCKNVLEKLIlDKDKYQFGKTKIFFR 751
Cdd:cd14937 601 STSKDSSLTDKEKVSMILQNTV-DPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
84-750 |
3.24e-91 |
|
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: 310.89 E-value: 3.24e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 84 AVLHNLRVRFIDSKLiYTYCGIVLVAINPYEqlpiygeDIINAY---SGQNMGDMdPHIFAVAEEAYKQMARDERNQSII 160
Cdd:cd14881 2 AVMKCLQARFYAKEF-FTNVGPILLSVNPYR-------DVGNPLtltSTRSSPLA-PQLLKVVQEAVRQQSETGYPQAII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 161 VSGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKryriiGANMR 240
Cdd:cd14881 73 LSGTSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-----GALYR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 241 T----YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG--NADNFNYTkQGGSPVIEGVDDAKEMAHTRQACTL 314
Cdd:cd14881 148 TkihcYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgySPANLRYL-SHGDTRQNEAEDAARFQAWKACLGI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 315 LGISESHQMgifRILAGILHLGNVGFTsrDADSCTIPPKHE-PLCIFCDLMGVDYEEMchwlcHRKLATATET----YIK 389
Cdd:cd14881 227 LGIPFLDVV---RVLAAVLLLGNVQFI--DGGGLEVDVKGEtELKSVAALLGVSGAAL-----FRGLTTRTHNargqLVK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 390 PISKLQATNA-RDALAKHIYAKLFNWIVDNVN--QALHSAVKQHS---FIGVLDIYGFETFEINSFEQFCINYANEKLQQ 463
Cdd:cd14881 297 SVCDANMSNMtRDALAKALYCRTVATIVRRANslKRLGSTLGTHAtdgFIGILDMFGFEDPKPSQLEHLCINLCAETMQH 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 464 QFNMHVFKLEQEEYMKEQIPWTL-IDFYDNQPCINLIES-KLGILDLLDEECKmPKGTDDTWAQKLYNTHLNKCALFEKP 541
Cdd:cd14881 377 FYNTHIFKSSIESCRDEGIQCEVeVDYVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 542 RLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVL--KSSKFKMLPELfQDdekaisptsatssgrtpltrtpakp 619
Cdd:cd14881 456 PQDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFykQNCNFGFATHT-QD------------------------- 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 620 tkgrpgqmakehkktvghqFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPS 699
Cdd:cd14881 510 -------------------FHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPH 570
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462544153 700 RWTYQEFFSRYRVL--MKQKDVLSDRKQTCKNVLEKLILDKDK---------YQFGKTKIFF 750
Cdd:cd14881 571 RMRFKAFNARYRLLapFRLLRRVEEKALEDCALILQFLEAQPPsklssvstsWALGKRHIFL 632
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
83-750 |
1.45e-89 |
|
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: 307.99 E-value: 1.45e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYS-------GQNMGDMDPHIFAVAEEAYKQMARDE 154
Cdd:cd14884 1 PNVLQNLKNRYLKNK-IYTFHASLLLALNPYKPLKeLYDQDVMNVYLhkksnsaASAAPFPKAHIYDIANMAYKNMRGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 155 RNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR--- 231
Cdd:cd14884 80 KRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVent 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 232 ------YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQL---CASAKLPEFKMLR------LGNADNFNYTKQGGSPVI 296
Cdd:cd14884 160 qknmfnGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVlrgLSDEDLARRNLVRncgvygLLNPDESHQKRSVKGTLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 297 EGVD-----------DAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNvgftsrDADSCTippkheplcifCDLMG 365
Cdd:cd14884 240 LGSDsldpseeekakDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGN------RAYKAA-----------AECLQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 366 VDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQAL------------HSAVKQHSFI 433
Cdd:cd14884 303 IEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdesdneDIYSINEAII 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 434 GVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESklgILDLLDEEC 513
Cdd:cd14884 383 SILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAK---IFRRLDDIT 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 514 KMP----KGTDDTWAQKLYNTHlNKCALFEK-------PRL---SNKA-------FIIQHFADKVEYQCEGFLEKNKDTV 572
Cdd:cd14884 460 KLKnqgqKKTDDHFFRYLLNNE-RQQQLEGKvsygfvlNHDadgTAKKqnikkniFFIRHYAGLVTYRINNWIDKNSDKI 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 573 feeqikvlksskfkmlpelfqddEKAISPTSATSSGRTpLTRTPAKPTKGrpgqmakeHKKTVGHQFRNSLHLLMETLNA 652
Cdd:cd14884 539 -----------------------ETSIETLISCSSNRF-LREANNGGNKG--------NFLSVSKKYIKELDNLFTQLQS 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 653 TTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkQKDVLSDRKQTCKNVLE 732
Cdd:cd14884 587 TDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKETAAALKEQI-AKELEKCNSNTDIEYQR 665
|
730
....*....|....*...
gi 2462544153 733 KLILDKDKYQFGKTKIFF 750
Cdd:cd14884 666 RLAALDVQFIPDGRLYAF 683
|
|
| Myo5-like_CBD |
cd14945 |
Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied ... |
1477-1800 |
4.93e-86 |
|
Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5 a,b,c) in vertebrates and two (myo2 and myo4) in fungi and related to plant class XI myosins. Their C-terminal cargo binding domains is important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. MyoV-CBDs interact with several adaptor proteins that in turn interact with the cargo.
Pssm-ID: 271253 [Multi-domain] Cd Length: 288 Bit Score: 283.14 E-value: 4.93e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1477 EDEQKLVKNLILELKPRGVAVNLipgLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNT 1556
Cdd:cd14945 1 SEEDSLLRGIVTDFEPSSGDHKL---TPAYILYLCIRHAASNGLTGQSTSLLNKVLKTIQQVVQQHNDDMQLLAFWLSNA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1557 CRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmivsgmlehetiqgvsgv 1636
Cdd:cd14945 78 SELLYFLKQDSKLYGAAGEAPQKEEEQKLTVSDLNELKQDLEAVSIKIYQQALKYLNKNLQP------------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1637 kptglrkrtssiadegtyTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRY 1716
Cdd:cd14945 140 ------------------KIRDIVKFLNSFLDLLKSFHVHPEIRSQVFTQLFSFINARLFNQLITKKDALSWSRGMQIRA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1717 NVSQLEEWLRDKNLmNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFI 1796
Cdd:cd14945 202 NISRLEEWCEGRGL-EHLAVDFLSKLIQAVQLLQLKKYTQEDIEILCELCPSLNPAQLQAILTQYQPANYGESPVPKEIL 280
|
....
gi 2462544153 1797 RTIQ 1800
Cdd:cd14945 281 RTLA 284
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
97-751 |
9.31e-86 |
|
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: 296.23 E-value: 9.31e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 97 KLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSgQNMGdMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKY 175
Cdd:cd14905 14 EIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN-QRRG-LPPHLFALAAKAISDMQDFRRDQLIFIGGESGSGKSENTKI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 176 AMRYFATVSGSASEAnVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEE 255
Cdd:cd14905 92 IIQYLLTTDLSRSKY-LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQNKG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 256 ERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHL 335
Cdd:cd14905 171 ERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFIIIL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 336 GNVGFTSRDADSctippkheplcifcdlmGVDYEEMCHWLCHRKLATATETYIKPISKL-----QATNARDALAKHIYAK 410
Cdd:cd14905 251 GNVTFFQKNGKT-----------------EVKDRTLIESLSHNITFDSTKLENILISDRsmpvnEAVENRDSLARSLYSA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 411 LFNWIVDNVNQALHSAVKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPW-TLIDF 489
Cdd:cd14905 314 LFHWIIDFLNSKLKPTQYSHT-LGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWmTPISF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 490 YDNQPCINLIESklgILDLLDEECKMPKGTDDTWAQKLYNtHLNKCALF-EKPrlsNKaFIIQHFADKVEYQCEGFLEKN 568
Cdd:cd14905 393 KDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKLQN-FLSRHHLFgKKP---NK-FGIEHYFGQFYYDVRGFIIKN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 569 KDTVFEEQIKVLKSSKFKMLpeLFQDDEKAISPTSA---------TSSGRTPLT----------------RTPAKPTKGR 623
Cdd:cd14905 465 RDEILQRTNVLHKNSITKYL--FSRDGVFNINATVAelnqmfdakNTAKKSPLSivkvllscgsnnpnnvNNPNNNSGGG 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 624 PGQMAKEHKKTVGHQFRNSLHLLMETLNATTP--HYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRW 701
Cdd:cd14905 543 GGGGNSGGGSGSGGSTYTTYSSTNKAINNSNCdfHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHY 622
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462544153 702 TYQEFFSRYRVLMKQkdvlsdrKQTCKNVLEKLI---LDKDK-----YQFGKTKIFFR 751
Cdd:cd14905 623 NNKIFFDRFSFFFQN-------QRNFQNLFEKLKendINIDSilpppIQVGNTKIFLR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
84-751 |
1.09e-79 |
|
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: 277.14 E-value: 1.09e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYsgqnmgdmdpHIFAVAEEAYKQMARDERN-QSIIVS 162
Cdd:cd14874 2 GIAQNLHERF-KKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 163 GESGAGKTVSAKYAMRYFATVSGSASEAnveEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMR-T 241
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTT---KHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLNLKyT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 242 YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSpvIEGV-DDAKEMAHTRQACTLLGISES 320
Cdd:cd14874 147 VPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNS--TENIqSDVNHFKHLEDALHVLGFSDD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 321 HQMGIFRILAGILHLGNVGFTSRdadscTIPPKHEPLCIFCD---------LMGVDYEEMCHWLchrklaTATETYIKPI 391
Cdd:cd14874 225 HCISIYKIISTILHIGNIYFRTK-----RNPNVEQDVVEIGNmsevkwvafLLEVDFDQLVNFL------LPKSEDGTTI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 392 SKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFK 471
Cdd:cd14874 294 DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV-ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFH 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 472 LEQEEYMKEQIPwtlIDF-----YDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCAlFEKPRLSN 545
Cdd:cd14874 373 DQLVDYAKDGIS---VDYkvpnsIENGKTVELLFKKpYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS-YGKARNKE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 546 K-AFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQddekaiSPTSATSsgrtpltrtpakptkgrp 624
Cdd:cd14874 449 RlEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE------SYSSNTS------------------ 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 625 gqmakEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQ 704
Cdd:cd14874 505 -----DMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKT 579
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 2462544153 705 EFFSRYRVLM--------KQKDVLSDRKQTCKNVLEklildkDKYQFGKTKIFFR 751
Cdd:cd14874 580 TFARQYRCLLpgdiamcqNEKEIIQDILQGQGVKYE------NDFKIGTEYVFLR 628
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
86-750 |
1.96e-75 |
|
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: 267.61 E-value: 1.96e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 86 LHNLRVRF-IDSklIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQN----------MGDMDPHIFAVAEEAYKQMARDE 154
Cdd:cd14893 4 LYTLRARYrMEQ--VYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSReqtplyekdtVNDAPPHVFALAQNALRCMQDAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 155 RNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEAN-----------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKY 223
Cdd:cd14893 82 EDQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPdsegasgvlhpIGQQILHAFTILEAFGNAATRQNRNSSRFAKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 224 IEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKL-PEFK-MLRLGN-ADNFNYTKQGGSPVIEGVD 300
Cdd:cd14893 162 ISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdPTLRdSLEMNKcVNEFVMLKQADPLATNFAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 301 DAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGF----------------TSRDADSCTIPPKHEPLcIFCDLM 364
Cdd:cd14893 242 DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvgganstTVSDAQSCALKDPAQIL-LAAKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 365 GVDYEEMCHWLCHRKL----ATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQAL---------HSAVKQHS 431
Cdd:cd14893 321 EVEPVVLDNYFRTRQFfskdGNKTVSSLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdryekSNIVINSQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 432 FIGVLDIYGFETFE--INSFEQFCINYANEKLQQQF-------NMHVFKLEQEEYMKEQIPWTLIDF-YDNQPCINLIES 501
Cdd:cd14893 401 GVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvqntlaiNFSFLEDESQQVENRLTVNSNVDItSEQEKCLQLFED 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 502 K-LGILDLLDEECKMPKGTDDTWAQKLYN--------THLNKCALFEKPRLSNKA-----FIIQHFADKVEYQCEGFLEK 567
Cdd:cd14893 481 KpFGIFDLLTENCKVRLPNDEDFVNKLFSgneavgglSRPNMGADTTNEYLAPSKdwrllFIVQHHCGKVTYNGKGLSSK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 568 NKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISP-TSATSSGRTPLTRTPAKPTKGRPGQmAKEHKKTVGHQFRNSLHLL 646
Cdd:cd14893 561 NMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSeKAAKQTEERGSTSSKFRKSASSARE-SKNITDSAATDVYNQADAL 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 647 METLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYrvlmkqKDVLSDRKqT 726
Cdd:cd14893 640 LHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY------KNVCGHRG-T 712
|
730 740
....*....|....*....|....*...
gi 2462544153 727 CKNVLEKL----ILDKDKYQFGKTKIFF 750
Cdd:cd14893 713 LESLLRSLsaigVLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
85-751 |
1.13e-64 |
|
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: 233.48 E-value: 1.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 85 VLHNLRVRfIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 164
Cdd:cd14882 3 ILEELRHR-YLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 165 SGAGKTVSAKYAMRYFATVSGSASeaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 244
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNR--GATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 245 EKSRVVFQAEEERNYHIFY----QLCASAKLPEF--------KMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAhtrQAC 312
Cdd:cd14882 160 EKLRVSTTDGNQSNFHIFYyfydFIEAQNRLKEYnlkagrnyRYLRIPPEVPPSKLKYRRDDPEGNVERYKEFE---EIL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 313 TLLGISESHQMGIFRILAGILHLGNVGFtsRDADSCTIPPKHEPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPIS 392
Cdd:cd14882 237 KDLDFNEEQLETVRKVLAAILNLGEIRF--RQNGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 393 KLQATNARDALAKHIYAKLFNWIVDNVNQALH--SAV--KQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMH 468
Cdd:cd14882 315 TEEARDARDVLASTLYSRLVDWIINRINMKMSfpRAVfgDKYS-ISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYNQR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 469 VFKLEQEEYMKEQIPWTLIDFYDNQPCI-NLIESKLGILDLLDEECKMPKGtddtwAQKLYNTHLNKCALFEKPrLSNKA 547
Cdd:cd14882 394 IFISEMLEMEEEDIPTINLRFYDNKTAVdQLMTKPDGLFYIIDDASRSCQD-----QNYIMDRIKEKHSQFVKK-HSAHE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 548 FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekaisptsatssgrtpltrtpakptkgrpgqm 627
Cdd:cd14882 468 FSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN--------------------------------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 628 AKEHK-KTVGHQFRNSLHLLMETL----NATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWT 702
Cdd:cd14882 515 SQVRNmRTLAATFRATSLELLKMLsigaNSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIP 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 2462544153 703 YQEFFSRYRVLMKQKDVLSD-RKQTCKNVLEKLILdkDKYQFGKTKIFFR 751
Cdd:cd14882 595 FQEFLRRYQFLAFDFDETVEmTKDNCRLLLIRLKM--EGWAIGKTKVFLK 642
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
106-229 |
8.11e-49 |
|
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: 171.76 E-value: 8.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 106 VLVAINPYEQLPIYGED-IINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVS 184
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462544153 185 GSASEAN--------------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFD 229
Cdd:cd01363 81 FNGINKGetegwvylteitvtLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLD 139
|
|
| DIL |
pfam01843 |
DIL domain; The DIL domain has no known function. |
1682-1785 |
3.11e-42 |
|
DIL domain; The DIL domain has no known function.
Pssm-ID: 460359 [Multi-domain] Cd Length: 103 Bit Score: 150.05 E-value: 3.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1682 QVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLmNSGAKETLEPLIQAAQLLQVKKKTDDDAEA 1761
Cdd:pfam01843 1 QLFSQLFYFINAELFNRLLLRKKYCSWSKGMQIRYNLSRLEEWARSNGL-ESEARDHLAPLIQAAQLLQLRKSTLEDLDS 79
|
90 100
....*....|....*....|....
gi 2462544153 1762 ICSMCNALTTAQIVKVLNLYTPVN 1785
Cdd:pfam01843 80 ILQVCPALNPLQLHRLLTLYQPDD 103
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
83-749 |
4.40e-40 |
|
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: 160.39 E-value: 4.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 83 PAVLHNLRVRFIDSKLiYTYCGIVLVAINPYEQLPIYGEDIINAYSGQN-MGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14938 1 PSVLYHLKERFKNNKF-YTKMGPLLIFINPKINNNINNEETIEKYKCIDcIEDLSLNEYHVVHNALKNLNELKRNQSIII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 162 SGESGAGKTVSAKYAMRYFA-TVSGSASEA---------------------NVEEKVLASNPIMESIGNAKTTRNDNSSR 219
Cdd:cd14938 80 SGESGSGKSEIAKNIINFIAyQVKGSRRLPtnlndqeednihneentdyqfNMSEMLKHVNVVMEAFGNAKTVKNNNSSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 220 FGKYIEIGFDKRyRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGV 299
Cdd:cd14938 160 FSKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 300 DDAKEMAHTRQACTLLGISESHQMgIFRILAGILHLGNVGF--------TSRDADSCTIPPKHEP--------------- 356
Cdd:cd14938 239 YSGKILELLKSLNYIFDDDKEIDF-IFSVLSALLLLGNTEIvkafrkksLLMGKNQCGQNINYETilselensediglde 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 357 ----LCIFCDLMGVDYEEMCHWLCHRKLATATeTYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQ---ALHSAVKQ 429
Cdd:cd14938 318 nvknLLLACKLLSFDIETFVKYFTTNYIFNDS-ILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEkctQLQNININ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 430 HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTL-IDFYDNQPCIN-LIESKLGILD 507
Cdd:cd14938 397 TNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNlLVGPTEGSLF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 508 LLDEECKMPKGTDDTwaqKLYNTHLNKCA-----LFEKPRLSN-KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLK 581
Cdd:cd14938 477 SLLENVSTKTIFDKS---NLHSSIIRKFSrnskyIKKDDITGNkKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVK 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 582 SSKFKMLPELFQ----DDEKAISPTSATSSGRTPLtrtpaKPTKGR---PGQMAKEhkktvghQFRNSLHLLMETLNATT 654
Cdd:cd14938 554 QSENEYMRQFCMfynyDNSGNIVEEKRRYSIQSAL-----KLFKRRydtKNQMAVS-------LLRNNLTELEKLQETTF 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 655 PHYVRCIKPNDFK-FPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkqkdvlSDRKQTCKNVLEK 733
Cdd:cd14938 622 CHFIVCMKPNESKrELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKN------EDLKEKVEALIKS 695
|
730
....*....|....*.
gi 2462544153 734 LILDKDKYQFGKTKIF 749
Cdd:cd14938 696 YQISNYEWMIGNNMIF 711
|
|
| Myo5p-like_CBD_DIL_ANK |
cd15473 |
cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ... |
1503-1832 |
4.62e-32 |
|
cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ankyrin domain-containing protein are a group of fungal proteins that contain a domain homologous to the cargo binding domain of class V myosins and ankyrin repeats. Their function is unknown.
Pssm-ID: 271257 [Multi-domain] Cd Length: 316 Bit Score: 128.44 E-value: 4.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1503 LPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNTCRFLHCLKQysgEEGFmkhntsrqne 1582
Cdd:cd15473 32 VPANLLFLCARYAHYHCSPELLEDLLLGALDRIEDVVEANPWDMTLLAFWLSNVTLLLHYLKK---DAGL---------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1583 hcltNFDLAEYRQVLSDLAIQIYQQLVRVLEnilqpmivsgmlehetiqgvsgvkptglrKRTSSIADEGTYTLDSIlrq 1662
Cdd:cd15473 99 ----VEATPEFQQELAELINEIFVLIIRDAE-----------------------------RRIDKLLDASPRNITSL--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1663 LNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLM-------NSGA 1735
Cdd:cd15473 143 LSSTLYVLELYDVHPAIIIQALSQLFYWLGCELFNRILTNKKYLCRSKAMQIRMNLSALEDWARSNNLQpekgespPRIA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1736 KETLEPLIQAAQLLQVKKKTDDDAEAICSM--CNALTTAQIVKVLNLYTP-VNefEERVSVSFIRTIQMRLRDRKDSpql 1812
Cdd:cd15473 223 RSHLAPVIQLLQWLQCLSSLDDFESLIATIqqLDALNPLQLLRAVKDYRYeVN--EGRMPEECVKYLAQLQKDWLDS--- 297
|
330 340
....*....|....*....|
gi 2462544153 1813 lmdaKHIFPVTFPFNPSSLA 1832
Cdd:cd15473 298 ----RYMLPFSLPTDTEMLV 313
|
|
| Myo5p-like_CBD_fungal |
cd15474 |
cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin ... |
1482-1826 |
1.26e-29 |
|
cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin cables, actin filaments that are bundled by fimbrin, in the presence of tropomyosin. This is in contrast to the other vertebrate class V myosins. Like other class V myosins, fungal myosin 2 and 4 contain a C-terminal cargo binding domain. In case of Myo4 it has been shown to bind to the adapter protein She3p (Swi5p-dependent HO expression 3), which in turn anchors myosin 4 to its cargos, zip-coded mRNP (messenger ribonucleoprotein particles) and tER (tubular endoplasmic reticulum). Myo 2 binds to Vac17, vacuole-specific cargo adaptor, and Mmr1, mitochondria-specific cargo adaptor. Both adaptors bind competitivly at the same site.
Pssm-ID: 271258 Cd Length: 352 Bit Score: 122.53 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1482 LVKNLILELKPRGVAVN----LIPGLPAYILFMCVRHADYLNDDQKVRSL--LTSTINSIKKVLKKRgDDFETVSFWLSN 1555
Cdd:cd15474 11 LKSVEVLELKDISDEVSgdnlLFLGHVNFLIYSQMWKSLLELLTQSERFLshVLSYIASIVDSLPKK-ETIPDGAFWLAN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1556 TCRFLHCL--KQYSGEEGFMKHNTSRQNEHCLTNFDlaEYRQVLSdlaiQIYQQLVRVLENILQPMIVSGMLEHETIQGV 1633
Cdd:cd15474 90 LHELRSFVvyLLSLIEHSSSDEFSKESEEYWNTLFD--KTLKHLS----NIYSTWIDKLNKHLSPKIEGAVLVLLTSLDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1634 SGvkptgLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQ 1713
Cdd:cd15474 164 SE-----LIDLNKEFFNKPKKKMADLITFLNEVYDLLQSFSVQPELLNAIVSSTLQYINVEAFNSLITKRSALSWKRGSQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1714 IRYNVSQLEEWLRDKNLmnSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNeFEERVSV 1793
Cdd:cd15474 239 ISYNVSRLKEWCHQHGL--SDANLQLEPLIQASKLLQLRKDDENDFKIILSVCYALNPAQIQKLLDKYQPAN-YEAPVPK 315
|
330 340 350
....*....|....*....|....*....|....
gi 2462544153 1794 SFIRTI-QMRLRDRKDSPQLLMDAKHIFPVTFPF 1826
Cdd:cd15474 316 EFLNALeKLIKKENLSLPGRKNNSKMEIPESSNF 349
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
196-734 |
3.76e-29 |
|
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: 126.78 E-value: 3.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 196 VLASNPIMESIGNAKTTRNDNSSRFGKY--IEIGFDK---RYRIIGANMRTYLLEKSRVVFQA------EEERNYHIFYQ 264
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLhpwEFQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 265 LCASAKLPEF-----KMLRLGNADNFNYTKQGGSP-----VIEGVD----DAKEMAHTRQACTLLGISESHQMGIFRILA 330
Cdd:cd14894 329 MVAGVNAFPFmrllaKELHLDGIDCSALTYLGRSDhklagFVSKEDtwkkDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 331 GILHLGNVGFTSRDADSCTIPPKH------EPLCIFCDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALA 404
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalnapQKVVELLELGSVEKLERMLMTKSVSLQSTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 405 KHIYAKLFNWIVDNVNQALH-----------------SAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQqfnm 467
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEATKmsalstdgnkhqmdsnaSAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYA---- 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 468 hvfKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKLGILDLLdEECKMPKGTDDTWAQ------KLYNTHL---NKCALF 538
Cdd:cd14894 565 ---REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASL-EELTILHQSENMNAQqeekrnKLFVRNIydrNSSRLP 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 539 EKPRLSNKA------------FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLK---SSKF-KMLPELFQDDEKAISPT 602
Cdd:cd14894 641 EPPRVLSNAkrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKtsnSSHFcRMLNESSQLGWSPNTNR 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 603 SATSSGRTPLTRTpakptkgrpgqmakehKKTVGhQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLR 682
Cdd:cd14894 721 SMLGSAESRLSGT----------------KSFVG-QFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCR 783
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462544153 683 ACGV---LETIRISAAGFPS-RWTYQEFFSRYRVLMKQKDVLSDRKQTCKNVLEKL 734
Cdd:cd14894 784 SQRLirqMEICRNSSSSYSAiDISKSTLLTRYGSLLREPYILDDVAGDNSNLMNWL 839
|
|
| fMyo2p_CBD |
cd15480 |
cargo binding domain of fungal myosin 2; Yeast myosin V travels along actin cables, actin ... |
1655-1850 |
4.18e-29 |
|
cargo binding domain of fungal myosin 2; Yeast myosin V travels along actin cables, actin filaments that are bundled by fimbrin, in the presence of tropomyosin. This is in contrast to the other vertebrate class V myosins. Like other class V myosins, fungal myosin 2 and 4 contain a C-terminal cargo binding domain. Myo 2 binds to Vac17, vacuole-specific cargo adaptor, and Mmr1, mitochondria-specific cargo adaptor. Both adaptors bind competitivly at the same site.
Pssm-ID: 271264 Cd Length: 363 Bit Score: 121.15 E-value: 4.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1655 TLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNlMNSG 1734
Cdd:cd15480 167 TMDDILNFFNKVYKSMKSYYIEESVIRQVVTELLKLIGVTAFNDLLMRRNFLSWKRGLQINYNITRLEEWCKSHD-IPEG 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1735 AkETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTpVNEFEERVSVSFIRTIQMRLR--DRKDSPQL 1812
Cdd:cd15480 246 T-LQLEHLMQATKLLQLKKATLEDIEIIYDVCWILTPAQIQKLISQYY-VADYENPISPEILKAVAARVKpeDKSDHLLL 323
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462544153 1813 LMDAKHIFPVTFPFNPSSLALETIqIPASLGLGFISRV 1850
Cdd:cd15480 324 IPLVEEVGPFEDPFPREIAGLEAY-IPAWLNLPHIRRL 360
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
902-1281 |
4.93e-16 |
|
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: 84.72 E-value: 4.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 902 KRELKKLKIEARSVERYKKLHigmeNKIMQLQRKVdeQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVA 981
Cdd:TIGR02168 199 ERQLKSLERQAEKAERYKELK----AELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 982 TGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQekealnhriVQQAKEMTETMEKKLV 1061
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE---------LESKLDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1062 EETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmvhvpkpghKRTDSTHSSNESEYIFSSEI----AEMEDIP 1137
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLE----------TLRSKVAQLELQIASLNNEIerleARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1138 SRTEEPSEKKVPLDMSL----FLKLQKRVTELEQEKQVMQDELDRKEEQvlrskaKEEERPQIRGAELEYESLKRQELES 1213
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLeeaeLKELQAELEELEEELEELQEELERLEEA------LEELREELEEAEQALDAAERELAQL 487
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462544153 1214 ENKK--LKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLV------SQKEAIQ 1281
Cdd:TIGR02168 488 QARLdsLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVvvenlnAAKKAIA 563
|
|
| Myo5p-like_CBD_afadin |
cd15471 |
cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and ... |
1504-1783 |
5.83e-16 |
|
cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and Rap1 small G protein-binding protein, found in cadherin-based adherens junctions in epithelial cells, endothelial cells, and fibroblasts. It interacts with cell adhesion molecules and signaling molecules and plays a role in the formation of cell junctions, cell polarization, migration, survival, proliferation, and differentiation. Afadin is a multi domain protein, that contains beside a myosin5-like CBD, two Ras-associated domains, a forkhead-associated domain, a PDZ domain, three proline-rich domains, and an F-actin-binding domain.
Pssm-ID: 271255 Cd Length: 322 Bit Score: 81.20 E-value: 5.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1504 PAYILFMCVRH---ADYLNDD------QKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNTCRFLHCLKQysgeegfmk 1574
Cdd:cd15471 25 PAYTLYLAARYrlsTHYRPELtpteraHKLTAFLNKIASLIQQVIQEQRNIAGALAFWMANASELLNFLKQ--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1575 hntsrqnEHCLTNFDLaEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSGVKPTglrkrtssiadegTY 1654
Cdd:cd15471 96 -------DRDLSAFSV-QAQDVLAEAVQSAFSYLVRCLQEELERSLPAFLDSLVSLDDEPAIGDV-------------LH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1655 TLDSILRQLNsfhsvmcQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKD--MCSWSKGMQIRYNVSQLEEWLrDKNLMN 1732
Cdd:cd15471 155 TLSSAMRLLR-------RCRVNAALTIQLFSQLFHFINAWLFNSLVSNPDsgLCTRYWGKRLRQRLAHVEAWA-ERQGLE 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2462544153 1733 SGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTP 1783
Cdd:cd15471 227 LAADCHLDRIVQAANLLTAPKYSAEDVANLSSTCFKLNSLQLRALLSHYQP 277
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
957-1231 |
4.16e-13 |
|
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: 75.09 E-value: 4.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 957 YNSETEKLRSDLERLQLSEEEakvatgrvlsLQEEIAKLRKDLEQTRSEkkciEEHADRYKQETEQLVSNLKEENTLLKQ 1036
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAE----------LEKALAELRKELEELEEE----LEQLRKELEELSRQISALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1037 EKEALNHRIVQQAKEMTETMEK---------KLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMvhvpk 1107
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEieeleerleEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL----- 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1108 pGHKRTDSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEKkvpldmslFLKLQKRVTELEQEKQVMQDELDRKEEQvlrsK 1187
Cdd:TIGR02168 816 -NEEAANLRERLESLERRIAATERRLEDLEEQIEELSED--------IESLAAEIEELEELIEELESELEALLNE----R 882
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2462544153 1188 AKEEERPQIRGAELEYESLKRQELESENKKLKNELNELRKALSE 1231
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
902-1281 |
1.23e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.56 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 902 KRELKKLKIEARSVERYKKLHI---------------GMENKIMQLQRKVDEQNKDykclVEKLTNLEGIYNSETEKLRS 966
Cdd:TIGR02169 197 RQQLERLRREREKAERYQALLKekreyegyellkekeALERQKEAIERQLASLEEE----LEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 967 DLErlQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEkkcIEEHADRYKQETEQLVsNLKEENTLLKQEKEALNHRIV 1046
Cdd:TIGR02169 273 LLE--ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERS---IAEKERELEDAEERLA-KLEAEIDKLLAEIEELEREIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1047 QQAKEMTETME--KKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMtlmvhvpkpghkrtdsthssNESEY 1124
Cdd:TIGR02169 347 EERKRRDKLTEeyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI--------------------NELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1125 IFSSEIAEMEDIPSRTEEpsekkvpLDMSLFLKLQKrVTELEQEKQVMQDELDRKEEQVLRSKA-KEEERPQIRGAELEY 1203
Cdd:TIGR02169 407 ELDRLQEELQRLSEELAD-------LNAAIAGIEAK-INELEEEKEDKALEIKKQEWKLEQLAAdLSKYEQELYDLKEEY 478
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462544153 1204 eslkrQELESENKKLKNELNELRKalsEKSAPEVTAPGAPAyrvlmeqltsVSEELDVRKEEVLILRSQLVSQKEAIQ 1281
Cdd:TIGR02169 479 -----DRVEKELSKLQRELAEAEA---QARASEERVRGGRA----------VEEVLKASIQGVHGTVAQLGSVGERYA 538
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
902-1280 |
3.11e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 902 KRELKKLKIEARSVERYKKLHIGMEnkimqlQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVA 981
Cdd:COG1196 199 ERQLEPLERQAEKAERYRELKEELK------ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 982 TGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEentlLKQEKEALNHRIVQQAKEMTETMEKKLV 1061
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE----LEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1062 EETK--QLELDLNDERLRYQNLLNEFSRLEERYDDLKEEmtlmvhvpkpghkrtdsthssneseyiFSSEIAEMEDIPSR 1139
Cdd:COG1196 349 AEEEleEAEAELAEAEEALLEAEAELAEAEEELEELAEE---------------------------LLEALRAAAELAAQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1140 TEEPSEKKvpldmslfLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEErpqiRGAELEYESLKRQELESENKKLK 1219
Cdd:COG1196 402 LEELEEAE--------EALLERLERLEEELEELEEALAELEEEEEEEEEALEE----AAEEEAELEEEEEALLELLAELL 469
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462544153 1220 NELNELRKALSEKSAPEVTApgAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAI 1280
Cdd:COG1196 470 EEAALLEAALAELLEELAEA--AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
942-1439 |
3.31e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 942 DYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKqETE 1021
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-ELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1022 QLVSNLKEENTLLKQEKEALNHRIVQqakemTETMEKKLVEETKQLEldlndERLRYqnlLNEFSRLEERYDDLKEEMTL 1101
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRE-----LEERIEELKKEIEELE-----EKVKE---LKELKEKAEEYIKLSEFYEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1102 MVHVPKPGHKRTDSTHSSNESeyiFSSEIAEMEDIPSRTEEPSEKKVpldmslflKLQKRVTELEQEKQVMQDELDRKEE 1181
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEING---IEERIKELEEKEERLEELKKKLK--------ELEKRLEELEERHELYEEAKAKKEE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1182 -QVLRSKAKEEERPQIRgAELEYESLKRQELESENKK-------LKNELNELRKALSEKSAPEVTAP--GAP-------- 1243
Cdd:PRK03918 374 lERLKKRLTGLTPEKLE-KELEELEKAKEEIEEEISKitarigeLKKEIKELKKAIEELKKAKGKCPvcGRElteehrke 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1244 ---AYRVLMEQLTSVSEELDVRKEEVLI----LRSQLVSQKEAIQPKnTMTDSTILLEDVQKMKDKGEIAQA---YIGLK 1313
Cdd:PRK03918 453 lleEYTAELKRIEKELKEIEEKERKLRKelreLEKVLKKESELIKLK-ELAEQLKELEEKLKKYNLEELEKKaeeYEKLK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1314 ETNRLLESQLQSQKRS------HENEAEALRGEIQSLKEEnnrqqqllaqnlqlppeariEASLQHEITRLTNENLYFEE 1387
Cdd:PRK03918 532 EKLIKLKGEIKSLKKElekleeLKKKLAELEKKLDELEEE--------------------LAELLKELEELGFESVEELE 591
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2462544153 1388 LYADDPKKYQSYRISLYKRMIDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1439
Cdd:PRK03918 592 ERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
901-1440 |
1.17e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.09 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 901 AKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGiynsETEKLRSDLERL--------Q 972
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELRE----ELEKLEKEVKELeelkeeieE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 973 LSEEEAKVaTGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQ-----ETEQLVSNLKEENTLLKQEKEALNHRIVQ 1047
Cdd:PRK03918 243 LEKELESL-EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaEEYIKLSEFYEEYLDELREIEKRLSRLEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1048 QAKEMtetmeKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPKpghkrtdstHSSNESEYIFS 1127
Cdd:PRK03918 322 EINGI-----EERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELER---------LKKRLTGLTPE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1128 SEIAEMEDIPSRTEEPSEKkvpldmslFLKLQKRVTELEQEKQVMQDELDRKEEQ-----VLRSKAKEEERPQIRG---A 1199
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEE--------ISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEeytA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1200 ELEYESLKRQELESENKKLKNELNELRKALSEKsaPEVTapgapAYRVLMEQLTSVSEELDVR---------------KE 1264
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKE--SELI-----KLKELAEQLKELEEKLKKYnleelekkaeeyeklKE 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1265 EVLILRSQLVSQKEAIQPKNTMTDSTILLEdvqKMKDKGEIAQAYIgLKETNRL-------LESQLQSQKRSH------- 1330
Cdd:PRK03918 533 KLIKLKGEIKSLKKELEKLEELKKKLAELE---KKLDELEEELAEL-LKELEELgfesveeLEERLKELEPFYneylelk 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1331 --ENEAEALRGEIQSLKEENNRQQQLLAQNlqlppEARIEaSLQHEITRLtnENLYFEELYADDPKKYQSYRiSLYKRMI 1408
Cdd:PRK03918 609 daEKELEREEKELKKLEEELDKAFEELAET-----EKRLE-ELRKELEEL--EKKYSEEEYEELREEYLELS-RELAGLR 679
|
570 580 590
....*....|....*....|....*....|....*.
gi 2462544153 1409 DLMEQLEKQ----DKTVRKLKKQLKVFAKKIGELEV 1440
Cdd:PRK03918 680 AELEELEKRreeiKKTLEKLKEELEEREKAKKELEK 715
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
898-1433 |
1.89e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.24 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 898 RMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYnSETEKLRSDLERLQLSEEE 977
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV-KELEELKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 978 AKvatGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQ-----ETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEM 1052
Cdd:PRK03918 250 LE---GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1053 tetmeKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPKpghkrtdstHSSNESEYIFSSEIAE 1132
Cdd:PRK03918 327 -----EERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELER---------LKKRLTGLTPEKLEKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1133 MEDIPSRTEEPSEKkvpldmslFLKLQKRVTELEQEKQVMQDELDRKEEQ-----VLRSKAKEEERPQIRG---AELEYE 1204
Cdd:PRK03918 393 LEELEKAKEEIEEE--------ISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEeytAELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1205 SLKRQELESENKKLKNELNELRKALSEKsaPEVTApgapaYRVLMEQLTSVSEELDVR---------------KEEVLIL 1269
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKE--SELIK-----LKELAEQLKELEEKLKKYnleelekkaeeyeklKEKLIKL 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1270 RSQLVSQKEAIQPKNTMTDSTILL---------------------------EDVQKMKDKGEIAQAYIGLKETNRLLESQ 1322
Cdd:PRK03918 538 KGEIKSLKKELEKLEELKKKLAELekkldeleeelaellkeleelgfesveELEERLKELEPFYNEYLELKDAEKELERE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1323 LQSQKRShENEAEALRGEIQSLKEENNRQqqllaqnlqlppEARIEASL----QHEITRLTNENLYFEELYA---DDPKK 1395
Cdd:PRK03918 618 EKELKKL-EEELDKAFEELAETEKRLEEL------------RKELEELEkkysEEEYEELREEYLELSRELAglrAELEE 684
|
570 580 590
....*....|....*....|....*....|....*...
gi 2462544153 1396 YQSYRISLYKRMIDLMEQLEKQDKTVRKLKKQLKVFAK 1433
Cdd:PRK03918 685 LEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALER 722
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
902-1209 |
3.15e-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: 65.47 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 902 KRELKKLKIEARS-VERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLE-GIYNSETE--KLRSDLERLQ----- 972
Cdd:TIGR02169 697 LRRIENRLDELSQeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEqEIENVKSElkELEARIEELEedlhk 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 973 ----LSEEEAKVATGRVLSLQEEIAKLRK----------DLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEK 1038
Cdd:TIGR02169 777 leeaLNDLEARLSHSRIPEIQAELSKLEEevsriearlrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1039 EALNHRivqqaKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPKpghkrtdsthS 1118
Cdd:TIGR02169 857 ENLNGK-----KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS----------E 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1119 SNESEYIFSSEIAEMEDIPSRTEEPSEKKVPLDmslflKLQKRVTELEQEKQVMQ-------DELDRKEEQVLRSKAK-- 1189
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGEDEEIPEEELSLE-----DVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKra 996
|
330 340
....*....|....*....|..
gi 2462544153 1190 --EEERPQIRGAELEYESLKRQ 1209
Cdd:TIGR02169 997 klEEERKAILERIEEYEKKKRE 1018
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
924-1347 |
4.12e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 924 GMENKIMQLQRKVDEqnKDYKCLVEKLTNLEgiynSETEKLRSDLERLQLSEEEAKVATG--------------RVLSLQ 989
Cdd:PRK02224 184 DQRGSLDQLKAQIEE--KEEKDLHERLNGLE----SELAELDEEIERYEEQREQARETRDeadevleeheerreELETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 990 EEIAKLRKDLEQTRSEKkciEEHADRYKQETEQLvSNLKEENT--LLKQEKEALNHRIVQQAKEmteTMEKKLVEetkqL 1067
Cdd:PRK02224 258 AEIEDLRETIAETERER---EELAEEVRDLRERL-EELEEERDdlLAEAGLDDADAEAVEARRE---ELEDRDEE----L 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1068 ELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmvhvpkpgHKRTDSTHSSNESEyifsseiAEMEDIPSRTEEPSEkk 1147
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAESLREDADDLEERAE---------ELREEAAELESELE-------EAREAVEDRREEIEE-- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1148 vpldmslflkLQKRVTELEQEKQVMQDELDRKEEqvlRSKAKEEERPQIRGaeleyeslKRQELESENKKLKNELNELRK 1227
Cdd:PRK02224 389 ----------LEEEIEELRERFGDAPVDLGNAED---FLEELREERDELRE--------REAELEATLRTARERVEEAEA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1228 ALSEKSAPEVTAPGAPAYRVlmeqltSVSEELDVRKEEVLILRSQLVSQKEAIQPKNTMTDSTILLED-VQKMKDKGEIA 1306
Cdd:PRK02224 448 LLEAGKCPECGQPVEGSPHV------ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDrIERLEERREDL 521
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2462544153 1307 QAYIGLKET----NRLLESQLQSQKRSHENEAEALRGEIQSLKEE 1347
Cdd:PRK02224 522 EELIAERREtieeKRERAEELRERAAELEAEAEEKREAAAEAEEE 566
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
896-1437 |
9.94e-10 |
|
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: 63.61 E-value: 9.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 896 FRRMMAKRELKKLKIEarsverYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQL-- 973
Cdd:pfam05557 9 ARLSQLQNEKKQMELE------HKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 974 ----------SEEEAKVATGR--VLSLQEEIAKLRK-------DLEQTRSEKKCIEEHADRYK---QETEQLVSNLKEEN 1031
Cdd:pfam05557 83 kylealnkklNEKESQLADARevISCLKNELSELRRqiqraelELQSTNSELEELQERLDLLKakaSEAEQLRQNLEKQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1032 TLLK---QEKEALNHRIVQQA--KEMTETMEKKLVEETkqlELDLNDERLRYQN-LLNEFSR----LEERYDDLKEEMtl 1101
Cdd:pfam05557 163 SSLAeaeQRIKELEFEIQSQEqdSEIVKNSKSELARIP---ELEKELERLREHNkHLNENIEnkllLKEEVEDLKRKL-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1102 mvhvpkpghkrtdsthssnESEYIFSSEIAEMEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEE 1181
Cdd:pfam05557 238 -------------------EREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1182 Q-VLRSKAKEEERpqirgaeleyeslKRQELESENKKLKNELNELRKALSEKSApevtapgapAYRVLMEQLTSVSEELD 1260
Cdd:pfam05557 299 NsSLTSSARQLEK-------------ARRELEQELAQYLKKIEDLNKKLKRHKA---------LVRRLQRRVLLLTKERD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1261 VRKEEVLILRSQLVSQKEAIQPKNTMTDSTILLEDVQ----KMKDKGEIAQAYIG-LKETNRLLESQLQSQKR------- 1328
Cdd:pfam05557 357 GYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQahneEMEAQLSVAEEELGgYKQQAQTLERELQALRQqesladp 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1329 -SHENEAEALRGEIQSLKEENNRQQQLLAQNlqlppEARIE----------------------------------ASLQH 1373
Cdd:pfam05557 437 sYSKEEVDSLRRKLETLELERQRLREQKNEL-----EMELErrclqgdydpkktkvlhlsmnpaaeayqqrknqlEKLQA 511
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462544153 1374 EITRLTNENLYFEELYADDPKKYQSYRISLYKRMIDLMEQLEKQDKTVRKLKkqlKVFAKKIGE 1437
Cdd:pfam05557 512 EIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQRLK---EVFQAKIQE 572
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
957-1347 |
1.73e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.16 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 957 YNSETEKLRSDLERLQLSEEEakvatgrvlsLQEEIAKLRKDLEQTRSEKkcieEHADRYKQeteqLVSNLKE-ENTLLK 1035
Cdd:TIGR02169 168 FDRKKEKALEELEEVEENIER----------LDLIIDEKRQQLERLRRER----EKAERYQA----LLKEKREyEGYELL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1036 QEKEALNHRIVQQAKEMTEtmekkLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHvpkpghKRTDS 1115
Cdd:TIGR02169 230 KEKEALERQKEAIERQLAS-----LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK------EKIGE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1116 THSsneseyifssEIAEMEDIPSRTEEPSEKkvpldmslfLKLQKRVTELEQEKQVMQ-DELDRKEEQVLRSKAKEEERP 1194
Cdd:TIGR02169 299 LEA----------EIASLERSIAEKERELED---------AEERLAKLEAEIDKLLAEiEELEREIEEERKRRDKLTEEY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1195 QIRGAELEYESLKRQELESENKKLKNELNELRKALSEksapevtapgapayrvLMEQLTSVSEELDVRKEEVLILRSQLV 1274
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK----------------LKREINELKRELDRLQEELQRLSEELA 423
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462544153 1275 SQKEAIqpkntmtdsTILLEDVQKMKDKGEIAQAYIGLKETNRlleSQLQSQKRSHENEAEALRGEIQSLKEE 1347
Cdd:TIGR02169 424 DLNAAI---------AGIEAKINELEEEKEDKALEIKKQEWKL---EQLAADLSKYEQELYDLKEEYDRVEKE 484
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
900-1232 |
2.43e-09 |
|
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: 62.68 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 900 MAKRELKKLKIEARSVERYKKLHIGMEN-KIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEA 978
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEELKKLKLEAEElLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 979 KvatgrvlSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEalnhrivqQAKEMTETMEK 1058
Cdd:pfam02463 774 K-------ELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQE--------EKIKEEELEEL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1059 KLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRTDSTHSSNESEYIFSSEIAEMEDIPS 1138
Cdd:pfam02463 839 ALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1139 RTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAELEYESLK--RQELESENK 1216
Cdd:pfam02463 919 IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEerYNKDELEKE 998
|
330
....*....|....*.
gi 2462544153 1217 KLKNELNELRKALSEK 1232
Cdd:pfam02463 999 RLEEEKKKLIRAIIEE 1014
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
904-1302 |
2.52e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 904 ELKKLKIEARSVERYKKlHIGMENKIMQLQRKVDEQNK--DYKCLVEKLTNLEGIYNSETEKLRSDleRLQLSEEEAKVA 981
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKK-KAEEKKKADEAKKKAEEAKKadEAKKKAEEAKKAEEAKKKAEEAKKAD--EAKKKAEEAKKA 1485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 982 TgRVLSLQEEIAKLRKDLEQTRSEKKCIEE--HADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTETMEKK 1059
Cdd:PTZ00121 1486 D-EAKKKAEEAKKKADEAKKAAEAKKKADEakKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK 1564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1060 LVEETKQLELDLNDERLRYQNLLN-EFSRLEERYDDLKEEMTLMVHVPKpghkrtdsthsSNESEYIFSSEIAEMEDIPS 1138
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAK-----------KAEEAKIKAEELKKAEEEKK 1633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1139 RTEEPSEKKVPLdmslfLKLQKRVTELEQEKQVMQDELDRKEEQVLRS-----KAKEEERPQIRGAELEYESLKRQEles 1213
Cdd:PTZ00121 1634 KVEQLKKKEAEE-----KKKAEELKKAEEENKIKAAEEAKKAEEDKKKaeeakKAEEDEKKAAEALKKEAEEAKKAE--- 1705
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1214 ENKKLKNElnELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILrSQLVSQKEAIQPKNTMTDSTILL 1293
Cdd:PTZ00121 1706 ELKKKEAE--EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI-AHLKKEEEKKAEEIRKEKEAVIE 1782
|
....*....
gi 2462544153 1294 EDVQKMKDK 1302
Cdd:PTZ00121 1783 EELDEEDEK 1791
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
902-1381 |
6.96e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 6.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 902 KRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVA 981
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 982 TGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTETMEKKLV 1061
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1062 EETKQLELDLNDERLryQNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRTDSTHSSNESEyifssEIAEMEDIPSRTE 1141
Cdd:COG1196 465 LAELLEEAALLEAAL--AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG-----AVAVLIGVEAAYE 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1142 EPsekkvpLDMSLFLKLQKRVTELEQE-KQVMQDELDRKEEQV--LRSKAKEEERPQIRGAELEYESLKRQELESENKKL 1218
Cdd:COG1196 538 AA------LEAALAAALQNIVVEDDEVaAAAIEYLKAAKAGRAtfLPLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1219 KNELNELRKALSEKSAPEVTAPGAPAYRV-LMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKNTMTDSTILLEDVQ 1297
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVtLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1298 KMKDKGEIAQAYIGLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQHEITR 1377
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
....
gi 2462544153 1378 LTNE 1381
Cdd:COG1196 772 LERE 775
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
903-1439 |
7.47e-09 |
|
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: 60.80 E-value: 7.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 903 RELKKLKieaRSVERYKKLhigMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGiYNSETEKLRSDLERLqlsEEEAKVAT 982
Cdd:TIGR04523 162 NDLKKQK---EELENELNL---LEKEKLNIQKNIDKIKNKLLKLELLLSNLKK-KIQKNKSLESQISEL---KKQNNQLK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 983 GRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNhrivqQAKEMTETMEKKLVE 1062
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN-----QLKSEISDLNNQKEQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1063 E-TKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMvhvpkpghkRTDSTHSSNESEYIfSSEIAEMED-IPSRT 1140
Cdd:TIGR04523 307 DwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL---------KKELTNSESENSEK-QRELEEKQNeIEKLK 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1141 EEPSEKKvpldmslflklqKRVTELEQEKQVMQDELDRKEEQvlrSKAKEEerpQIRGAELEYESLKR--QELESENKKL 1218
Cdd:TIGR04523 377 KENQSYK------------QEIKNLESQINDLESKIQNQEKL---NQQKDE---QIKKLQQEKELLEKeiERLKETIIKN 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1219 KNELNELRKalsEKSAPEVTAPGAPAYR-VLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIqpkNTMTDSTILLEdvQ 1297
Cdd:TIGR04523 439 NSEIKDLTN---QDSVKELIIKNLDNTReSLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL---KKLNEEKKELE--E 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1298 KMKD-KGEIAQayigLKETnrllESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQlppEARIEaSLQHEIT 1376
Cdd:TIGR04523 511 KVKDlTKKISS----LKEK----IEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEK---NKEIE-ELKQTQK 578
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462544153 1377 RLTNENLYFEELYaddpKKYQsyrislyKRMIDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1439
Cdd:TIGR04523 579 SLKKKQEEKQELI----DQKE-------KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
856-1429 |
7.90e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 7.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 856 RYRKILREHKAVIIQKRVRGWLARTHYKRSMHAIIylqccfrrmmAKRELKKLKIEARSVERYKKLHIgMENKIMQLQRK 935
Cdd:COG1196 214 RYRELKEELKELEAELLLLKLRELEAELEELEAEL----------EELEAELEELEAELAELEAELEE-LRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 936 VDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADR 1015
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1016 YKQETEQLVSNLKEENTLLKQEKEAlnhrivQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDL 1095
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEE------LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1096 KEEmtlmvhvpkpgHKRTDSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEKKvpLDMSLFLKLQKRVTELEQEKQvMQDE 1175
Cdd:COG1196 437 EEE-----------EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA--ALAELLEELAEAAARLLLLLE-AEAD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1176 LDRKEEQVLRSKAKEEERP------QIRGAELEYESL---------------------KRQELESENKKLKNELNELRKA 1228
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGlagavaVLIGVEAAYEAAleaalaaalqnivveddevaaAAIEYLKAAKAGRATFLPLDKI 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1229 LSEKSAPEVTAPGAPAYRVLMEQLTSVSEELdVRKEEVLILRSQLVSQKEAIQPKNTMTDSTILLEDVQKMKDKGEIAQA 1308
Cdd:COG1196 583 RARAALAAALARGAIGAAVDLVASDLREADA-RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1309 YIGLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNENLYFEEL 1388
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2462544153 1389 YADDpkkyqSYRISLYKRMIDLMEQLEKQDKTVRKLKKQLK 1429
Cdd:COG1196 742 LEEE-----ELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
917-1439 |
4.09e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.49 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 917 RYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLR 996
Cdd:TIGR04523 23 GYKNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 997 KDLEQTRSEKKcieehadrykqETEQLVSNLKEENTLLKQEKEALNHRIvqqakemtetmeKKLVEETKQLELDLNDERL 1076
Cdd:TIGR04523 103 SDLSKINSEIK-----------NDKEQKNKLEVELNKLEKQKKENKKNI------------DKFLTEIKKKEKELEKLNN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1077 RYQNLLNEFSRLEERYDDLKEEMTlmvhvpKPGHKRTDSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEKKvpldmSLFL 1156
Cdd:TIGR04523 160 KYNDLKKQKEELENELNLLEKEKL------NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELK-----KQNN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1157 KLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEE---RPQIRGAELEYESLKRQELESENKKLKNELNELRKalsEKS 1233
Cdd:TIGR04523 229 QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKikkQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN---QKE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1234 ApevtapgapayrvlmEQLTSVSEELDVRKEEVLILRSQLVSQKEAI--------QPKNTMTDSTI--------LLEDVQ 1297
Cdd:TIGR04523 306 Q---------------DWNKELKSELKNQEKKLEEIQNQISQNNKIIsqlneqisQLKKELTNSESensekqreLEEKQN 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1298 KMKDKGEIAQAYiglKETNRLLESQ---LQSQKRSHENEAEALRGEIQSLKEENNRQqqllaqnlqlppEARIE------ 1368
Cdd:TIGR04523 371 EIEKLKKENQSY---KQEIKNLESQindLESKIQNQEKLNQQKDEQIKKLQQEKELL------------EKEIErlketi 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462544153 1369 ASLQHEITRLTNENLYFEELYA--DDPKKYQSYRISLYKRMIDLMEQ-LEKQDKTVRKLKKQLKVFAKKIGELE 1439
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSVKELIIKnlDNTRESLETQLKVLSRSINKIKQnLEQKQKELKSKEKELKKLNEEKKELE 509
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
992-1291 |
4.62e-08 |
|
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: 58.21 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 992 IAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKE---ALNHRIVQQAKEMTETMEK-KLVEETKQL 1067
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKArqaEMDRQAAIYAEQERMAMEReRELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1068 ELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRTDSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEKK 1147
Cdd:pfam17380 357 ERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1148 VPLDMSLFLKLQKRVTELEQEKQ-----VMQDELDRKEEQVLRSKAK------EEERPQIrgAELEYESLKRQELESENK 1216
Cdd:pfam17380 437 VRRLEEERAREMERVRLEEQERQqqverLRQQEEERKRKKLELEKEKrdrkraEEQRRKI--LEKELEERKQAMIEEERK 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1217 K--LKNELNELRKALSEKSAPEV------TAPGAPAYRVLMEQLTSVSEE---LDVRKEEVLILRSQLVSQKEAIQPKNT 1285
Cdd:pfam17380 515 RklLEKEMEERQKAIYEEERRREaeeerrKQQEMEERRRIQEQMRKATEErsrLEAMEREREMMRQIVESEKARAEYEAT 594
|
....*.
gi 2462544153 1286 MTDSTI 1291
Cdd:pfam17380 595 TPITTI 600
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
897-1481 |
5.08e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 897 RRMMAKRELKklkiEARSVERYKKLHigmENKIMQLQRKVDEQNKDYKCL--VEKLTNLEGIYNSETEKLRSDLERLQLS 974
Cdd:PTZ00121 1200 RKAEAARKAE----EERKAEEARKAE---DAKKAEAVKKAEEAKKDAEEAkkAEEERNNEEIRKFEEARMAHFARRQAAI 1272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 975 EEEAKVATGRVLSLQE--EIAKLRKDLEQTRSE--KKCIEE--HADRYKQETEQL---VSNLKEENTLLKQEKEALNHRI 1045
Cdd:PTZ00121 1273 KAEEARKADELKKAEEkkKADEAKKAEEKKKADeaKKKAEEakKADEAKKKAEEAkkkADAAKKKAEEAKKAAEAAKAEA 1352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1046 VQQAKEMTETMEKKLVEETKQLELDLNDERLRYQnlLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRTDSTHSSNESEyi 1125
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK--AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE-- 1428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1126 fssEIAEMEDIPSRTEE----------PSEKKVPLDMSLFLKLQKRVTELEQ--EKQVMQDELDRKEEQVLR----SKAK 1189
Cdd:PTZ00121 1429 ---EKKKADEAKKKAEEakkadeakkkAEEAKKAEEAKKKAEEAKKADEAKKkaEEAKKADEAKKKAEEAKKkadeAKKA 1505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1190 EEERPQIRGAELEYESLKRQELESENKKLKNElnELRKALSEKSAPEVTAPgapayrvlmEQLTSVSEELDV---RKEE- 1265
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKAD--EAKKAEEKKKADELKKA---------EELKKAEEKKKAeeaKKAEe 1574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1266 ---VLILRSQLVSQKEAIQPKNTMTdstiLLEDVQKMK-------DKGEIAQAYIGLKETNRLLESQLQSQKRSHENEAE 1335
Cdd:PTZ00121 1575 dknMALRKAEEAKKAEEARIEEVMK----LYEEEKKMKaeeakkaEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1336 ALRGEiqslKEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNENLYFEELYADDPKKYQSYRISLYKRMIDLMEQLE 1415
Cdd:PTZ00121 1651 ELKKA----EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462544153 1416 KQDKTVRKLKKQLKVFAKKIGELEVGQMENISPGQIIDEPIRPVNIPRKEKDFQGMLEYKKEDEQK 1481
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKR 1792
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
900-1273 |
6.81e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 6.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 900 MAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYN-----SETEKLRSDLERLQLS 974
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 975 EEEAKVATGRVLSLQEEIAKLRKDLEQTRSEkkcIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTE 1054
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEE---LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1055 TMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVP---------------------KPGHKRT 1113
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvlgllallflllarekASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1114 DSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEER 1193
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1194 PQIRGAELEYEslKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQL 1273
Cdd:COG4717 385 EELRAALEQAE--EYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL 462
|
|
| Myo5p-like_CBD_Rasip1 |
cd15472 |
cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 ... |
1504-1783 |
1.27e-07 |
|
cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 (Rasip1 or RAIN) is an effector of the small G protein Rap1 and plays an important role in endothelial junction stabilization. Rasip1, like afadin, is a multi domain protein, that contains beside a myosin5-like CBD, a Ras-associated domain and a PDZ domain.
Pssm-ID: 271256 Cd Length: 366 Bit Score: 55.74 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1504 PAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVL----KKRGD---------------------DFETVSFWLSNTCR 1558
Cdd:cd15472 25 PAFLLCLCIQHSATHFEPGHFGKLLLKIAKRIQEIVwektKELAEkqpehqdpaslsllsiaelapDLQPLLFWMSNSIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1559 FLHCLKQ----YSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmIVSGMLE-----HET 1629
Cdd:cd15472 105 LLYFIQQkvplYEQSMEEELDVGSKESLLSSTLTASEEAMTVLEEVIMYTFQQCVYYLTKTLYV-ALPALLDsnpftAEE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1630 IQGVSG--VKPTGLRkRTSSIADEgtyTLDsILRQLnsfhsvmCQHgmdPELIKQVVKQMFYIIGAITLNNLLLRKDMCS 1707
Cdd:cd15472 184 RESWSGgsRLPEGVR-RVLEIYQA---TLD-LLRQY-------QVH---PEIASQMFAYLFFFSNASLFNQLMEKGSGGG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1708 ---WSKGMQIRYNVSQLEEWLRDKNLmNSGAKETLEPLIQAAQLLQVKKKTDDDAE--AICSMCNALTTAQIVKVLNLYT 1782
Cdd:cd15472 249 ffqWSRGVQIRANLDLLLDWLQGAGL-GDLAEEFFRKLSSTVNLLATPKEQLLQMSwsSLRAEFPALNPAQLHHLLRQYQ 327
|
.
gi 2462544153 1783 P 1783
Cdd:cd15472 328 L 328
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
898-1336 |
1.41e-07 |
|
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: 56.90 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 898 RMMAKRELKKLKIEAR-----SVERYKKLHIGMENKIMQLQRKVDEQNK---DYKCLVEKLTNLEGIYNSETEKLRSDLE 969
Cdd:TIGR00618 415 RTSAFRDLQGQLAHAKkqqelQQRYAELCAAAITCTAQCEKLEKIHLQEsaqSLKEREQQLQTKEQIHLQETRKKAVVLA 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 970 RLQLSEEEAK--------------------VATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETE-------- 1021
Cdd:TIGR00618 495 RLLELQEEPCplcgscihpnparqdidnpgPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQeiqqsfsi 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1022 --QLVSNLKEENTLLKQEKEALNHRIVQQAKEmtetmEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYddlKEEM 1099
Cdd:TIGR00618 575 ltQCDNRSKEDIPNLQNITVRLQDLTEKLSEA-----EDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA---LKLT 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1100 TLmvhvpkpgHKRTDSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEKKvpldmSLFLKLQKRVTELEQekqvmQDELDRK 1179
Cdd:TIGR00618 647 AL--------HALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQ-----SEKEQLTYWKEMLAQ-----CQTLLRE 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1180 EEQVLrskakEEERPQIRGAELEYESLKrQELESENKKLKNELNELRKALSEK-----SAPEVTAPGAPAYRVLMEQLTS 1254
Cdd:TIGR00618 709 LETHI-----EEYDREFNEIENASSSLG-SDLAAREDALNQSLKELMHQARTVlkartEAHFNNNEEVTAALQTGAELSH 782
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1255 VSEELDVRKEEVLILRSQLVSQKEAIQPKNTMTDSTILLEDVQKMKDK--------------GEIAQAYIGLKETNRLLE 1320
Cdd:TIGR00618 783 LAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEeqflsrleeksatlGEITHQLLKYEECSKQLA 862
|
490
....*....|....*.
gi 2462544153 1321 SQLQSQKRSHENEAEA 1336
Cdd:TIGR00618 863 QLTQEQAKIIQLSDKL 878
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
928-1259 |
2.46e-07 |
|
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: 56.23 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 928 KIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLrSDLERlQLSEEEAkvatgRVLSLQEEIAKLRKDLEQTRSEKK 1007
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL-SDASR-KIGEIEK-----EIEQLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1008 CIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNH----------RIVQQAKEMTETMEKKLVEETKQLELDLNDERLR 1077
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1078 YQNLLNEFSRLEERYDDLKEEMtlmvhvpkpghkrtdsthssneseyifSSEIAEMEDIPSRTEEPSEKkvpldmslFLK 1157
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQI---------------------------KSIEKEIENLNGKKEELEEE--------LEE 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1158 LQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEErpqirgAELEYEsLKRQELESENKKLKNELNELRKALSEKSAPEV 1237
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEE------LEAQIE-KKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
330 340
....*....|....*....|..
gi 2462544153 1238 TAPGAPAYRVLMEQLTSVSEEL 1259
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRVEEEI 967
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
911-1345 |
2.59e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.89 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 911 EARSVERYKKLHIGMENKIMQLQRKvdEQNKDYKClveKLTNLEgiynSETEKLRSDLErlqlseEEAKVATGRVLSLQE 990
Cdd:pfam15921 285 EKASSARSQANSIQSQLEIIQEQAR--NQNSMYMR---QLSDLE----STVSQLRSELR------EAKRMYEDKIEELEK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 991 EIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEAlNHRIVQQAKEMTETMEkklveetkQLELD 1070
Cdd:pfam15921 350 QLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQ-NKRLWDRDTGNSITID--------HLRRE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1071 LNDERLRYQnllnefsRLEERYDDLKEEMTLMVhvpkpgHKRTDSTHSSNESEYIFSSEIAEMEDIPSR----TEEPSEK 1146
Cdd:pfam15921 421 LDDRNMEVQ-------RLEALLKAMKSECQGQM------ERQMAAIQGKNESLEKVSSLTAQLESTKEMlrkvVEELTAK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1147 KVPLDMS------LFLKLQKRVTELE---QEKQVMQDELDRKEEQVLRSKAKEEerpQIRGAELEYESLK---------- 1207
Cdd:pfam15921 488 KMTLESSertvsdLTASLQEKERAIEatnAEITKLRSRVDLKLQELQHLKNEGD---HLRNVQTECEALKlqmaekdkvi 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1208 ---RQELES-----------------ENKKLKNELNELR------KALSEKSAPEVTAPGAPAYRVLMEQLTSV---SEE 1258
Cdd:pfam15921 565 eilRQQIENmtqlvgqhgrtagamqvEKAQLEKEINDRRlelqefKILKDKKDAKIRELEARVSDLELEKVKLVnagSER 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1259 L----DVRKEevlilRSQLVSQKeaiqpKNTMTDSTILLEDVQKMKdkgeiaQAYIGLKETNRLLESQLQSQKRSHENEA 1334
Cdd:pfam15921 645 LravkDIKQE-----RDQLLNEV-----KTSRNELNSLSEDYEVLK------RNFRNKSEEMETTTNKLKMQLKSAQSEL 708
|
490
....*....|.
gi 2462544153 1335 EALRGEIQSLK 1345
Cdd:pfam15921 709 EQTRNTLKSME 719
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
904-1483 |
4.80e-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: 55.11 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 904 ELKKLKIEARSVERYKKLHIGMENKIMQLQRK---------------VDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDL 968
Cdd:pfam05483 89 KIKKWKVSIEAELKQKENKLQENRKIIEAQRKaiqelqfenekvslkLEEEIQENKDLIKENNATRHLCNLLKETCARSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 969 ERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTR--SEKKCIEEHAdRYKQETEQlVSNLKEENTLLKQEKEALNHRIV 1046
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRvqAENARLEMHF-KLKEDHEK-IQHLEEEYKKEINDKEKQVSLLL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1047 QQAKEMTETMEKK--LVEETKQLELDLNDE-RLRYQNLlnefSRLEERYDDLKEEMTLMvhvpKPGHKRTDSTHSSNESE 1123
Cdd:pfam05483 247 IQITEKENKMKDLtfLLEESRDKANQLEEKtKLQDENL----KELIEKKDHLTKELEDI----KMSLQRSMSTQKALEED 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1124 Y-IFSSEIAEM-EDIPSRTEEPSEKKVPLDMSlflklqkrVTELEQEKQVMQdELDRKEEQVLRskaKEEERPQIRGAEL 1201
Cdd:pfam05483 319 LqIATKTICQLtEEKEAQMEELNKAKAAHSFV--------VTEFEATTCSLE-ELLRTEQQRLE---KNEDQLKIITMEL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1202 EYESLKRQELESENKKLKNELNELRKALSEKsapEVTAPGAPAYRVLMEQLTSVSEE----LDVRKEEVLILRSQLVSQK 1277
Cdd:pfam05483 387 QKKSSELEEMTKFKNNKEVELEELKKILAED---EKLLDEKKQFEKIAEELKGKEQEliflLQAREKEIHDLEIQLTAIK 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1278 EAIQPKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETNRLLES------QLQSQKRSHEN---EAEALRGEIQSLKEEN 1348
Cdd:pfam05483 464 TSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEasdmtlELKKHQEDIINckkQEERMLKQIENLEEKE 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1349 NRQQQLLAQNLQLPPEARIEASLQHEITRLTNENLYFEELYADDPKKYQSYRISLYKRMID----LMEQLEKQDKTVRKL 1424
Cdd:pfam05483 544 MNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEnknkNIEELHQENKALKKK 623
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462544153 1425 ----KKQLKVFAKKIGELEvgqMENISPGQIIDEPIrpvniprkeKDFQGMLEYKKEDEQKLV 1483
Cdd:pfam05483 624 gsaeNKQLNAYEIKVNKLE---LELASAKQKFEEII---------DNYQKEIEDKKISEEKLL 674
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
896-1258 |
5.25e-07 |
|
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: 54.74 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 896 FRRMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNS----ETEKLRS----- 966
Cdd:pfam17380 293 FEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEerkrELERIRQeeiam 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 967 ------DLERLQLSEeeakvatgrvlslQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEA 1040
Cdd:pfam17380 373 eisrmrELERLQMER-------------QQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1041 LNHrivQQAKEMTETMEKKLvEETKQLELDLNDERLRYQNLLnEFSRlEERYDDLKEEMTLMVhVPKPGHKRTDSTHSSN 1120
Cdd:pfam17380 440 LEE---ERAREMERVRLEEQ-ERQQQVERLRQQEEERKRKKL-ELEK-EKRDRKRAEEQRRKI-LEKELEERKQAMIEEE 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1121 ESEYIFSSEIAEMEDipsrteepsekkvpldmSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKakeEERPQIRGAE 1200
Cdd:pfam17380 513 RKRKLLEKEMEERQK-----------------AIYEEERRREAEEERRKQQEMEERRRIQEQMRKAT---EERSRLEAME 572
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462544153 1201 LEYEsLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEE 1258
Cdd:pfam17380 573 RERE-MMRQIVESEKARAEYEATTPITTIKPIYRPRISEYQPPDVESHMIRFTTQSPE 629
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
901-1099 |
7.52e-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: 7.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 901 AKRELKKLKIEARSVErykklhigmeNKIMQLQRKVDEQNKDYKCLVEKLTNLEG---IYNSETEKLRSDLERLqlsEEE 977
Cdd:TIGR02168 808 LRAELTLLNEEAANLR----------ERLESLERRIAATERRLEDLEEQIEELSEdieSLAAEIEELEELIEEL---ESE 874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 978 AKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLvsnlKEENTLLKQEKEALNHRIVQQAK------- 1050
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL----REKLAQLELRLEGLEVRIDNLQErlseeys 950
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462544153 1051 ---EMTETMEKKLVEETKQLELDLNDERLRYQNL-------LNEFSRLEERYDDLKEEM 1099
Cdd:TIGR02168 951 ltlEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQK 1009
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
959-1420 |
8.69e-07 |
|
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: 54.20 E-value: 8.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 959 SETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEqtrSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEK 1038
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQ---LLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1039 EALNH----RIVQQAKEMTETMEKKLVEETKQLE-----LDLNDERLRYQ----NLLNEFSRL-------EERYDDLKEE 1098
Cdd:TIGR00618 240 QSHAYltqkREAQEEQLKKQQLLKQLRARIEELRaqeavLEETQERINRArkaaPLAAHIKAVtqieqqaQRIHTELQSK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1099 MTLMVHVPKPGHKRTDSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEKKVPLDMSL-----FLKLQKRVTELEQEKQVMQ 1173
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHtltqhIHTLQQQKTTLTQKLQSLC 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1174 DELDRKEEQVLRSKAKEEERPQIRG----------AELEYESLKRQELESENKKLKNE---LNELRKALSEKSAPEVTAp 1240
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDLQGqlahakkqqeLQQRYAELCAAAITCTAQCEKLEkihLQESAQSLKEREQQLQTK- 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1241 gapayRVLMEQLTSVSEELDVRKEEVLILRSQLvsQKEAIQPKNTMTDSTILLEDVQKMKdkgEIAQAYIGLKETNRLLE 1320
Cdd:TIGR00618 479 -----EQIHLQETRKKAVVLARLLELQEEPCPL--CGSCIHPNPARQDIDNPGPLTRRMQ---RGEQTYAQLETSEEDVY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1321 SQLQS---QKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEAR--IEASLQHEITRLTNENLYFEELyaddPKK 1395
Cdd:TIGR00618 549 HQLTSerkQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQdlTEKLSEAEDMLACEQHALLRKL----QPE 624
|
490 500
....*....|....*....|....*
gi 2462544153 1396 YQSYRISLYKRMIDLMEQLEKQDKT 1420
Cdd:TIGR00618 625 QDLQDVRLHLQQCSQELALKLTALH 649
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
960-1347 |
9.64e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 960 ETE-KLRS---DLERLQLSEEEakvatgrvlsLQEEIAKLRKDLEQtrsekkcieehADRYKQeteqlvsnLKEENTLLK 1035
Cdd:COG1196 176 EAErKLEAteeNLERLEDILGE----------LERQLEPLERQAEK-----------AERYRE--------LKEELKELE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1036 QEKEALNHRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEmtlmvhvpkpghkrtds 1115
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE----------------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1116 thssnesEYIFSSEIAEMEdipsrteepSEKKVpldmslflkLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEErpq 1195
Cdd:COG1196 290 -------EYELLAELARLE---------QDIAR---------LEERRRELEERLEELEEELAELEEELEELEEELEE--- 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1196 irgaeleyESLKRQELESENKKLKNELNELRKALSEKSApevtapgapayrvlmEQLTSVSEELDVRKEEVLILRSQLVS 1275
Cdd:COG1196 342 --------LEEELEEAEEELEEAEAELAEAEEALLEAEA---------------ELAEAEEELEELAEELLEALRAAAEL 398
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462544153 1276 QKEAIQPKNTMTDSTILLEDVQkmKDKGEIAQAYIGLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEE 1347
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLE--EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
925-1388 |
1.13e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 925 MENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRS 1004
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1005 EKKCIEEHADRYKQETEQlvsnLKEENTLLKQEKEALNHRIvQQAKEMTETMEKKLVEetkqLELDLNDERLRYQNLLNE 1084
Cdd:PRK02224 336 AAQAHNEEAESLREDADD----LEERAEELREEAAELESEL-EEAREAVEDRREEIEE----LEEEIEELRERFGDAPVD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1085 FSRLEERYDDLKEEmtlmvhvpkpghkRTDSTHSSNESEYIFSSE---IAE----------------MEDIP--SRTEEP 1143
Cdd:PRK02224 407 LGNAEDFLEELREE-------------RDELREREAELEATLRTArerVEEaealleagkcpecgqpVEGSPhvETIEED 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1144 SEKKVPLDMSL------FLKLQKRVTELEQEKQVmQDELDRKEEQVLRSkakeEERPQIRGAELEYESLKRQELESENKK 1217
Cdd:PRK02224 474 RERVEELEAELedleeeVEEVEERLERAEDLVEA-EDRIERLEERREDL----EELIAERRETIEEKRERAEELRERAAE 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1218 LKNELNELRKALSEKsapevtapgapayrvlmeqltsvSEELDVRKEEVLILRSQLVSQKEAIQPKNTMTDSTILLEDVQ 1297
Cdd:PRK02224 549 LEAEAEEKREAAAEA-----------------------EEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAE 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1298 kmKDKGEIAQAYIGLKETNRLLESQLQSQKRSHENEAEALRGE-IQSLKEENNRQQQLLAQNLQLPPEARIE-ASLQHEI 1375
Cdd:PRK02224 606 --DEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREErDDLQAEI 683
|
490
....*....|...
gi 2462544153 1376 TRLTNENLYFEEL 1388
Cdd:PRK02224 684 GAVENELEELEEL 696
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
930-1347 |
1.36e-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: 53.57 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 930 MQLQRKVDEQNKDYKCLVEKLTNLEGIYN--SETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKK 1007
Cdd:pfam05483 384 MELQKKSSELEEMTKFKNNKEVELEELKKilAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIK 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1008 CIEEHadrYKQETEQLVSNLkeentllkqEKEALNHRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSR 1087
Cdd:pfam05483 464 TSEEH---YLKEVEDLKTEL---------EKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1088 LEERYDDLKEEmtlmvhvpkpghkrtdSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEKKVPLDMSLfLKLQKRVTELEQ 1167
Cdd:pfam05483 532 MLKQIENLEEK----------------EMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEV-LKKEKQMKILEN 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1168 EKQVMQDELDRK---------EEQVLRSKAKEEERpQIRGAELEYESLKrQELESENKKLKNELNELRKALSEKSAPEvt 1238
Cdd:pfam05483 595 KCNNLKKQIENKnknieelhqENKALKKKGSAENK-QLNAYEIKVNKLE-LELASAKQKFEEIIDNYQKEIEDKKISE-- 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1239 apgapayrvlmEQLTSVSEELDVRKEEVLILRSQLvsqkeAIQPKNTMTDSTILLEDVQKMKDK-GEIAQAYIGLKETNr 1317
Cdd:pfam05483 671 -----------EKLLEEVEKAKAIADEAVKLQKEI-----DKRCQHKIAEMVALMEKHKHQYDKiIEERDSELGLYKNK- 733
|
410 420 430
....*....|....*....|....*....|
gi 2462544153 1318 llESQLQSQKRSHENEAEALRGEIQSLKEE 1347
Cdd:pfam05483 734 --EQEQSSAKAALEIELSNIKAELLSLKKQ 761
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
900-1066 |
1.45e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.24 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 900 MAKRELKKLKIEARSVERYKKLHIgmENKIMQLQRKVDEQNKDYKclvEKLTNLEGIYNSETEKLRSDLERLQLSEEEAK 979
Cdd:PRK12704 39 EAKRILEEAKKEAEAIKKEALLEA--KEEIHKLRNEFEKELRERR---NELQKLEKRLLQKEENLDRKLELLEKREEELE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 980 VATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQE--TEQLVSNLKEEntlLKQEKEALNHRIVQQAKEMTETME 1057
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEeaKEILLEKVEEE---ARHEAAVLIKEIEEEAKEEADKKA 190
|
....*....
gi 2462544153 1058 KKLVEETKQ 1066
Cdd:PRK12704 191 KEILAQAIQ 199
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
911-1347 |
1.51e-06 |
|
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: 53.29 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 911 EARSVERYKKLHIGMENKIMQL----QRKVDE-------------QNKDYK----CLVEKLTNLE---GIYNSETEKLRS 966
Cdd:pfam10174 273 EIKQMEVYKSHSKFMKNKIDQLkqelSKKESEllalqtkletltnQNSDCKqhieVLKESLTAKEqraAILQTEVDALRL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 967 DLER-----------LQLSEEEAKVATG--------------RVLSLQEEIAKLrkdLEQTRSEKKCIEEHADRYKqETE 1021
Cdd:pfam10174 353 RLEEkesflnkktkqLQDLTEEKSTLAGeirdlkdmldvkerKINVLQKKIENL---QEQLRDKDKQLAGLKERVK-SLQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1022 QLVSNlkeENTLLKQEKEAL--NHRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEM 1099
Cdd:pfam10174 429 TDSSN---TDTALTTLEEALseKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHA 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1100 TLMVHVPKpghkRTDSTHSSNESEyifsseIAEMEDIPSRTEEPSEKKVPLDMSLFLK--LQKRVTELEQEKQVMQDELD 1177
Cdd:pfam10174 506 SSLASSGL----KKDSKLKSLEIA------VEQKKEECSKLENQLKKAHNAEEAVRTNpeINDRIRLLEQEVARYKEESG 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1178 RKEEQV------LRSKAKEEERPQIRGAELEyeSLKRQELESENKK---LKNELNELRK---ALSEKSAPEVTAPGAPAY 1245
Cdd:pfam10174 576 KAQAEVerllgiLREVENEKNDKDKKIAELE--SLTLRQMKEQNKKvanIKHGQQEMKKkgaQLLEEARRREDNLADNSQ 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1246 RVLMEQLTsvsEELDVRKEEVLILRSQLVSQKEAIQPKNTMTDSTIL-----LEDVQKMKDkgEIAQAYIGLKETNRLLE 1320
Cdd:pfam10174 654 QLQLEELM---GALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAerrkqLEEILEMKQ--EALLAAISEKDANIALL 728
|
490 500 510
....*....|....*....|....*....|.
gi 2462544153 1321 SQLQSQKRSHENEAEALRGE----IQSLKEE 1347
Cdd:pfam10174 729 ELSSSKKKKTQEEVMALKREkdrlVHQLKQQ 759
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
980-1244 |
1.60e-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: 52.46 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 980 VATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEentlLKQEKEALNHRIVQQAKEMTETMEK- 1058
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAEl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1059 -KLVEETKQLELDLNDERLRYQNLLNEFSRLEERyddlkEEMTLMVHVPKPghkrTDSTHSSNESEYIFSSEIAEMEDIP 1137
Cdd:COG4942 86 aELEKEIAELRAELEAQKEELAELLRALYRLGRQ-----PPLALLLSPEDF----LDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1138 SRTEEpsekkvpldmslflkLQKRVTELEQEKQVMQDELDRKEEQVLR-SKAKEEERPQIRGAELEYESLKRQ--ELESE 1214
Cdd:COG4942 157 ADLAE---------------LAALRAELEAERAELEALLAELEEERAAlEALKAERQKLLARLEKELAELAAElaELQQE 221
|
250 260 270
....*....|....*....|....*....|
gi 2462544153 1215 NKKLKNELNELRKALSEKSAPEVTAPGAPA 1244
Cdd:COG4942 222 AEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
813-835 |
1.95e-06 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 45.78 E-value: 1.95e-06
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
892-1273 |
2.96e-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: 51.82 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 892 LQCCFRR---MMAKRELKKLKIEaRSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYnSETEKLRSDL 968
Cdd:pfam07888 36 LEECLQEraeLLQAQEAANRQRE-KEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKY-KELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 969 --ERLQLSEEEAKvATGRVLSLQEEIaklrkdleQTRSEKKC-IEEHADRYKQETEQLVSNLKEENTllkqEKEALNHRI 1045
Cdd:pfam07888 114 seEKDALLAQRAA-HEARIRELEEDI--------KTLTQRVLeRETELERMKERAKKAGAQRKEEEA----ERKQLQAKL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1046 vQQAKEMTETMEKKLVEETKQLE------LDLNDERLRYQNLLNEFSRLEERYDDLKEEMtlmvhvpkpghkRT--DSTH 1117
Cdd:pfam07888 181 -QQTEEELRSLSKEFQELRNSLAqrdtqvLQLQDTITTLTQKLTTAHRKEAENEALLEEL------------RSlqERLN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1118 SSNESEYIFSSEIAEMEDIPSRTE--------EPSEKKVPL-DMSLFLKLQKrvTELEQEKQVMQdeldrkeeqvlRSKA 1188
Cdd:pfam07888 248 ASERKVEGLGEELSSMAAQRDRTQaelhqarlQAAQLTLQLaDASLALREGR--ARWAQERETLQ-----------QSAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1189 KEEERPQIRGAELEYESLKRQELESENKKLKNEL------NELRKALSEKSAPEVTApgapAYRVLMEQltsvSEELDVR 1262
Cdd:pfam07888 315 ADKDRIEKLSAELQRLEERLQEERMEREKLEVELgrekdcNRVQLSESRRELQELKA----SLRVAQKE----KEQLQAE 386
|
410
....*....|.
gi 2462544153 1263 KEEVLILRSQL 1273
Cdd:pfam07888 387 KQELLEYIRQL 397
|
|
| fMyo4p_CBD |
cd15479 |
cargo binding domain of fungal myosin 4; Yeast myosin V travels along actin cables, actin ... |
1663-1791 |
2.97e-06 |
|
cargo binding domain of fungal myosin 4; Yeast myosin V travels along actin cables, actin filaments that are bundled by fimbrin, in the presence of tropomyosin. This is in contrast to the other vertebrate class V myosins. Like other class V myosins, fungal myosin 2 and 4 contain a C-terminal cargo binding domain. In case of Myo4 it has been shown to bind to the adapter protein She3p (Swi5p-dependent HO expression 3), which in turn anchors myosin 4 to its cargos, zip-coded mRNP (messenger ribonucleoprotein particles) and tER (tubular endoplasmic reticulum).
Pssm-ID: 271263 Cd Length: 329 Bit Score: 51.51 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1663 LNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKnlmNSGAKETLEPL 1742
Cdd:cd15479 168 LNEFDAVLCKFQVVDSMHTKIFNDTLKYLNVMLFNDLITKCPALNWKYGYEVDRNIERLVSWFEPR---IEDVRPNLIQI 244
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2462544153 1743 IQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERV 1791
Cdd:cd15479 245 IQAVKILQLKISNLNEFKLLFDFWYALNPAQIQAILLKYKPANKGEAGV 293
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
984-1347 |
3.24e-06 |
|
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: 52.28 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 984 RVLSLQ--EEIAKLRKDLEQTRSE--------KKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRivQQAKEMT 1053
Cdd:pfam02463 136 NFLVQGgkIEIIAMMKPERRLEIEeeaagsrlKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA--KKALEYY 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1054 ETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEmtlmvhvpkpghKRTDSTHSSNESEYIFSSEIAEM 1133
Cdd:pfam02463 214 QLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ------------EIEKEEEKLAQVLKENKEEEKEK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1134 EDIPSRTEEpSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQirgaELEYESLKRQELES 1213
Cdd:pfam02463 282 KLQEEELKL-LAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEK----ELKELEIKREAEEE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1214 ENKKLKNELNELRKALSEKSApevtapgapAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKNTMTDS--TI 1291
Cdd:pfam02463 357 EEEELEKLQEKLEQLEEELLA---------KKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEekKE 427
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462544153 1292 LLEDVQKMKDKGEIAQAYIGLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEE 1347
Cdd:pfam02463 428 ELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQ 483
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
639-663 |
3.31e-06 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 49.27 E-value: 3.31e-06
10 20
....*....|....*....|....*
gi 2462544153 639 FRNSLHLLMETLNATTPHYVRCIKP 663
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
901-1098 |
3.35e-06 |
|
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: 52.38 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 901 AKRELKKL-KIEARSVERYKKLhigmENKIMQLQRKVDEQNKDYKCLVEKLTNLEgiynSETEKLRSDLERLqlsEEEAK 979
Cdd:TIGR02169 313 KERELEDAeERLAKLEAEIDKL----LAEIEELEREIEEERKRRDKLTEEYAELK----EELEDLRAELEEV---DKEFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 980 VATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQL---VSNLKEENTLLKQEKEALNHRIvqqakemtetm 1056
Cdd:TIGR02169 382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLnaaIAGIEAKINELEEEKEDKALEI----------- 450
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462544153 1057 eKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEE 1098
Cdd:TIGR02169 451 -KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
900-1225 |
3.36e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.28 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 900 MAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLegIYNSETEKLRSDLERLQLSEEEAK 979
Cdd:TIGR00618 602 KLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTL--TQERVREHALSIRVLPKELLASRQ 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 980 VATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQ-------QAKEM 1052
Cdd:TIGR00618 680 LALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKElmhqartVLKAR 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1053 TETMEKKLVEETKQLELDLNDERLRyQNLLNEFSRLEERYDDLKE-EMTLMVHVPKPGHKRTDSTHSSNESEYIFSSEIA 1131
Cdd:TIGR00618 760 TEAHFNNNEEVTAALQTGAELSHLA-AEIQFFNRLREEDTHLLKTlEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLE 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1132 E----MEDIPSRTEEPSEKKVPLDMSlfLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKE--EERPQIRGAELEYES 1205
Cdd:TIGR00618 839 EksatLGEITHQLLKYEECSKQLAQL--TQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEitLYANVRLANQSEGRF 916
|
330 340
....*....|....*....|
gi 2462544153 1206 LKRQELESENKKLKNELNEL 1225
Cdd:TIGR00618 917 HGRYADSHVNARKYQGLALL 936
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
972-1304 |
3.44e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 972 QLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRI--VQQA 1049
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQeeLESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1050 KEMTETMEKKLVE---ETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLM---VHVPKPGHKRTDSTHSSNESE 1123
Cdd:COG4372 107 QEEAEELQEELEElqkERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLqeeLAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1124 YIFSSEIAEMEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAELEY 1203
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1204 ESLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPK 1283
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
330 340
....*....|....*....|.
gi 2462544153 1284 NTMTDSTILLEDVQKMKDKGE 1304
Cdd:COG4372 347 LVGLLDNDVLELLSKGAEAGV 367
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
902-1231 |
6.39e-06 |
|
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: 51.17 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 902 KRELKKLKIEARSverYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEgiynSETEKLRSDLERLqlSEEEAKva 981
Cdd:TIGR04523 369 QNEIEKLKKENQS---YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ----QEKELLEKEIERL--KETIIK-- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 982 tgrvlsLQEEIaklrKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMtetmeKKLV 1061
Cdd:TIGR04523 438 ------NNSEI----KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL-----KKLN 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1062 EETKQleldlnderlryqnllnefsrLEERYDDLKEEMTlmvhvpkpghkrtdsthSSNESEYIFSSEIAEMED-IPSRT 1140
Cdd:TIGR04523 503 EEKKE---------------------LEEKVKDLTKKIS-----------------SLKEKIEKLESEKKEKESkISDLE 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1141 EEPSEKKVPLDMSLF----LKLQKRVTELEQEkqvmQDELDRKEEQV-LRSKAKEEERPQIRGAELEYESLKRQ------ 1209
Cdd:TIGR04523 545 DELNKDDFELKKENLekeiDEKNKEIEELKQT----QKSLKKKQEEKqELIDQKEKEKKDLIKEIEEKEKKISSlekele 620
|
330 340
....*....|....*....|..
gi 2462544153 1210 ELESENKKLKNELNELRKALSE 1231
Cdd:TIGR04523 621 KAKKENEKLSSIIKNIKSKKNK 642
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1129-1270 |
6.85e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.01 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1129 EIAEMEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLR-----SKAKEEERPQIRgAELEY 1203
Cdd:COG2433 389 ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERlerelSEARSEERREIR-KDREI 467
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462544153 1204 ESLKR--QELESENKKLKNELNELR------KALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILR 1270
Cdd:COG2433 468 SRLDReiERLERELEEERERIEELKrklerlKELWKLEHSGELVPVKVVEKFTKEAIRRLEEEYGLKEGDVVYLR 542
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1156-1438 |
7.73e-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: 51.21 E-value: 7.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1156 LKLQKRVTELEQEKQVMQDELDrKEEQVLRSKAKEEERPQIRGAELEYESlKRQELESENKKLKNELNELRKALSEKSAP 1235
Cdd:TIGR02168 205 LERQAEKAERYKELKAELRELE-LALLVLRLEELREELEELQEELKEAEE-ELEELTAELQELEEKLEELRLEVSELEEE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1236 EVTAPGApayrvlMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKNTMTDST--ILLEDVQKMKDK-----GEIAQA 1308
Cdd:TIGR02168 283 IEELQKE------LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKldELAEELAELEEKleelkEELESL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1309 YIGLKETNRLLEsQLQSQKRSHENEAEALRGEIQSLKEE----NNRQQQLlaqnlqlppEARIEaSLQHEITRLTNENLY 1384
Cdd:TIGR02168 357 EAELEELEAELE-ELESRLEELEEQLETLRSKVAQLELQiaslNNEIERL---------EARLE-RLEDRRERLQQEIEE 425
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462544153 1385 FEELYADDPKKYQSYRISLYKRMI--------DLMEQLEKQDKTVRKLKKQLKVFAKKIGEL 1438
Cdd:TIGR02168 426 LLKKLEEAELKELQAELEELEEELeelqeeleRLEEALEELREELEEAEQALDAAERELAQL 487
|
|
| MyosinXI_CBD |
cd15475 |
cargo binding domain of myosin XI; Class XI myosins are a plant specific group, homologous to ... |
1528-1781 |
1.32e-05 |
|
cargo binding domain of myosin XI; Class XI myosins are a plant specific group, homologous to class V myosins. C-terminal domain of Arabidopsis myosin XI has been shown to be homologous to the cargo-binding domain of yeast myosin V myo2p, which targets myosin to vacuole- and mitochondria, as well as secretory vesicle.
Pssm-ID: 271259 Cd Length: 326 Bit Score: 49.49 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1528 LTSTINSIKKVlkkrGDDFETVSFWLSNTCRFLhCLKQysgeegfmkhntsrqneHCLTnfdlaeyrqvlsdlAIQIYQQ 1607
Cdd:cd15475 52 IIQTIGSAIED----QDNNDHLAYWLSNTSTLL-FLLQ-----------------RSLP--------------ALLFKQQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1608 LVRVLENILqPMI-------VSGMLEhETIQGVSGVKPTGLRKRTSSIADEGTYTL---DSILRQLNSFHSVMCQHGMDP 1677
Cdd:cd15475 96 LTAYVEKIY-GIIrdnlkkeLSPLLS-LCIQAPRTSRGSSSKSSSSANSLGQQSPSshwQSIIKSLNSLLSTLKENHVPP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1678 ELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDknlmnsgAKET--------LEPLIQAAQLL 1749
Cdd:cd15475 174 FLVQKIFTQVFSFINVQLFNSLLLRRECCSFSNGEYVKAGLAELELWCSQ-------ATEEyagsswdeLKHIRQAVGFL 246
|
250 260 270
....*....|....*....|....*....|...
gi 2462544153 1750 QVKKKTDDDAEAICS-MCNALTTAQIVKVLNLY 1781
Cdd:cd15475 247 VIHQKSRKSYDEITNdLCPVLSVQQLYRICTMY 279
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
897-1234 |
2.90e-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: 49.27 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 897 RRMMAKRELKKLKIEARSVERYKKlhiGMENKIMQLQRKVD---EQNKDYKCLVE------KLTNLEGIYNSETEKLRSD 967
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQEKT---ELLVEQGRLQLQADrhqEHIRARDSLIQslatrlELDGFERGPFSERQIKNFH 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 968 LERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLkQEKEALNHRIVQ 1047
Cdd:TIGR00606 397 TLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL-QQLEGSSDRILE 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1048 QAKEMTETM-------EKKLVEETKQLELDLNDERLryqNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRTDSTHSSN 1120
Cdd:TIGR00606 476 LDQELRKAErelskaeKNSLTETLKKEVKSLQNEKA---DLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIR 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1121 ESEYIFSSE-IAEMEDIP-----SRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKeeerp 1194
Cdd:TIGR00606 553 KIKSRHSDElTSLLGYFPnkkqlEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDK----- 627
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2462544153 1195 qirgaelEYESLKRQELESENKKLKNELNELRKALSEKSA 1234
Cdd:TIGR00606 628 -------LFDVCGSQDEESDLERLKEEIEKSSKQRAMLAG 660
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
902-1231 |
3.06e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 902 KRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKva 981
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYE-- 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 982 tgrvlSLQEEIAKLRKDLEQTRSEKKCIEEhadrYKQETEQLVSNLKEentlLKQEKEALNHRIVQQAKEMTETMEKKLv 1061
Cdd:PRK03918 529 -----KLKEKLIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLDE----LEEELAELLKELEELGFESVEELEERL- 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1062 eetKQLElDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmvhvpkpgHKRTDSTHSSNESEYIfSSEIAEMEDI--PSR 1139
Cdd:PRK03918 595 ---KELE-PFYNEYLELKDAEKELEREEKELKKLEEELD---------KAFEELAETEKRLEEL-RKELEELEKKysEEE 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1140 TEEPSEKKVPLDMSLFlKLQKRVTELEQEKQVMQDELDRKEEQvlrskaKEEerpqIRGAELEYESLKR-----QELESE 1214
Cdd:PRK03918 661 YEELREEYLELSRELA-GLRAELEELEKRREEIKKTLEKLKEE------LEE----REKAKKELEKLEKalervEELREK 729
|
330
....*....|....*..
gi 2462544153 1215 NKKLKNELNElrKALSE 1231
Cdd:PRK03918 730 VKKYKALLKE--RALSK 744
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
904-1199 |
3.35e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.96 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 904 ELKKLKI------EARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTN----LEGIYN----------SETEK 963
Cdd:pfam15921 631 ELEKVKLvnagseRLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNkseeMETTTNklkmqlksaqSELEQ 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 964 LRSDLERLQLSEEEA-KVATGrvlsLQEEIAKLRKDLEQTRSEKKCIEEhadrykqeteqLVSNLKEENTLLKQEKEALN 1042
Cdd:pfam15921 711 TRNTLKSMEGSDGHAmKVAMG----MQKQITAKRGQIDALQSKIQFLEE-----------AMTNANKEKHFLKEEKNKLS 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1043 HRIVQQAK---------EMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMV-HVPKPGHkr 1112
Cdd:pfam15921 776 QELSTVATeknkmagelEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVkELQGPGY-- 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1113 tdSTHSSNESEYIFSSEIAEME-DIPSRTEEPSekkvpldmslFLKLQKRVTELEQE------KQVMQD--ELDRKEEQV 1183
Cdd:pfam15921 854 --TSNSSMKPRLLQPASFTRTHsNVPSSQSTAS----------FLSHHSRKTNALKEdptrdlKQLLQElrSVINEEPTV 921
|
330
....*....|....*.
gi 2462544153 1184 LRSKAKEEERPQIRGA 1199
Cdd:pfam15921 922 QLSKAEDKGRAPSLGA 937
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
959-1232 |
4.54e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 48.33 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 959 SETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADR------------YKQETEQLVSN 1026
Cdd:pfam02029 50 LKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENneeeensswekeEKRDSRLGRYK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1027 LKEENTLLKQEKEALNHRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEfsrLEERYDDLK---------- 1096
Cdd:pfam02029 130 EEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKE---KKVKYESKVfldqkrghpe 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1097 ---EEMTLMVHVPKPGHKRTDSTHSSNESEYIFSSEIAE----MEDIP-SRTEEPSEKKVPLDMslflKLQKRVTELEqe 1168
Cdd:pfam02029 207 vksQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEaeqkLEELRrRRQEKESEEFEKLRQ----KQQEAELELE-- 280
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462544153 1169 kqvmqdELDRKEEQvlRSKAKEEERPQiRGAEleyESLKRQELESENKKLKNELNELRKALSEK 1232
Cdd:pfam02029 281 ------ELKKKREE--RRKLLEEEEQR-RKQE---EAERKLREEEEKRRMKEEIERRRAEAAEK 332
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
923-1099 |
5.61e-05 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 48.13 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 923 IGMENKIMqlqrKVDEQNKdYKCLVEKLTNLEGIYnSETEKLRSDLERLQlseeEAKVATGRVLSLQEEIAKLRKDLEQT 1002
Cdd:pfam05911 624 SSMEDEIK----KHDCIDK-VTLSENKVAQVDNGC-SEIDNLSSDPEIPS----DGPLVSGSNDLKTEENKRLKEEFEQL 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1003 RSEKKCIEEHADRYK----------QETEQLVSNLKEENTLLKQEKEALNHRIVQQAkEMTETMEKKLVEetkqLELDLN 1072
Cdd:pfam05911 694 KSEKENLEVELASCTenlestksqlQESEQLIAELRSELASLKESNSLAETQLKCMA-ESYEDLETRLTE----LEAELN 768
|
170 180 190
....*....|....*....|....*....|....
gi 2462544153 1073 DERLRYQNLLNEFS-------RLEERYDDLKEEM 1099
Cdd:pfam05911 769 ELRQKFEALEVELEeekncheELEAKCLELQEQL 802
|
|
| IQ |
pfam00612 |
IQ calmodulin-binding motif; Calmodulin-binding motif. |
815-835 |
6.32e-05 |
|
IQ calmodulin-binding motif; Calmodulin-binding motif.
Pssm-ID: 459869 Cd Length: 21 Bit Score: 41.53 E-value: 6.32e-05
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
881-1491 |
6.32e-05 |
|
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: 48.04 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 881 HYKRSMHAIIYLQCCFRRMmaKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSE 960
Cdd:pfam02463 221 LEEEYLLYLDYLKLNEERI--DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 961 TEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEA 1040
Cdd:pfam02463 299 KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1041 LNHRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLmvhvpkpghkRTDSTHSSN 1120
Cdd:pfam02463 379 KKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESI----------ELKQGKLTE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1121 ESEYIFSSEIAEMEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAE 1200
Cdd:pfam02463 449 EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAH 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1201 leyESLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAI 1280
Cdd:pfam02463 529 ---GRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1281 QPKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQ 1360
Cdd:pfam02463 606 AQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1361 LPPEARIEASLQHEITRLTNENLYFEEL-YADDPKKYQSYRISLYKRMIDLMEQLEKQDKTVR---KLKKQLKVFAKKIG 1436
Cdd:pfam02463 686 ESELAKEEILRRQLEIKKKEQREKEELKkLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEeeeEEKSRLKKEEKEEE 765
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 2462544153 1437 ELEVGQMENISPGQIIDEPIRPVNIpRKEKDFQGMLEYKKEDEQKLVKNLILELK 1491
Cdd:pfam02463 766 KSELSLKEKELAEEREKTEKLKVEE-EKEEKLKAQEEELRALEEELKEEAELLEE 819
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
926-1283 |
8.23e-05 |
|
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: 47.86 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 926 ENKIMQLQRKVDEQNKDYKCLVEKLTNLEGiYNSEtekLRSDLERLQLSEEEAkvaTGRVLSLQEEIAKLRKDLEQT--- 1002
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEA-QISE---LQEDLESERAARNKA---EKQRRDLGEELEALKTELEDTldt 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1003 -------RSE--------KKCIEEHADRYKQE---------------TEQLvSNLKEENTLLKQEKEALNH--------- 1043
Cdd:pfam01576 315 taaqqelRSKreqevtelKKALEEETRSHEAQlqemrqkhtqaleelTEQL-EQAKRNKANLEKAKQALESenaelqael 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1044 RIVQQAKEMTETMEKKLVEETKQLELDLND-ERLRyQNLLNEFSRLEERYDDLKeemTLMVHVPKPGHKRTDSThSSNES 1122
Cdd:pfam01576 394 RTLQQAKQDSEHKRKKLEGQLQELQARLSEsERQR-AELAEKLSKLQSELESVS---SLLNEAEGKNIKLSKDV-SSLES 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1123 eyifsseiaEMEDIPSRTEEPSEKKvpldmslfLKLQKRVTELEQEKQVMQDELDrKEEQVLRSKAKEEERPQIRGAE-- 1200
Cdd:pfam01576 469 ---------QLQDTQELLQEETRQK--------LNLSTRLRQLEDERNSLQEQLE-EEEEAKRNVERQLSTLQAQLSDmk 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1201 --LEYESLKRQELESENKKLKNELNELRKALSEKSApevtapgapAYRVLMEQLTSVSEELDVRKEEVLILRsQLVSQKE 1278
Cdd:pfam01576 531 kkLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAA---------AYDKLEKTKNRLQQELDDLLVDLDHQR-QLVSNLE 600
|
....*
gi 2462544153 1279 AIQPK 1283
Cdd:pfam01576 601 KKQKK 605
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
957-1099 |
9.46e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 957 YNSETEKLRSDLERLQL-------------SEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQL 1023
Cdd:COG3206 180 LEEQLPELRKELEEAEAaleefrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1024 -----VSNLKEENTLLKQEKEAL------NHRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEfsrLEERY 1092
Cdd:COG3206 260 lqspvIQQLRAQLAELEAELAELsarytpNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREAS---LQAQL 336
|
....*..
gi 2462544153 1093 DDLKEEM 1099
Cdd:COG3206 337 AQLEARL 343
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
958-1444 |
9.49e-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: 9.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 958 NSETEKLRSDLE-RLQLSEEEAKVAT---------GRVLSLQEEIAKLRKDL-----------EQTRSEKKCIE---EHA 1013
Cdd:pfam10174 205 EKENIHLREELHrRNQLQPDPAKTKAlqtviemkdTKISSLERNIRDLEDEVqmlktngllhtEDREEEIKQMEvykSHS 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1014 DRYKQETEQLVSNL--KEENTLLKQEK-EALNHrivQQAKEmtetmeKKLVEETKQlelDLNDERLRYQNLLNEFSRLEE 1090
Cdd:pfam10174 285 KFMKNKIDQLKQELskKESELLALQTKlETLTN---QNSDC------KQHIEVLKE---SLTAKEQRAAILQTEVDALRL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1091 RYDDlKEEMTlmvhvpkpgHKRTDSTHSSNESEYIFSSEIAEMED---------------IPSRTEEPSEKKVPLDmslf 1155
Cdd:pfam10174 353 RLEE-KESFL---------NKKTKQLQDLTEEKSTLAGEIRDLKDmldvkerkinvlqkkIENLQEQLRDKDKQLA---- 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1156 lKLQKRVTELEQEKQ-------VMQDELDRKEEQVLRSKAKEEERPQIRGAELEyeSLKRqelesENKKLKNELNELRKA 1228
Cdd:pfam10174 419 -GLKERVKSLQTDSSntdtaltTLEEALSEKERIIERLKEQREREDRERLEELE--SLKK-----ENKDLKEKVSALQPE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1229 LSEKSA-----PEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLV---SQKEAIQPKNTMTDSTILLE-DVQKM 1299
Cdd:pfam10174 491 LTEKESslidlKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKkahNAEEAVRTNPEINDRIRLLEqEVARY 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1300 KDKGEIAQAyiglkETNRLLE--SQLQSQKRSHENEAEALRGEI-QSLKEENnrqqQLLAQNLQLPPEARIEASLQHEIT 1376
Cdd:pfam10174 571 KEESGKAQA-----EVERLLGilREVENEKNDKDKKIAELESLTlRQMKEQN----KKVANIKHGQQEMKKKGAQLLEEA 641
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462544153 1377 RLTNENLyfeelyADDPKKYQsyrislykrMIDLMEQLEKQ----DKTVRKLKKQLKVFAKKIGELEVGQME 1444
Cdd:pfam10174 642 RRREDNL------ADNSQQLQ---------LEELMGALEKTrqelDATKARLSSTQQSLAEKDGHLTNLRAE 698
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
929-1203 |
1.41e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 929 IMQLQRKVDEQNKDYKCLVEKLTNLEGI--YNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEK 1006
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQAAKLQGSDLDrtVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEK 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1007 KCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRI-VQQAKEMTETMEKKLV----EETKQLELDLNDERLRYQNL 1081
Cdd:TIGR00606 874 LQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSpLETFLEKDQQEKEELIsskeTSNKKAQDKVNDIKEKVKNI 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1082 LNEFSRLEERYDDLKEEM---------TLMVHVPK-PGHKRTDSTHSSNESEYIFSSEIAE---MEDIPSRTEEPSEKKV 1148
Cdd:TIGR00606 954 HGYMKDIENKIQDGKDDYlkqketelnTVNAQLEEcEKHQEKINEDMRLMRQDIDTQKIQErwlQDNLTLRKRENELKEV 1033
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462544153 1149 PLDMSLFLKL--QKRVTELEQEKQVMQDELD--------------RKEEQVLRSKAKEEErPQIRGAELEY 1203
Cdd:TIGR00606 1034 EEELKQHLKEmgQMQVLQMKQEHQKLEENIDlikrnhvlalgrqkGYEKEIKHFKKELRE-PQFRDAEEKY 1103
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
926-1098 |
1.42e-04 |
|
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: 46.30 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 926 ENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSE 1005
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1006 kkcIEEH------------------------ADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMT--ETMEKK 1059
Cdd:COG4942 106 ---LAELlralyrlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAelEALLAE 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462544153 1060 LVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEE 1098
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
904-1267 |
2.14e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 904 ELKKLKIEARSVERYKKLhiGMENKIMQLQRKVDEQNKdykclVEKLTNLEGIYNSETEKLRSDL---ERLQLSEEEAKV 980
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKK--ADEAKKAEEAKKADEAKK-----AEEAKKADEAKKAEEKKKADELkkaEELKKAEEKKKA 1566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 981 ATGRVLSLQEEIAkLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNL-KEENTLLKQE---KEALNHRIVQQAKEMTETm 1056
Cdd:PTZ00121 1567 EEAKKAEEDKNMA-LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkKAEEAKIKAEelkKAEEEKKKVEQLKKKEAE- 1644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1057 EKKLVEETKQLEldlNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRTDSTHSSNESEYIFSSEIAEMEDI 1136
Cdd:PTZ00121 1645 EKKKAEELKKAE---EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1137 psRTEEPSEKkvpldmslfLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQELESENK 1216
Cdd:PTZ00121 1722 --KKAEEENK---------IKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2462544153 1217 KLKNELNELRKALSEKSA--PEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVL 1267
Cdd:PTZ00121 1791 KRRMEVDKKIKDIFDNFAniIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQL 1843
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
926-1429 |
2.24e-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: 46.50 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 926 ENKIMQLQRKVD---EQNKDYKCLVEKLTNLEGiyNSETEKLRSDLERLQLSeeeakVATGRVLSLQEEIAKLRKDLEQT 1002
Cdd:TIGR00618 378 TQHIHTLQQQKTtltQKLQSLCKELDILQREQA--TIDTRTSAFRDLQGQLA-----HAKKQQELQQRYAELCAAAITCT 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1003 RSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEalNHRIVQQAKEMTETMEKKLVEETKQLELDLNDERL------ 1076
Cdd:TIGR00618 451 AQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETR--KKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNpgpltr 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1077 RYQNLLNEFSRLEERYDDLKEEMTlmvHVPKPGHKRTDSTHSSNESEYIFSSEIAEM-EDIPSRTEEPSEKKVPLDMSLF 1155
Cdd:TIGR00618 529 RMQRGEQTYAQLETSEEDVYHQLT---SERKQRASLKEQMQEIQQSFSILTQCDNRSkEDIPNLQNITVRLQDLTEKLSE 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1156 LKLQKRVT--ELEQEKQVMQDELDRKEEQvlRSKAKEEERPQIRGAELEYESLKRQELES-------ENKKLKNELNELR 1226
Cdd:TIGR00618 606 AEDMLACEqhALLRKLQPEQDLQDVRLHL--QQCSQELALKLTALHALQLTLTQERVREHalsirvlPKELLASRQLALQ 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1227 KALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEvliLRSQLVSQKEAIQPKNTMTDSTilledvqkmkdkgeia 1306
Cdd:TIGR00618 684 KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE---IENASSSLGSDLAAREDALNQS---------------- 744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1307 qayigLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNlqlppeaRIEASLQHEITRLTNEnlyFE 1386
Cdd:TIGR00618 745 -----LKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFN-------RLREEDTHLLKTLEAE---IG 809
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2462544153 1387 ELYADDPKKYQSYRISLYKRMIDLMEQLEKQDKTVRKLKKQLK 1429
Cdd:TIGR00618 810 QEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLL 852
|
|
| IQCD |
cd23767 |
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
809-839 |
2.40e-04 |
|
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.
Pssm-ID: 467745 [Multi-domain] Cd Length: 37 Bit Score: 40.22 E-value: 2.40e-04
10 20 30
....*....|....*....|....*....|.
gi 2462544153 809 AKFLRRTKAATIIQKYWRMYVVRRRYKIRRA 839
Cdd:cd23767 3 EELQRMNRAATLIQALWRGYKVRKELKKKKK 33
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
902-1477 |
4.45e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.42 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 902 KRELKKLKIEARSVERykklhigMENKIMQLQRKVDEQNKDYKclvEKLTNLEGiynseTEKLRSDLERLQlseEEAKVA 981
Cdd:TIGR00606 590 RDRLAKLNKELASLEQ-------NKNHINNELESKEEQLSSYE---DKLFDVCG-----SQDEESDLERLK---EEIEKS 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 982 TGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADR---YKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTETMEK 1058
Cdd:TIGR00606 652 SKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRvfqTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGL 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1059 KLVE--ETKQLELDLNDERLRYQNLLNEFSRLEeryDDLKEEMTLMvhvpkpghkrtDSTHSSNESEYIFSSEIAEMEDI 1136
Cdd:TIGR00606 732 APGRqsIIDLKEKEIPELRNKLQKVNRDIQRLK---NDIEEQETLL-----------GTIMPEEESAKVCLTDVTIMERF 797
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1137 PSRTEEpSEKKVPLDMSLF--LKLQKRVTELEQEKQVMQDELDRKEEQV-LRSKAKEEERPQIrgaeleyeslkrQELES 1213
Cdd:TIGR00606 798 QMELKD-VERKIAQQAAKLqgSDLDRTVQQVNQEKQEKQHELDTVVSKIeLNRKLIQDQQEQI------------QHLKS 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1214 ENKKLKNELNELRKALSEKSAPEVTApgapayRVLMEQLTSVSEELDVRKEEVL----ILRSQLVSQKEAIQPKNTmtDS 1289
Cdd:TIGR00606 865 KTNELKSEKLQIGTNLQRRQQFEEQL------VELSTEVQSLIREIKDAKEQDSpletFLEKDQQEKEELISSKET--SN 936
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1290 TILLEDVQKMKDKgeIAQAYIGLKETNRLLESQLQSQKRSHENEaeaLRGEIQSLKEENNRQQQLLAQNLQLppeaRIEA 1369
Cdd:TIGR00606 937 KKAQDKVNDIKEK--VKNIHGYMKDIENKIQDGKDDYLKQKETE---LNTVNAQLEECEKHQEKINEDMRLM----RQDI 1007
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1370 SLQHEITRLTNENLyfeelyaddpkkyqsyrislykrmidlmeQLEKQDKTVRKLKKQLKVFAKKIGELEVGQMENisPG 1449
Cdd:TIGR00606 1008 DTQKIQERWLQDNL-----------------------------TLRKRENELKEVEEELKQHLKEMGQMQVLQMKQ--EH 1056
|
570 580
....*....|....*....|....*....
gi 2462544153 1450 QIIDEPIRpvNIPRKE-KDFQGMLEYKKE 1477
Cdd:TIGR00606 1057 QKLEENID--LIKRNHvLALGRQKGYEKE 1083
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
960-1098 |
5.17e-04 |
|
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: 43.00 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 960 ETEKLRSDLERL-----QLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRsekkcieehadRYKQETEQLVSNLKEENTLL 1034
Cdd:pfam08614 22 ENAKLQSEPESVlpstsSSKLSKASPQSASIQSLEQLLAQLREELAELY-----------RSRGELAQRLVDLNEELQEL 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1035 KQEKEALNHRI------VQQAKEMTETMEKKLVEETKQLElDLNDErlrYQNLLNEFSRLEERYDDLKEE 1098
Cdd:pfam08614 91 EKKLREDERRLaaleaeRAQLEEKLKDREEELREKRKLNQ-DLQDE---LVALQLQLNMAEEKLRKLEKE 156
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
998-1493 |
5.89e-04 |
|
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: 44.68 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 998 DLEQTRSEKkciEEHADRYkQETEQLVSNLKEENTLLKQEKEALNHRIVQ--QAKEMTETMEKK----------LVEETK 1065
Cdd:pfam05622 1 DLSEAQEEK---DELAQRC-HELDQQVSLLQEEKNSLQQENKKLQERLDQleSGDDSGTPGGKKylllqkqleqLQEENF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1066 QLELDLNDERLRYQNLLNEFSRLEERYDD----------LKEEMtlmvhvpkpghkrtDSTHSSNESEYIFSSEIAemed 1135
Cdd:pfam05622 77 RLETARDDYRIKCEELEKEVLELQHRNEEltslaeeaqaLKDEM--------------DILRESSDKVKKLEATVE---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1136 ipsrteepSEKKVPLDMSlflKLQKRVTELEQEKQV-MQDELDRKEE----QVLRSKAkEEERPQIRG--AELEYESLKR 1208
Cdd:pfam05622 139 --------TYKKKLEDLG---DLRRQVKLLEERNAEyMQRTLQLEEElkkaNALRGQL-ETYKRQVQElhGKLSEESKKA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1209 QELESENKKLKNELNELRKalsEKsapevtapgapayrvlmEQLTSvseELDVRKEEVLILRSQLVSQKEAIQPKNTMTD 1288
Cdd:pfam05622 207 DKLEFEYKKLEEKLEALQK---EK-----------------ERLII---ERDTLRETNEELRCAQLQQAELSQADALLSP 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1289 STILLEDVQKMKDKGEIAQAYIGLKETNRLLESQlqsQKRSHENEAEALrgeiQSLKEENNRQQQLLAQNLQLPPEARIE 1368
Cdd:pfam05622 264 SSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLG---QEGSYRERLTEL----QQLLEDANRRKNELETQNRLANQRILE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1369 asLQHEITRLTnENLYFEELYADDPkkyqsyrISLYKRMIDLMEQLEKQDKTVRKLKKQLKvfakkigELEVGQMENisP 1448
Cdd:pfam05622 337 --LQQQVEELQ-KALQEQGSKAEDS-------SLLKQKLEEHLEKLHEAQSELQKKKEQIE-------ELEPKQDSN--L 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2462544153 1449 GQIIDEpiRPVNIPRKEKDFQGMLE-YKKEDEQklVKNLILELKPR 1493
Cdd:pfam05622 398 AQKIDE--LQEALRKKDEDMKAMEErYKKYVEK--AKSVIKTLDPK 439
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1158-1345 |
6.65e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1158 LQKRVTELEQEKQVMQDELDRKEEQvlrskaKEEERPQIRGAELEYESLKRQELESenkkLKNELNELRKALSEKSApev 1237
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEAR------LDALREELDELEAQIRGNGGDRLEQ----LEREIERLERELEERER--- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1238 tapgapAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQpkntmtdstilledvqkmkdkgeiaqayiGLKETNR 1317
Cdd:COG4913 360 ------RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE-----------------------------EELEALE 404
|
170 180
....*....|....*....|....*...
gi 2462544153 1318 LLESQLQSQKRSHENEAEALRGEIQSLK 1345
Cdd:COG4913 405 EALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1158-1384 |
7.65e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1158 LQKRVTELEQEKQVMQDELDRKEEQVLRSKAKE-----EERPQIRGAELEYESLKRQELESENKKLKNELNELRKALSEK 1232
Cdd:COG3206 173 ARKALEFLEEQLPELRKELEEAEAALEEFRQKNglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1233 SAPEVTAPGAPAYRVLMEQLTSvseeldvrkeevliLRSQLVSQKEAIQPKNtmtdstillEDVQKMKDKgeiaqayigL 1312
Cdd:COG3206 253 PDALPELLQSPVIQQLRAQLAE--------------LEAELAELSARYTPNH---------PDVIALRAQ---------I 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462544153 1313 KETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNlqlpPEARIE-ASLQHEITrlTNENLY 1384
Cdd:COG3206 301 AALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL----PELEAElRRLEREVE--VARELY 367
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
960-1225 |
8.11e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 8.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 960 ETEKLRSDLERLQLSEEEAKVATGR-VLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLkEENTLLKQEK 1038
Cdd:pfam01576 493 QLEDERNSLQEQLEEEEEAKRNVERqLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQL-EEKAAAYDKL 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1039 EALNHRIVQQAKEMTETM--EKKLVE--ETKQLELD--LNDERLRYQNLLNEFSRLEErydDLKEEMTLMVHVpkpGHKR 1112
Cdd:pfam01576 572 EKTKNRLQQELDDLLVDLdhQRQLVSnlEKKQKKFDqmLAEEKAISARYAEERDRAEA---EAREKETRALSL---ARAL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1113 TDSTHSSNESEYIFSSEIAEMEDIPSRTE---------EPSEKKVPLDMSlflKLQKRVTELEQEKQVMQDELDRKEEQV 1183
Cdd:pfam01576 646 EEALEAKEELERTNKQLRAEMEDLVSSKDdvgknvhelERSKRALEQQVE---EMKTQLEELEDELQATEDAKLRLEVNM 722
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1184 LRSKAK------------EEERPQIRG------AELEYESLKRQELESENKKLKNELNEL 1225
Cdd:pfam01576 723 QALKAQferdlqardeqgEEKRRQLVKqvreleAELEDERKQRAQAVAAKKKLELDLKEL 782
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
925-1095 |
8.69e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 925 MENKIMQLQRKVDEQNKDYKCLVEKLTNLEgiynSETEKLRSDLERLQlsEEEAKVATGRVL-SLQEEIAKLRKDLEQTR 1003
Cdd:COG1579 36 LEDELAALEARLEAAKTELEDLEKEIKRLE----LEIEEVEARIKKYE--EQLGNVRNNKEYeALQKEIESLKRRISDLE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1004 SEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEmtetmEKKLVEETKQLELDLNDErlryqnLLN 1083
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE-----LEELEAEREELAAKIPPE------LLA 178
|
170
....*....|..
gi 2462544153 1084 EFSRLEERYDDL 1095
Cdd:COG1579 179 LYERIRKRKNGL 190
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
926-1098 |
9.44e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 926 ENKIMQLQRKVDEQNKDYKCLVEKLTNLegiyNSETEKLRSDLERLQlseeeAKVATgrvlsLQEEIAKLRKDLEQTRSE 1005
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDAL----QAELEELNEEYNELQ-----AELEA-----LQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1006 kkcIEEHADRYKQ----------------------ETEQLVSNLKEENTLLKQEKEALNHriVQQAKEMTETMEKKLVEE 1063
Cdd:COG3883 81 ---IEERREELGEraralyrsggsvsyldvllgseSFSDFLDRLSALSKIADADADLLEE--LKADKAELEAKKAELEAK 155
|
170 180 190
....*....|....*....|....*....|....*
gi 2462544153 1064 TKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEE 1098
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
960-1238 |
1.16e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 960 ETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSnLKEENTLLkqEKE 1039
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE-LRERAAEL--EAE 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1040 ALNHRivQQAKEMTETMEKKLvEETKQLELDL--NDERL----RYQNLLNEFSRLEERYDDLKEemtlmvhvpkpghKRt 1113
Cdd:PRK02224 553 AEEKR--EAAAEAEEEAEEAR-EEVAELNSKLaeLKERIesleRIRTLLAAIADAEDEIERLRE-------------KR- 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1114 dsthssneseyifsSEIAEMEDIP-SRTEEPSEKKVPLDMSLflkLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEE 1192
Cdd:PRK02224 616 --------------EALAELNDERrERLAEKRERKRELEAEF---DEARIEEAREDKERAEEYLEQVEEKLDELREERDD 678
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2462544153 1193 -RPQIRGAELEYESLKrqELESENKKLKNELNELRKALSEKSAPEVT 1238
Cdd:PRK02224 679 lQAEIGAVENELEELE--ELRERREALENRVEALEALYDEAEELESM 723
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
987-1104 |
1.17e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.20 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 987 SLQEEIAKLRKDleqtrsekkciEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTETMEKKlvEETKQ 1066
Cdd:pfam13851 30 SLKEEIAELKKK-----------EERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLK--ARLKV 96
|
90 100 110
....*....|....*....|....*....|....*...
gi 2462544153 1067 LELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVH 1104
Cdd:pfam13851 97 LEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQ 134
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
901-1481 |
1.25e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 901 AKRELKKLKIEARSVERYKklhIGMENKIMQLQRKVDEQNKdykclVEKLTNLEGIYNSETEKLRSDLERLQLS---EEE 977
Cdd:PTZ00121 1092 ATEEAFGKAEEAKKTETGK---AEEARKAEEAKKKAEDARK-----AEEARKAEDARKAEEARKAEDAKRVEIArkaEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 978 AKVATGRVLSLQEEIAKLRKDLEQTRSEKkcIEEHADRYKQETEQLVSNLKEENTLLKQEKEalnhRIVQQAKEMTETme 1057
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRKAEE--LRKAEDARKAEAARKAEEERKAEEARKAEDA----KKAEAVKKAEEA-- 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1058 KKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRtdSTHSSNESEYIFSSEIAEMEDIP 1137
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKK--KADEAKKAEEKKKADEAKKKAEE 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1138 SRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAK--------EEERPQIRGAELEYESLKR- 1208
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKaeaaekkkEEAKKKADAAKKKAEEKKKa 1393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1209 QELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVlMEQLTSVSEEL-----------DVRKEEVLI--------- 1268
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK-ADEAKKKAEEAkkadeakkkaeEAKKAEEAKkkaeeakka 1472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1269 --LRSQLVSQKEAIQPKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETNRLLESQLQSQKRSHEN--------EAEALR 1338
Cdd:PTZ00121 1473 deAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEakkaeekkKADELK 1552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1339 G--EIQSLKEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNENLYFEE---LYADDPKKYQSYRISlykrmidlMEQ 1413
Cdd:PTZ00121 1553 KaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEekkMKAEEAKKAEEAKIK--------AEE 1624
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462544153 1414 LEKQDKtVRKLKKQLkvfaKKIGELEVGQMENISPGQiIDEPIRPVNIPRK-EKDFQGMLEYKKEDEQK 1481
Cdd:PTZ00121 1625 LKKAEE-EKKKVEQL----KKKEAEEKKKAEELKKAE-EENKIKAAEEAKKaEEDKKKAEEAKKAEEDE 1687
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
1161-1350 |
1.54e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 42.71 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1161 RVTELEQEKQvMQDEL---------DRKEEQVLRSKAKEEERPQIRGAELEYESLKRQ--ELESENKKLKNELNELRKAL 1229
Cdd:pfam04849 116 EILQLRHELS-KKDDLlqiysndaeESETESSCSTPLRRNESFSSLHGCVQLDALQEKlrGLEEENLKLRSEASHLKTET 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1230 SEKSAPE------VTAPGAPA---YRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQpkntmtdstilledvQKMK 1300
Cdd:pfam04849 195 DTYEEKEqqlmsdCVEQLSEAnqqMAELSEELARKMEENLRQQEEITSLLAQIVDLQHKCK---------------ELGI 259
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1301 DKGEIAQAYIGLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNR 1350
Cdd:pfam04849 260 ENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
962-1098 |
1.56e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.07 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 962 EKLRSDLER--------LQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQlvsnlkeentL 1033
Cdd:pfam05262 184 EALREDNEKgvnfrrdmTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQ----------K 253
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462544153 1034 LKQEKEALNHRIVQQAKEMTETMEKKLVE-ETKQLELDLNDERLRYQNllnefsrlEERYDDLKEE 1098
Cdd:pfam05262 254 QQEAKNLPKPADTSSPKEDKQVAENQKREiEKAQIEIKKNDEEALKAK--------DHKAFDLKQE 311
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
969-1109 |
1.58e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 969 ERLQLSE---EEAK-VATGRVLSLQEEIAKL---RKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKE--ENTLLKQEKE 1039
Cdd:PRK00409 495 KRLGLPEniiEEAKkLIGEDKEKLNELIASLeelERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEeeDKLLEEAEKE 574
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462544153 1040 AlnHRIVQQAKEMTETMEKKLVEETKQLELDLNDerlryQNLLNEFSRLEERYDDLKE---EMTLMVHVPKPG 1109
Cdd:PRK00409 575 A--QQAIKEAKKEADEIIKELRQLQKGGYASVKA-----HELIEARKRLNKANEKKEKkkkKQKEKQEELKVG 640
|
|
| Paralemmin |
pfam03285 |
Paralemmin; |
1160-1282 |
1.71e-03 |
|
Paralemmin;
Pssm-ID: 460875 Cd Length: 301 Bit Score: 42.42 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1160 KRVTELEQEKQvmQDELDRKEEQVLRSKAKEE----ERPQIRGAElEYESLKRQELESENKK---------LKNELNELR 1226
Cdd:pfam03285 5 KRQTEIENKRR--QLEDDRRQLQHLKSKALRErwllEGPPSSASE-EDEARRRQEEEDEQKKklleeiirrLEEEIELLE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462544153 1227 KALSEKSAPEvtapgapayrVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQP 1282
Cdd:pfam03285 82 EESSISAKKE----------NLAEKLLEITVEKDKVTGETRVLSSTTLLPDDVQPQ 127
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1157-1349 |
1.82e-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: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1157 KLQKRVTELEQEKQVMQDELDRKEEQVlrSKAKEEerpqIRGAELEYESLKRQ--ELESENKKLKNELNELRKALSEksa 1234
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAEL--EELNEE----YNELQAELEALQAEidKLQAEIAEAEAEIEERREELGE--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1235 pevtapgapAYRVLMEQLTSVSEeLDVrkeevlILRSQ----LVSQKEAIqpkNTMTDSTI-LLEDVQKMKDKgeiaqay 1309
Cdd:COG3883 91 ---------RARALYRSGGSVSY-LDV------LLGSEsfsdFLDRLSAL---SKIADADAdLLEELKADKAE------- 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462544153 1310 igLKETNRLLESQLQSQKRShENEAEALRGEIQSLKEENN 1349
Cdd:COG3883 145 --LEAKKAELEAKLAELEAL-KAELEAAKAELEAQQAEQE 181
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
932-1091 |
1.88e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 932 LQRKVDEQNKDYKCLVEKLTNLEgiynSETEKLRSDLERLQlsEEEAKVATGRVLSLQEEIAKLRKDLEQtrsekkcIEE 1011
Cdd:COG4913 293 LEAELEELRAELARLEAELERLE----ARLDALREELDELE--AQIRGNGGDRLEQLEREIERLERELEE-------RER 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1012 HADRYkqetEQLVSNLKEENTLLKQEKEALnHRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEER 1091
Cdd:COG4913 360 RRARL----EALLAALGLPLPASAEEFAAL-RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
788-810 |
2.07e-03 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 36.92 E-value: 2.07e-03
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
906-1428 |
2.14e-03 |
|
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: 43.24 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 906 KKLKIEARSVE-RYKKlhigMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSdLERLQLSEE----EAKV 980
Cdd:pfam01576 120 QKLQLEKVTTEaKIKK----LEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKS-LSKLKNKHEamisDLEE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 981 ATGRVLSLQEEIAKLRKDLEQTRSEKKciEEHADRYKQETEQLVSNLKEEntllkQEKEALNHRIVQQAKEMTETMEK-- 1058
Cdd:pfam01576 195 RLKKEEKGRQELEKAKRKLEGESTDLQ--EQIAELQAQIAELRAQLAKKE-----EELQAALARLEEETAQKNNALKKir 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1059 KLVEETKQLELDLNDERLRYqnllnefSRLEERYDDLKEEMTLMvhvpkpghkRTdsthssneseyifsseiaEMEDIPS 1138
Cdd:pfam01576 268 ELEAQISELQEDLESERAAR-------NKAEKQRRDLGEELEAL---------KT------------------ELEDTLD 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1139 RTEEPSEKKvpldmslflklQKRVTELEQEKQVMQDELDRKEEQV--LRSK---AKEEERPQIRGAELEYESLK--RQEL 1211
Cdd:pfam01576 314 TTAAQQELR-----------SKREQEVTELKKALEEETRSHEAQLqeMRQKhtqALEELTEQLEQAKRNKANLEkaKQAL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1212 ESENKKLKNELNELRKALSEKSAPEVTAPGapayrvlmeQLtsvsEELDVRKEEVLILRSQLVSQKEAIQpkNTMTDSTI 1291
Cdd:pfam01576 383 ESENAELQAELRTLQQAKQDSEHKRKKLEG---------QL----QELQARLSESERQRAELAEKLSKLQ--SELESVSS 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1292 LLEDVQK--MKDKGEIAQAYIGLKETNRLLES------QLQSQKRSHENEAEALRgEIQSLKEENNRQQQLLAQNlqlpp 1363
Cdd:pfam01576 448 LLNEAEGknIKLSKDVSSLESQLQDTQELLQEetrqklNLSTRLRQLEDERNSLQ-EQLEEEEEAKRNVERQLST----- 521
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462544153 1364 earIEASLQHEITRLTNENLYFEELyADDPKKYQSYRISLYKRMIDLMEQLEKQDKTVRKLKKQL 1428
Cdd:pfam01576 522 ---LQAQLSDMKKKLEEDAGTLEAL-EEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQEL 582
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
968-1347 |
2.15e-03 |
|
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: 42.71 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 968 LERLQLSEEEAKvatgrvlSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKeentllKQEKEAlnhrivQ 1047
Cdd:pfam05701 34 VERRKLVELELE-------KVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLE------RAQTEE------A 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1048 QAKEMTETMEKKlVEETKQ---------LELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRT-DSTH 1117
Cdd:pfam05701 95 QAKQDSELAKLR-VEEMEQgiadeasvaAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAeEAVS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1118 SSNESEYIFssEIAEMEDIPSRTE---------EPSEKKVPLDMSL---FLKLQKrvtELEQekqvMQDELDRKEEQVLR 1185
Cdd:pfam05701 174 ASKEIEKTV--EELTIELIATKESlesahaahlEAEEHRIGAALAReqdKLNWEK---ELKQ----AEEELQRLNQQLLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1186 SKAKEeerpqirgAELEYESLKRQELESE-NKKLKNELNELRKALSEKSAPEVTAPGApayrvlmeqLTSVSEEL-DVR- 1262
Cdd:pfam05701 245 AKDLK--------SKLETASALLLDLKAElAAYMESKLKEEADGEGNEKKTSTSIQAA---------LASAKKELeEVKa 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1263 -----KEEVLI-------LRSQLVSQKE---AIQPKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETN-RLLESQLQSQ 1326
Cdd:pfam05701 308 niekaKDEVNClrvaaasLRSELEKEKAelaSLRQREGMASIAVSSLEAELNRTKSEIALVQAKEKEAReKMVELPKQLQ 387
|
410 420
....*....|....*....|....*.
gi 2462544153 1327 KRSHENE-----AEALRGEIQSLKEE 1347
Cdd:pfam05701 388 QAAQEAEeakslAQAAREELRKAKEE 413
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
910-1300 |
2.21e-03 |
|
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: 43.11 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 910 IEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLV-EKLTNLEGIYNSETEKLRS---DLERLQLSEEEAKVATGRV 985
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIrDQITSKEAQLESSREIVKSyenELDPLKNRLKEIEHNLSKI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 986 LSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEA----LNHRIVQQAKEMTETMEKKLV 1061
Cdd:TIGR00606 265 MKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERelvdCQRELEKLNKERRLLNQEKTE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1062 EETKQLELDLNDERLRYQNLlnefsrleeRYDDLKEEMTLmvhvpkpgHKRTDSTHSSNESEyifsSEIAEMEDIPSRTE 1141
Cdd:TIGR00606 345 LLVEQGRLQLQADRHQEHIR---------ARDSLIQSLAT--------RLELDGFERGPFSE----RQIKNFHTLVIERQ 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1142 EPSEKKVPLDMSLFlklqkrvTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQELESENKKLKNE 1221
Cdd:TIGR00606 404 EDEAKTAAQLCADL-------QSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILEL 476
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462544153 1222 LNELRKALSEKSAPEVTApgapayrvLMEqlTSVSEELDVRKEEVLILRSqLVSQKEAIQPKNTMTDSTILLEDVQKMK 1300
Cdd:TIGR00606 477 DQELRKAERELSKAEKNS--------LTE--TLKKEVKSLQNEKADLDRK-LRKLDQEMEQLNHHTTTRTQMEMLTKDK 544
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
765-786 |
2.30e-03 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 36.92 E-value: 2.30e-03
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
902-1431 |
2.51e-03 |
|
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: 42.90 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 902 KRELKKLKIEARSVerYKKLHIGMENKIMQLQRKVDEQNKDYKclvEKLTNLEG-----IYNSET-EKLRSDLERLQLSE 975
Cdd:pfam12128 403 REARDRQLAVAEDD--LQALESELREQLEAGKLEFNEEEYRLK---SRLGELKLrlnqaTATPELlLQLENFDERIERAR 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 976 EEAKVATGRVLSLQEEIAKLRKDLEQTrsekkciEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTET 1055
Cdd:pfam12128 478 EEQEAANAEVERLQSELRQARKRRDQA-------SEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQS 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1056 MEK--------------KLVEETKQLELDLNDERLRYQNL-LNEFSRLEErydDLKEemtlmvhvpkpghkRTDSTHSSN 1120
Cdd:pfam12128 551 IGKvispellhrtdldpEVWDGSVGGELNLYGVKLDLKRIdVPEWAASEE---ELRE--------------RLDKAEEAL 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1121 ESEyifSSEIAEMEdipsrtEEPSEKKVPLD-MSLFLKLQKRVTELEQEKQ-----VMQDELDRKEEQVLRSKAKEEERp 1194
Cdd:pfam12128 614 QSA---REKQAAAE------EQLVQANGELEkASREETFARTALKNARLDLrrlfdEKQSEKDKKNKALAERKDSANER- 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1195 qirgaeleyeslkRQELESENKKLKNELNELRKALSEKSApEVTAPGAPAYRVLMEQLtsvSEELDVRKEEVLILRSQLV 1274
Cdd:pfam12128 684 -------------LNSLEAQLKQLDKKHQAWLEEQKEQKR-EARTEKQAYWQVVEGAL---DAQLALLKAAIAARRSGAK 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1275 SQKEAIQ-------------PKNTMTDSTILLEDVQKM----KDKGEIAQAYIGLKETNRLLESQLQSQKRSHENEAEAL 1337
Cdd:pfam12128 747 AELKALEtwykrdlaslgvdPDVIAKLKREIRTLERKIeriaVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISEL 826
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1338 RGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNENLYFEELYADDpkkyQSYRISLYKRMIDLMEQLEKQ 1417
Cdd:pfam12128 827 QQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANS----EQAQGSIGERLAQLEDLKLKR 902
|
570
....*....|....
gi 2462544153 1418 DKTVRKLKKQLKVF 1431
Cdd:pfam12128 903 DYLSESVKKYVEHF 916
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
971-1104 |
2.52e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 971 LQLSEEEAKVATG-RVLSLQEEIAKLRKDLEQTRSEKkciEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQA 1049
Cdd:PRK12704 44 LEEAKKEAEAIKKeALLEAKEEIHKLRNEFEKELRER---RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELE 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462544153 1050 KEMTETMEKKlvEETKQLELDLNDERLRYQNLLNEFSR---LEERYDDLKEEMTLMVH 1104
Cdd:PRK12704 121 QKQQELEKKE--EELEELIEEQLQELERISGLTAEEAKeilLEKVEEEARHEAAVLIK 176
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
960-1052 |
3.11e-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: 42.06 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 960 ETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKE 1039
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
90
....*....|...
gi 2462544153 1040 ALNHRIVQQAKEM 1052
Cdd:COG4942 231 RLEAEAAAAAERT 243
|
|
| CBD_MYO6-like |
cd21759 |
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ... |
767-794 |
3.34e-03 |
|
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).
Pssm-ID: 409646 [Multi-domain] Cd Length: 149 Bit Score: 39.80 E-value: 3.34e-03
10 20
....*....|....*....|....*...
gi 2462544153 767 RAACIRIQKTIRGWLLRKKYlRMRKAAI 794
Cdd:cd21759 45 REALIKIQKTVRGYLARKKH-RPRIKGL 71
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
900-1242 |
3.41e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 900 MAKRELKKLKIEArSVERYKKLHIGMENKIMQLQRKVDEqnkdYKCLVEKLTNLEgiynseTEKLRSDLERLQLSEEEAK 979
Cdd:COG5185 217 SESTLLEKAKEII-NIEEALKGFQDPESELEDLAQTSDK----LEKLVEQNTDLR------LEKLGENAESSKRLNENAN 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 980 VATGRVLSLQEEIAKLRKDLEQTRS-EKKCIEEHADRYKQETEQLVSNLKEENTLLKQEkealnhrIVQQAKEMTETMEk 1058
Cdd:COG5185 286 NLIKQFENTKEKIAEYTKSIDIKKAtESLEEQLAAAEAEQELEESKRETETGIQNLTAE-------IEQGQESLTENLE- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1059 KLVEETKQLELDLNDERLRyQNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRTDSTHSSNESEyiFSSEIAEMEDIPS 1138
Cdd:COG5185 358 AIKEEIENIVGEVELSKSS-EELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQ--IEELQRQIEQATS 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1139 RTEEPSEKKVPLDMSlflkLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKE--EERPQIRGAELEYeslkRQELESENK 1216
Cdd:COG5185 435 SNEEVSKLLNELISE----LNKVMREADEESQSRLEEAYDEINRSVRSKKEDlnEELTQIESRVSTL----KATLEKLRA 506
|
330 340
....*....|....*....|....*.
gi 2462544153 1217 KLKNELNELRKALSEKSAPEVTAPGA 1242
Cdd:COG5185 507 KLERQLEGVRSKLDQVAESLKDFMRA 532
|
|
| CBD_MYO6-like |
cd21759 |
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ... |
829-862 |
3.71e-03 |
|
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).
Pssm-ID: 409646 [Multi-domain] Cd Length: 149 Bit Score: 39.80 E-value: 3.71e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2462544153 829 VVRRRYKI--RRAATIVLQSYLRGFLARNRYRKILR 862
Cdd:cd21759 34 VIKLKNKIlyRREALIKIQKTVRGYLARKKHRPRIK 69
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
900-1098 |
3.80e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 900 MAKRELKKLKIEARSVERYKKlhiGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAK 979
Cdd:COG4372 35 KALFELDKLQEELEQLREELE---QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 980 VATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTETMEKK 1059
Cdd:COG4372 112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKE 191
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462544153 1060 LVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEE 1098
Cdd:COG4372 192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAK 230
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
969-1347 |
4.28e-03 |
|
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: 42.08 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 969 ERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEhadRYKQETEqLVSNLKEENTLL---KQEKEALNHRI 1045
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQE---QLQAETE-LCAEAEEMRARLaarKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1046 ---VQQAKEMTETME---KKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMvhvpkpghkrTDSTHSS 1119
Cdd:pfam01576 81 esrLEEEEERSQQLQnekKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLL----------EDQNSKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1120 NESEYIFSSEIAEMEDIPSRTEEPSEKKVPL---------DMSLFLKLQKRV-TELEQEKQVMQDELDRKEEQVLRSK-- 1187
Cdd:pfam01576 151 SKERKLLEERISEFTSNLAEEEEKAKSLSKLknkheamisDLEERLKKEEKGrQELEKAKRKLEGESTDLQEQIAELQaq 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1188 --------AKEEERPQIRGAELEYESLKRQELESENKKLKNELNELRKAL-SEKSApevTAPGAPAYRVLMEQLTSVSEE 1258
Cdd:pfam01576 231 iaelraqlAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLeSERAA---RNKAEKQRRDLGEELEALKTE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1259 LD-------VRKEevliLRSQlvSQKEAIQPKNTMTDSTILLE-DVQKMKDKGEIAqayigLKETNRLLEsQLQSQKRSH 1330
Cdd:pfam01576 308 LEdtldttaAQQE----LRSK--REQEVTELKKALEEETRSHEaQLQEMRQKHTQA-----LEELTEQLE-QAKRNKANL 375
|
410
....*....|....*..
gi 2462544153 1331 ENEAEALRGEIQSLKEE 1347
Cdd:pfam01576 376 EKAKQALESENAELQAE 392
|
|
| CBD_MYO6-like |
cd21759 |
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ... |
810-837 |
4.32e-03 |
|
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).
Pssm-ID: 409646 [Multi-domain] Cd Length: 149 Bit Score: 39.41 E-value: 4.32e-03
10 20
....*....|....*....|....*...
gi 2462544153 810 KFLRRTKAATIIQKYWRMYVVRRRYKIR 837
Cdd:cd21759 40 KILYRREALIKIQKTVRGYLARKKHRPR 67
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
988-1337 |
4.41e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 988 LQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEentllkqekealnhrIVQQAKEMTETMeKKLVEETKQl 1067
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE---------------LREEAQELREKR-DELNEKVKE- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1068 eldLNDERlryQNLLNEFSRLEERYDDLKEEMtlmvhvpkpghkrtDSTHSSNESEYIFSSEIAEMEDipsrteepsekk 1147
Cdd:COG1340 76 ---LKEER---DELNEKLNELREELDELRKEL--------------AELNKAGGSIDKLRKEIERLEW------------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1148 vpldmslflKLQKRVTELEQEKQVMqDELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQElesenKKLKNELNELRK 1227
Cdd:COG1340 124 ---------RQQTEVLSPEEEKELV-EKIKELEKELEKAKKALEKNEKLKELRAELKELRKEA-----EEIHKKIKELAE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1228 ALSEKSapevtapgapayrvlmEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKNTMTDstilledvQKMKDKGEIAQ 1307
Cdd:COG1340 189 EAQELH----------------EEMIELYKEADELRKEADELHKEIVEAQEKADELHEEII--------ELQKELRELRK 244
|
330 340 350
....*....|....*....|....*....|
gi 2462544153 1308 AYIGLKETNRllESQLQSQKRSHENEAEAL 1337
Cdd:COG1340 245 ELKKLRKKQR--ALKREKEKEELEEKAEEI 272
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
925-1224 |
4.41e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 925 MENKIMQLQRKVDEQNKDYKCLVEKLTNLegiyNSETEKLRsdlERLQLSEEEAKvatgrvlSLQEEIAKLRKDLEQTRS 1004
Cdd:COG1340 20 LREEIEELKEKRDELNEELKELAEKRDEL----NAQVKELR---EEAQELREKRD-------ELNEKVKELKEERDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1005 EKKCIEEHADRYKQETEQLVSNLKEENTlLKQEKEALNHRivQQAKEMTETMEKKLVEETKQLELDLnDERLRYQNLLNE 1084
Cdd:COG1340 86 KLNELREELDELRKELAELNKAGGSIDK-LRKEIERLEWR--QQTEVLSPEEEKELVEKIKELEKEL-EKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1085 FSRLEERYDDLKEEMtlmvhvpkpghkrtdSTHSSNESEYifsseiaeMEDIPSRTEEPSEKKVPLDmslflKLQKRVTE 1164
Cdd:COG1340 162 LKELRAELKELRKEA---------------EEIHKKIKEL--------AEEAQELHEEMIELYKEAD-----ELRKEADE 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462544153 1165 LEQEKQVMQDELDRKEEQVLRSKAKEEE-RPQIRGAELEYESLKRQELESENKKLKNELNE 1224
Cdd:COG1340 214 LHKEIVEAQEKADELHEEIIELQKELRElRKELKKLRKKQRALKREKEKEELEEKAEEIFE 274
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
959-1098 |
4.48e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 959 SETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEK 1038
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462544153 1039 EALNHRIVQQAKEMTEtmEKKLVEETKQLELDLndERLRYQNL--LNEFSRLEERYDDLKEE 1098
Cdd:COG1196 746 ELLEEEALEELPEPPD--LEELERELERLEREI--EALGPVNLlaIEEYEELEERYDFLSEQ 803
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
937-1212 |
4.83e-03 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 42.03 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 937 DEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLErLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQ------TRSEKKCIE 1010
Cdd:COG5192 439 DENEDVDFTGKKGAINNEDESDNEEVAFDSDSQ-FDESEGNLRWKEGLASKLAYSQSGKRGRNIQkifydeSLSPEECIE 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1011 EHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTETMEkKLVEETKQleLDLNDERLRYQNLLNEFSRLEE 1090
Cdd:COG5192 518 EYKGESAKSSESDLVVQDEPEDFFDVSKVANESISSNHEKLMESEFE-ELKKKWSS--LAQLKSRFQKDATLDSIEGEEE 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1091 RYDDLkEEMTLMVHVPKPGHKRTDSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEKKVPLDMSLflklqkrvtELEQEKQ 1170
Cdd:COG5192 595 LIQDD-EKGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVDYETEREENARKKEELRGNF---------ELEERGD 664
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2462544153 1171 VMQDELDRKEEQvlrsKAKEEErpQIRGAELEYESL---KRQELE 1212
Cdd:COG5192 665 PEKKDVDWYTEE----KRKIEE--QLKINRSEFETMvpeSRVVIE 703
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
904-1086 |
4.96e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 904 ELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDykclVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVATG 983
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK----AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 984 RVLSLQEEIAKLRKDLEQTRSEKKC-IEEHAD----RYKQETEQLVSNLKeENTLLKQEKEALNHRIVQQAKEMtETMEK 1058
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAvIEEELDeedeKRRMEVDKKIKDIF-DNFANIIEGGKEGNLVINDSKEM-EDSAI 1832
|
170 180
....*....|....*....|....*...
gi 2462544153 1059 KLVEETKQLELDLNDERLRYQNLLNEFS 1086
Cdd:PTZ00121 1833 KEVADSKNMQLEEADAFEKHKFNKNNEN 1860
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
943-1085 |
4.97e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.02 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 943 YKCLVEKLTNLEGIYNSETEKLRSDLERLQL------SEEEAKVATGRVLSLQE-EIAKLRKDLEQTRSEKKCIEEHADR 1015
Cdd:cd16269 144 YQLYLEDREKLVEKYRQVPRKGVKAEEVLQEflqskeAEAEAILQADQALTEKEkEIEAERAKAEAAEQERKLLEEQQRE 223
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1016 YKQETEQLVSNLKEENTLLKQEKEAlnhRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEF 1085
Cdd:cd16269 224 LEQKLEDQERSYEEHLRQLKEKMEE---ERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSL 290
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
904-1102 |
5.68e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.95 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 904 ELKKL--KIEARSVERYKKlHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYN---SETEKLRSDLERLQlseeea 978
Cdd:pfam15905 160 ELMKLrnKLEAKMKEVMAK-QEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIeekSETEKLLEYITELS------ 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 979 kvatgrvlSLQEEIAKLRKDLEQtrsekkcIEEHADRYKQETEQLVSNLKEENTLLKqekealnhrivQQAKEMTETMek 1058
Cdd:pfam15905 233 --------CVSEQVEKYKLDIAQ-------LEELLKEKNDEIESLKQSLEEKEQELS-----------KQIKDLNEKC-- 284
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462544153 1059 KLVEetKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLM 1102
Cdd:pfam15905 285 KLLE--SEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKL 326
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1157-1374 |
5.76e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1157 KLQKRVTELE----QEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAELEYESlKRQELESENKKLKNELNELRKALSek 1232
Cdd:COG4717 50 RLEKEADELFkpqgRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEE-ELEELEAELEELREELEKLEKLLQ-- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1233 sapevTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEaiqpkntmtdstiLLEDVQKMKDkgEIAQAYIGL 1312
Cdd:COG4717 127 -----LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEE-------------LEAELAELQE--ELEELLEQL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462544153 1313 KETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQHE 1374
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
899-1233 |
5.92e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 899 MMAKRELKKLKIEARSVERYKklhigMENKIMQLQRKVDEQ-------NKDYKCLVEKLTNLEgiynSETEKLRSDLERL 971
Cdd:PRK02224 298 LLAEAGLDDADAEAVEARREE-----LEDRDEELRDRLEECrvaaqahNEEAESLREDADDLE----ERAEELREEAAEL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 972 QLSEEEAKVAT----GRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEAL--NHRI 1045
Cdd:PRK02224 369 ESELEEAREAVedrrEEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVeeAEAL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1046 VQQAK-----------EMTETMEKKLvEETKQLELDLNDERLryqnllnEFSRLEERYDDLKEEMTLMVHVPKPGHKRTD 1114
Cdd:PRK02224 449 LEAGKcpecgqpvegsPHVETIEEDR-ERVEELEAELEDLEE-------EVEEVEERLERAEDLVEAEDRIERLEERRED 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1115 SthssneseyifSSEIAEMEDipsRTEEPSEKKVpldmslflKLQKRVTELEQEKQVMQDELDRKEEQV--LRSKAKEEE 1192
Cdd:PRK02224 521 L-----------EELIAERRE---TIEEKRERAE--------ELRERAAELEAEAEEKREAAAEAEEEAeeAREEVAELN 578
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462544153 1193 RpqiRGAEL--EYESLKR------------QELESENKKLKN--ELNELRK-ALSEKS 1233
Cdd:PRK02224 579 S---KLAELkeRIESLERirtllaaiadaeDEIERLREKREAlaELNDERReRLAEKR 633
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
888-1234 |
6.65e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 888 AIIYLQCCFRRMMAKRELKKLKIEARSV----ERYKKLH-IGmenkimQLQRKVDEQNKDYKCLV-EKLTNLEG-IYNSE 960
Cdd:PRK04778 19 AGLILRKRNYKRIDELEERKQELENLPVndelEKVKKLNlTG------QSEEKFEEWRQKWDEIVtNSLPDIEEqLFEAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 961 --TEKLRSDLERLQLSEEEAKVAT--GRVLSLQEEIAKLRKDLEQTRSE-----------KKCIEEHADRYKQETEQLVS 1025
Cdd:PRK04778 93 elNDKFRFRKAKHEINEIESLLDLieEDIEQILEELQELLESEEKNREEveqlkdlyrelRKSLLANRFSFGPALDELEK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1026 NLKEENTLLKQ---EKEALNH----RIVQQAKEMTETMEKKlVEETKQLELDLNDE--------------------RLRY 1078
Cdd:PRK04778 173 QLENLEEEFSQfveLTESGDYvearEILDQLEEELAALEQI-MEEIPELLKELQTElpdqlqelkagyrelveegyHLDH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1079 QNLLNEFSRLEERYDDLKEEMtlmvhvpkpghKRTDSTHSSNESEYIfSSEIAEMEDIpSRTEEPSEKKVpldMSLFLKL 1158
Cdd:PRK04778 252 LDIEKEIQDLKEQIDENLALL-----------EELDLDEAEEKNEEI-QERIDQLYDI-LEREVKARKYV---EKNSDTL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1159 QKRVTELEQEKQVMQDELDR-------KEEQVLRSKAKEEERPQIRG--------------------AELEYESLKRQEL 1211
Cdd:PRK04778 316 PDFLEHAKEQNKELKEEIDRvkqsytlNESELESVRQLEKQLESLEKqydeiteriaeqeiayselqEELEEILKQLEEI 395
|
410 420
....*....|....*....|...
gi 2462544153 1212 ESENKKLKNELNELRKalSEKSA 1234
Cdd:PRK04778 396 EKEQEKLSEMLQGLRK--DELEA 416
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1039-1347 |
6.78e-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: 41.03 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1039 EALNHRIVQQAKEMTETMeKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMtlmvhvpkpghKRTDSTHS 1118
Cdd:pfam07888 30 ELLQNRLEECLQERAELL-QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEEL-----------RQSREKHE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1119 SNESEY----IFSSEIAEMEDIPSRTEEPSEKKVpldmslfLKLQKRVTELEQEKQVMQDELDRKEEQVLRS----KAKE 1190
Cdd:pfam07888 98 ELEEKYkelsASSEELSEEKDALLAQRAAHEARI-------RELEEDIKTLTQRVLERETELERMKERAKKAgaqrKEEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1191 EERPQIRgAELEYESLKRQELESENKKLKNELNE-------LRKALSEKSAPEVTAPGAPA-YRVLMEQLTSVSEELDVR 1262
Cdd:pfam07888 171 AERKQLQ-AKLQQTEEELRSLSKEFQELRNSLAQrdtqvlqLQDTITTLTQKLTTAHRKEAeNEALLEELRSLQERLNAS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1263 KEEVLILRSQLVSQkeAIQPKNTMTDstILLEDVQKMKDKGEIAQAYIGLKETnrllESQLQSQKRSHENEAEALRGEIQ 1342
Cdd:pfam07888 250 ERKVEGLGEELSSM--AAQRDRTQAE--LHQARLQAAQLTLQLADASLALREG----RARWAQERETLQQSAEADKDRIE 321
|
....*
gi 2462544153 1343 SLKEE 1347
Cdd:pfam07888 322 KLSAE 326
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1269-1345 |
6.88e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 40.73 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1269 LRSQLVSQKEAIQPKNTMTDSTilLEDVQKMKDKGEIAQAYIgLKETNRLLESQLQSQKR----SHENEAEALRGEIQSL 1344
Cdd:pfam02841 220 QELLREKQKEEEQMMEAQERSY--QEHVKQLIEKMEAEREQL-LAEQERMLEHKLQEQEEllkeGFKTEAESLQKEIQDL 296
|
.
gi 2462544153 1345 K 1345
Cdd:pfam02841 297 K 297
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
925-1018 |
7.14e-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: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 925 MENKIMQLQRKVDE---QNKDYKCLVEKLtnlegiyNSETEKLRSDLERLQlSEEEAKVATGRVLS-LQEEIAKLRKDLE 1000
Cdd:COG2433 411 EEEEIRRLEEQVERleaEVEELEAELEEK-------DERIERLERELSEAR-SEERREIRKDREISrLDREIERLERELE 482
|
90
....*....|....*...
gi 2462544153 1001 QTRSEKKCIEEHADRYKQ 1018
Cdd:COG2433 483 EERERIEELKRKLERLKE 500
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1034-1445 |
7.31e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1034 LKQEKEALnHRIVQQAKEMTETMEKKLVEETKQLEldlnDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHvpkpgHKRT 1113
Cdd:COG4717 51 LEKEADEL-FKPQGRKPELNLKELKELEEELKEAE----EKEEEYAELQEELEELEEELEELEAELEELRE-----ELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1114 DSTHSSNESEYIFSSEI-AEMEDIPSRTEEPSEKKVPLdmslfLKLQKRVTELEQEKQVMQDELDRKEEQVlrskaKEEE 1192
Cdd:COG4717 121 LEKLLQLLPLYQELEALeAELAELPERLEELEERLEEL-----RELEEELEELEAELAELQEELEELLEQL-----SLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1193 RPQIRGAELEYESL--KRQELESENKKLKNELNELRKALSEKSAPEVTAP--------------------GAPAYRVLME 1250
Cdd:COG4717 191 EEELQDLAEELEELqqRLAELEEELEEAQEELEELEEELEQLENELEAAAleerlkearlllliaaallaLLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1251 QLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETNRLLESQLQSQKRSH 1330
Cdd:COG4717 271 LILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1331 ENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQH--EITRLTNENLYFEELYADDPKKYQSYRISLYKRmi 1408
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQaeEYQELKEELEELEEQLEELLGELEELLEALDEE-- 428
|
410 420 430
....*....|....*....|....*....|....*....
gi 2462544153 1409 DLMEQLEKQDKTVRKLKKQLKVFAKKIGEL--EVGQMEN 1445
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELeaELEQLEE 467
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
862-883 |
7.63e-03 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 35.38 E-value: 7.63e-03
|
| Rabaptin |
pfam03528 |
Rabaptin; |
932-1214 |
7.83e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 40.86 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 932 LQRKVDEQNKDYKCLVEKLTNLEGIYNSEteklRSDLERLQLS-EEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIE 1010
Cdd:pfam03528 6 LQQRVAELEKENAEFYRLKQQLEAEFNQK----RAKFKELYLAkEEDLKRQNAVLQEAQVELDALQNQLALARAEMENIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1011 EHA---DRYKQET-EQLVSNLKEENTLLK-------QEKEALNHRIVQQAK----EMTETMEKKLVEETKQLEldlndER 1075
Cdd:pfam03528 82 AVAtvsENTKQEAiDEVKSQWQEEVASLQaimketvREYEVQFHRRLEQERaqwnQYRESAEREIADLRRRLS-----EG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462544153 1076 LRYQNLLNEFSRLEERYDDLKEEMTLMVH-VPKPGHKRTDSTHSSNESEyifSSEIAEMEDIPSrteepSEKKVPLDMSL 1154
Cdd:pfam03528 157 QEEENLEDEMKKAQEDAEKLRSVVMPMEKeIAALKAKLTEAEDKIKELE---ASKMKELNHYLE-----AEKSCRTDLEM 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462544153 1155 FlklqkrVTELEQEKQVMQDELD--RKEEQVLRSKAkEEERPQIRGAELEYESLKRQELESE 1214
Cdd:pfam03528 229 Y------VAVLNTQKSVLQEDAEklRKELHEVCHLL-EQERQQHNQLKHTWQKANDQFLESQ 283
|
|
|