|
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: 1318.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd01380 1 PAVLHNLKVRFCQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 163 GESGAGKTVSAKYAMRYFATVSGSAS-EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATVGGSSSgETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 242 YLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISESH 321
Cdd:cd01380 161 YLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 322 QMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQATNARD 401
Cdd:cd01380 241 QMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 402 ALAKHIYAKLFNWIVDHVNQALHSAV--KQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 479
Cdd:cd01380 321 ALAKHIYAQLFDWIVDRINKALASPVkeKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 480 EQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNK-CALFEKPRLSNKAFIIQHFADKVE 558
Cdd:cd01380 401 EEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTAFIVKHFADDVE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 559 YQCEGFLEKNKDTVFEEQIKVLKSSKFkmlpelfqddekaisptsatssgrtpltrtlskptkgrpgqtakeHKKTVGHQ 638
Cdd:cd01380 481 YQVEGFLEKNRDTVSEEHLNVLKASKN---------------------------------------------RKKTVGSQ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 639 FRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKD 718
Cdd:cd01380 516 FRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKE 595
|
650 660 670
....*....|....*....|....*....|....
gi 1542868643 719 VL-SDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 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: 1079.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 72 NDLTALSYLHEPAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMA 151
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRY-KSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 152 RDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEAN---VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGF 228
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNvgrLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 229 DKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPVIEGVDDAKEMAHT 308
Cdd:pfam00063 161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 309 RQACTLLGISESHQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYI 388
Cdd:pfam00063 241 DKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETVS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 389 KPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHS-AVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNM 467
Cdd:pfam00063 321 KPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVkTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 468 HVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKPRL-SN 545
Cdd:pfam00063 401 HMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKpLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHFQKPRLqGE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 546 KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSgrtpltrtlskptKGRPG 625
Cdd:pfam00063 480 THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESG-------------KSTPK 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 626 QTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:pfam00063 547 RTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQE 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1542868643 706 FFSRYRVLMKQKDV--LSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 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: 1021.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 64 NPDILVGENDLTALSYLHEPAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVA 143
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRY-LKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 144 EEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEAN-VEEKVLASNPIMESIGNAKTTRNDNSSRFGK 222
Cdd:smart00242 80 DNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGsVEDQILESNPILEAFGNAKTLRNNNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 223 YIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPVIEGVDDA 302
Cdd:smart00242 160 FIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 303 KEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVVFMSRDSD-SCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLA 381
Cdd:smart00242 240 EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDnAASTVKDKEELSNAAELLGVDPEELEKALTKRKIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 382 TATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKL 461
Cdd:smart00242 320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 462 QQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEK 540
Cdd:smart00242 400 QQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKpPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFSKP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 541 PRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkaispTSATSSGRtpltrtlskpt 620
Cdd:smart00242 480 KKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGV-----SNAGSKKR----------- 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 621 kgrpgqtakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSR 700
Cdd:smart00242 544 -----------FQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYR 612
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1542868643 701 WTYQEFFSRYRVLMKQK--DVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFRAGQVAYLEKLR 762
Cdd:smart00242 613 LPFDEFLQRYRVLLPDTwpPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
7-1233 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 968.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 7 YTKFARVWIPDPEEVWKSAELLK-DYKPGDKVLLLQLEDG-------KDLEYRLDpktkelphlrNPDILVGENDLTALS 78
Cdd:COG5022 6 AEVGSGCWIPDEEKGWIWAEIIKeAFNKGKVTEEGKKEDGesvsvkkKVLGNDRI----------KLPKFDGVDDLTELS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 79 YLHEPAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQS 158
Cdd:COG5022 76 YLNEPAVLHNLEKRY-NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 159 IIVSGESGAGKTVSAKYAMRYFATVSGSASE--ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIG 236
Cdd:COG5022 155 IIISGESGAGKTENAKRIMQYLASVTSSSTVeiSSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 237 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLG 316
Cdd:COG5022 235 AKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 317 ISESHQMGIFRILAGILHLGNVVFMSrDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQA 396
Cdd:COG5022 315 IDEEEQDQIFKILAAILHIGNIEFKE-DRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 397 TNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:COG5022 394 LAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEE 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 477 YMKEQIPWTLIDFYDNQPCINLIESK--LGILDLLDEECKMPKGTDDTWAQKLYNT-HLNKCALFEKPRLSNKAFIIQHF 553
Cdd:COG5022 474 YVKEGIEWSFIDYFDNQPCIDLIEKKnpLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNKFVVKHY 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 554 ADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKaisptsatssgrtpltrtlsKPTKGRPgqtakehkK 633
Cdd:COG5022 554 AGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEEN--------------------IESKGRF--------P 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 634 TVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVL 713
Cdd:COG5022 606 TLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRIL 685
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 714 MKQK------DVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFRAGQVAYLEKLRADKLRAACIRIQKTIRGWLLRKKYL 787
Cdd:COG5022 686 SPSKswtgeyTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYL 765
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 788 RMRKAAITVQRYVRGHQARCYAKFLRRTKAATIIQKYWRMYVARRRYKITRTATIVLQSYL-RGYLARNRYHKILREHKA 866
Cdd:COG5022 766 QALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIkREKKLRETEEVEFSLKAE 845
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 867 VIIQKWVRGWLARTCYRRSIHAIIYLQCCFRRMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQ-NKDYKC 945
Cdd:COG5022 846 VLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDlIENLEF 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 946 LMEKLTNLEGIYNSETEKLRSDLERLQLSEeeakiatgrVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVS 1025
Cdd:COG5022 926 KTELIARLKKLLNNIDLEEGPSIEYVKLPE---------LNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKN 996
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1026 NLKEENTLLKQEKEVLNHriVEQAKEMT------ETMEKKLVEETKQLELDLNDERLRYQNLLnEFSRLEERYDDLKeem 1099
Cdd:COG5022 997 FKKELAELSKQYGALQES--TKQLKELPvevaelQSASKIISSESTELSILKPLQKLKGLLLL-ENNQLQARYKALK--- 1070
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1100 tlmvnVPKPGHKRTDSTHSSNESEYTFSSEIAETE----DIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQ-----EKQ 1170
Cdd:COG5022 1071 -----LRRENSLLDDKQLYQLESTENLLKTINVKDlevtNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQlvntlEPV 1145
|
1210 1220 1230 1240 1250 1260
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1542868643 1171 VMQDELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQE--LESENKKLKNELNELRKALSEKS 1233
Cdd:COG5022 1146 FQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSalYDEKSKLSSSEVNDLKNELIALF 1210
|
|
| 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: 885.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMG-DMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd00124 1 AAILHNLRERY-ARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 162 SGESGAGKTVSAKYAMRYFATVSGSAS------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRII 235
Cdd:cd00124 80 SGESGAGKTETTKLVLKYLAALSGSGSskssssASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 236 GANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANN----FHYTNQGGSPVIEGVDDAKEMAHTRQA 311
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSyyylNDYLNSSGCDRIDGVDDAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 312 CTLLGISESHQMGIFRILAGILHLGNVVFMSRDSD--SCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIK 389
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 390 PISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQH--SFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNM 467
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 468 HVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNK 546
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKpLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAKL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 547 AFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKfkmlpelfqddekaisptsatssgrtpltrtlskptkgrpgq 626
Cdd:cd00124 480 EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS------------------------------------------ 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 627 takehkktvghQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEF 706
Cdd:cd00124 518 -----------QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEF 586
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1542868643 707 FSRYRVLMKQKDVLSDR--KQTCKNVLEKLIVDKDKYQFGKTKIFFR 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: 799.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd01377 1 ASVLHNLRERY-YSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 163 GESGAGKTVSAKYAMRYFATVSGSA--------SEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRI 234
Cdd:cd01377 80 GESGAGKTENTKKVIQYLASVAASSkkkkesgkKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 235 IGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTL 314
Cdd:cd01377 160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 315 LGISESHQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISKL 394
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 395 QATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 474
Cdd:cd01377 320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 475 EEYMKEQIPWTLIDF-YDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR--LSNKAFII 550
Cdd:cd01377 400 EEYKKEGIEWTFIDFgLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKpkKSEAHFIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 551 QHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLtrtlskptkgrpgqtake 630
Cdd:cd01377 480 KHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGGGKKKKKGGSF------------------ 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 631 hkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRY 710
Cdd:cd01377 542 --RTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRY 619
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1542868643 711 RVLMKQ--KDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 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: 773.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd01384 1 PGVLHNLKVRY-ELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 162 SGESGAGKTVSAKYAMRYFATVSGSAS--EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANM 239
Cdd:cd01384 80 SGESGAGKTETTKMLMQYLAYMGGRAVteGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 240 RTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISE 319
Cdd:cd01384 160 RTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 320 SHQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEP---LSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQA 396
Cdd:cd01384 240 EEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSefhLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 397 TNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:cd01384 320 TLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 477 YMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNThLNKCALFEKPRLSNKAFIIQHFAD 555
Cdd:cd01384 400 YTKEEIDWSYIEFVDNQDVLDLIEKKpGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKPKLSRTDFTIDHYAG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekAISPTSATSSGrtpltrtlSKPTkgrpgqtakehkkTV 635
Cdd:cd01384 479 DVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLF-----PPLPREGTSSS--------SKFS-------------SI 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK 715
Cdd:cd01384 533 GSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAP 612
|
650 660 670
....*....|....*....|....*....|....*..
gi 1542868643 716 QKDVLS-DRKQTCKNVLEKliVDKDKYQFGKTKIFFR 751
Cdd:cd01384 613 EVLKGSdDEKAACKKILEK--AGLKGYQIGKTKVFLR 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: 758.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 84 AVLHNLRVRFIDsKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd01381 2 GILRNLLIRYRE-KLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 164 ESGAGKTVSAKYAMRYFATVSGSASEanVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYL 243
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHSW--IEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 244 LEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQM 323
Cdd:cd01381 159 LEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 324 GIFRILAGILHLGNVVFMSRDS---DSCTIpPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQATNAR 400
Cdd:cd01381 239 DIFKLLAAILHLGNIKFEATVVdnlDASEV-RDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 401 DALAKHIYAKLFNWIVDHVNQALHSAVKQHSF---IGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEY 477
Cdd:cd01381 318 DAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 478 MKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPR-LSNKAFIIQHFAD 555
Cdd:cd01381 398 DKEGINWQHIEFVDNQDVLDLIALKpMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNN-KNYLKPKsDLNTSFGINHFAG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkaisPTSATSSGRTPltrtlskptkgrpgqtakehkkTV 635
Cdd:cd01381 477 VVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDI----SMGSETRKKSP----------------------TL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK 715
Cdd:cd01381 531 SSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP 610
|
650 660 670
....*....|....*....|....*....|....*...
gi 1542868643 716 --QKDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 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: 740.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDmdPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd01383 1 PSVLHNLEYRY-SQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKLLDS--PHVYAVADTAYREMMRDEINQSIIIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 163 GESGAGKTVSAKYAMRYFATVSGSASeaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTY 242
Cdd:cd01383 78 GESGAGKTETAKIAMQYLAALGGGSS--GIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 243 LLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQ 322
Cdd:cd01383 156 LLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKEDQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 323 MGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQATNARDA 402
Cdd:cd01383 236 EHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 403 LAKHIYAKLFNWIVDHVNQALHSAVKQHS-FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQ 481
Cdd:cd01383 316 LAKAIYASLFDWLVEQINKSLEVGKRRTGrSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 482 IPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLyNTHLNKCALFEKPRlsNKAFIIQHFADKVEYQ 560
Cdd:cd01383 396 IDWTKVDFEDNQECLDLIEKKpLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCFKGER--GGAFTIRHYAGEVTYD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 561 CEGFLEKNKDTVFEEQIKVLKSSKFKmLPELF-----QDDEKAISPTSATSSGRTpltrtlskptkgrpgqtakehKKTV 635
Cdd:cd01383 473 TSGFLEKNRDLLHSDLIQLLSSCSCQ-LPQLFaskmlDASRKALPLTKASGSDSQ---------------------KQSV 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLM- 714
Cdd:cd01383 531 ATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLp 610
|
650 660 670
....*....|....*....|....*....|....*..
gi 1542868643 715 KQKDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd01383 611 EDVSASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| 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: 725.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14883 2 GINTNLKVRY-KKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 164 ESGAGKTVSAKYAMRYFATVSGSASEanVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYL 243
Cdd:cd14883 81 ESGAGKTETTKLILQYLCAVTNNHSW--VEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 244 LEKSRVVFQAEEERNYHIFYQLCASADLS-EFK-VLRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISESH 321
Cdd:cd14883 159 LEQSRITFQAPGERNYHVFYQLLAGAKHSkELKeKLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPEEM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 322 QMGIFRILAGILHLGNVVFMSRDSDSCTIPPKH-EPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQATNAR 400
Cdd:cd14883 239 QEGIFSVLSAILHLGNLTFEDIDGETGALTVEDkEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 401 DALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKE 480
Cdd:cd14883 319 DAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 481 QIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKP--RLSNKAFIIQHFADKV 557
Cdd:cd14883 399 GINWSHIVFTDNQECLDLIEKPpLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPdrRRWKTEFGVKHYAGEV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 558 EYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQ-DDEKAISPTSATSSGRTPLTRTlskpTKGRPgqtakehkkTVG 636
Cdd:cd14883 478 TYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTyPDLLALTGLSISLGGDTTSRGT----SKGKP---------TVG 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 637 HQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQ 716
Cdd:cd14883 545 DTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPR 624
|
650 660 670
....*....|....*....|....*....|....*..
gi 1542868643 717 KDVLSDRKQ--TCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14883 625 ARSADHKETcgAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| Myo5a_CBD |
cd15478 |
Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, ... |
1479-1853 |
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 1542868643 1479 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 1558
Cdd:cd15478 1 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1559 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 1638
Cdd:cd15478 81 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1639 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAVTLNNLLLRKDMCSWSKGMQIR 1718
Cdd:cd15478 161 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1719 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 1798
Cdd:cd15478 241 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1542868643 1799 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 1853
Cdd:cd15478 321 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 375
|
|
| 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: 715.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd01378 2 AINENLKKRF-ENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 164 ESGAGKTVSAKYAMRYFATVSGSaSEANVE---EKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMR 240
Cdd:cd01378 81 ESGAGKTEASKRIMQYIAAVSGG-SESEVErvkDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHIT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 241 TYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISES 320
Cdd:cd01378 160 NYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 321 HQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKhEPLSIFCDLMGVDFEELCHWLCHRKLATATE---TYIKPISKLQAT 397
Cdd:cd01378 240 EQDSIFRILAAILHLGNIQFAEDEEGNAAISDT-SVLDFVAYLLGVDPDQLEKALTHRTIETGGGgrsVYEVPLNVEQAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 398 NARDALAKHIYAKLFNWIVDHVNQALHSAVKQHS-FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:cd01378 319 YARDALAKAIYSRLFDWIVERINKSLAAKSGGKKkVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 477 YMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECK-MPKGTDDTWAQKLyNTHLNKCALFEKP----RLSNKAFII 550
Cdd:cd01378 399 YVREGIEWTPIKYFNNKIICDLIEEKpPGIFAILDDACLtAGDATDQTFLQKL-NQLFSNHPHFECPsghfELRRGEFRI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 551 QHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKaisptsatssgrtpltrtlsKPTKGRPgqtake 630
Cdd:cd01378 478 KHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD--------------------LDSKKRP------ 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 631 hkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRY 710
Cdd:cd01378 532 --PTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERY 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1542868643 711 RVLMK----------QKDVLSDRKQTCknvlekliVDKDKYQFGKTKIFFR 751
Cdd:cd01378 610 KLLSPktwpawdgtwQGGVESILKDLN--------IPPEEYQMGKTKIFIR 652
|
|
| Myo5b_CBD |
cd15477 |
Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, ... |
1479-1850 |
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: 646.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1479 KEDEQKLVKNLILELKPRGVAVNlIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 1558
Cdd:cd15477 1 KEDEALLIRNLVTDLKPQAVSAT-VPCLPAYILYMCIRHADYINDDQKVHSLLTSTINGIKKVLKKHNDDFEMTSFWLAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1559 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 1638
Cdd:cd15477 80 TCRLLHCLKQYSGDEGFMTQNTAKQNEHCLKNFDLTEYRQVLSDLSIQIYQQLIKIAEGILQPMIVSAMLENESIQGLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1639 VKPTGLRKRTSSIAD-EGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAVTLNNLLLRKDMCSWSKGMQI 1717
Cdd:cd15477 160 VKPMGYRKRSSSMADgDNSYTLEALIRQLNTFHSIMCDQGLDPEIIQQVFKQLFYMINAVTLNNLLLRKDVCSWSTGMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1718 RYNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVS 1797
Cdd:cd15477 240 RYNISQLEEWLRGRNLHQSGAAQTMEPLIQAAQLLQLKKKTSEDAEAICSLCTALSTQQIVKILNLYTPLNEFEERVTVS 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1542868643 1798 FIRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFI 1850
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: 641.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14903 1 AAILYNVKKRFL-RKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 162 SGESGAGKTVSAKYAMRYFATVSGSASEANVEeKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:cd14903 80 SGESGAGKTETTKILMNHLATIAGGLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 242 YLLEKSRVVFQAEEERNYHIFYQLCASADLSEfkVLRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISESH 321
Cdd:cd14903 159 YLLEKTRVISHERPERNYHIFYQLLASPDVEE--RLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 322 QMGIFRILAGILHLGNVVFMSRDSD--SCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQATNA 399
Cdd:cd14903 237 QEVLFEVLAGILHLGQLQIQSKPNDdeKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDC 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 400 RDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 479
Cdd:cd14903 317 RDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 480 EQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKAFIIQHFADKVEY 559
Cdd:cd14903 397 EGIRWAHIDFADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSRTQFTIKHYAGPVTY 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 560 QCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqdDEKAISPTSATSSGRTPltrtlskptkGRPGQTAKEHKKTVGHQF 639
Cdd:cd14903 477 ESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLF--KEKVESPAAASTSLARG----------ARRRRGGALTTTTVGTQF 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 640 RNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQK-D 718
Cdd:cd14903 545 KDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGrN 624
|
650 660 670
....*....|....*....|....*....|....
gi 1542868643 719 VLSDRKQTCKNVLEKLIVDK-DKYQFGKTKIFFR 751
Cdd:cd14903 625 TDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| 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: 631.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14872 1 AMIVHNLRKRFKNDQ-IYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 163 GESGAGKTVSAKYAMRYFATVSGSASeaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTY 242
Cdd:cd14872 80 GESGAGKTEATKQCLSFFAEVAGSTN--GVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 243 LLEKSRVVFQAEEERNYHIFYQLCASADLSefKVLRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQ 322
Cdd:cd14872 158 LLEKSRVVYQIKGERNFHIFYQLLASPDPA--SRGGWGSSAAYGYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFDDADI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 323 MGIFRILAGILHLGNVVF---MSRDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLAT-ATETYIKPISKLQATN 398
Cdd:cd14872 236 NNVMSLIAAILKLGNIEFasgGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLTPAQATD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 399 ARDALAKHIYAKLFNWIVDHVNQALHSA-VKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEY 477
Cdd:cd14872 316 ACDALAKAAYSRLFDWLVKKINESMRPQkGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEALY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 478 MKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTH-LNKCALFEKPRLSNKAFIIQHFAD 555
Cdd:cd14872 396 QSEGVKFEHIDFIDNQPVLDLIEKKQpGLMLALDDQVKIPKGSDATFMIAANQTHaAKSTFVYAEVRTSRTEFIVKHYAG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkaisptsatssgrtpltrtLSKPTKgrpgqtakehKKTV 635
Cdd:cd14872 476 DVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSE-------------------GDQKTS----------KVTL 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK 715
Cdd:cd14872 527 GGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVK 606
|
650 660 670
....*....|....*....|....*....|....*...
gi 1542868643 716 --QKDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14872 607 tiAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 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: 629.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 86 LHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGES 165
Cdd:cd01385 4 LENLRARFKHGK-IYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 166 GAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLE 245
Cdd:cd01385 83 GSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 246 KSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQMGI 325
Cdd:cd01385 163 KSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQRQI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 326 FRILAGILHLGNVVFMSRD---SDSCTIPPKhEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQATNARDA 402
Cdd:cd01385 243 FSVLSAVLHLGNIEYKKKAyhrDESVTVGNP-EVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 403 LAKHIYAKLFNWIVDHVNQAL----HSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYM 478
Cdd:cd01385 322 MAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 479 KEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKlYNTHLNKCALFEKPRLSNKAFIIQHFADKV 557
Cdd:cd01385 402 KEGISWHNIEYTDNTGCLQLISKKpTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQVMEPAFIIAHYAGKV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 558 EYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAI-----------------SPTSATSSGRTPLTRTLSKP- 619
Cdd:cd01385 481 KYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVAVfrwavlrafframaafrEAGRRRAQRTAGHSLTLHDRt 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 620 TKGRPGQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPS 699
Cdd:cd01385 561 TKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSV 640
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1542868643 700 RWTYQEFFSRYRVLMKqKDVLSdRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd01385 641 RYTFQEFITQFQVLLP-KGLIS-SKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| 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 1542868643 86 LHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 164
Cdd:cd01382 4 LNNIRVRYSKDK-IYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 165 SGAGKTVSAKYAMRYFATVSGSASeANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 244
Cdd:cd01382 83 SGAGKTESTKYILRYLTESWGSGA-GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 245 EKSRVVFQAEEERNYHIFYQLCASADLSEFKVLrLGDANnfhytnqggspviegVDDAKEMAHTRQACTLLGISESHQMG 324
Cdd:cd01382 162 EKSRICVQSKEERNYHIFYRLCAGAPEDLREKL-LKDPL---------------LDDVGDFIRMDKAMKKIGLSDEEKLD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 325 IFRILAGILHLGNVVFMSRDSDS---CTIPPKHEP-LSIFCDLMGVDFEELCHWLCHRKLATATE----TYIK-PISKLQ 395
Cdd:cd01382 226 IFRVVAAVLHLGNIEFEENGSDSgggCNVKPKSEQsLEYAAELLGLDQDELRVSLTTRVMQTTRGgakgTVIKvPLKVEE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 396 ATNARDALAKHIYAKLFNWIVDHVNQAL---HSAvkqhSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKL 472
Cdd:cd01382 306 ANNARDALAKAIYSKLFDHIVNRINQCIpfeTSS----YFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 473 EQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPRLS------- 544
Cdd:cd01382 382 EQELYEKEGLGVKEVEYVDNQDCIDLIEAKLvGILDLLDEESKLPKPSDQHFTSAVHQKHKNH-FRLSIPRKSklkihrn 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 545 ---NKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAiSPTSATSSGRTPLtrtlskptk 621
Cdd:cd01382 461 lrdDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNN-NKDSKQKAGKLSF--------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 622 grpgqtakehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRW 701
Cdd:cd01382 531 -----------ISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRT 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1542868643 702 TYQEFFSRYRVLMKQKDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd01382 600 SFHDLYNMYKKYLPPKLARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| Myo5_CBD |
cd15470 |
Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, ... |
1480-1846 |
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: 614.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1480 EDEQKLVKNLILELKPRGvAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNT 1559
Cdd:cd15470 1 EDESRLIKNLITDLKPRG-AVGLLPGLPAYILFMCIRHADYVNDEAKVRSLLTATINAIKKVLKKHSEDFEMLSFWLVNT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1560 CRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmivsgmlehetiqgvsgv 1639
Cdd:cd15470 80 CRLLNCLKQYSGEEEFMKHNTPKQNEHCLKNFDLSEYRQVLSDLAIQIYQQLIKRAEEILQP------------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1640 kptglrkrtssiadegtyTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAVTLNNLLLRKDMCSWSKGMQIRY 1719
Cdd:cd15470 142 ------------------TLDSLLQQLNSFHTTLTQHGLDPELIKQVFRQLFYLICASTLNNLLLRKDLCSWSKGMQIRY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1720 NVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFI 1799
Cdd:cd15470 204 NVSQLEEWLRDKGLQDSGARETLEPLIQAAQLLQVKKTTEEDAQSICEMCTKLTTAQIVKILNLYTPVDDFEERVTPSFI 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1542868643 1800 RTIQMRLRDRKDSP--QLLMDAKHIFPVTFPFNPSSLALETIQIPASLG 1846
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: 614.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd01387 2 TVLWNLKTRY-ERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 164 ESGAGKTVSAKYAMRYFATVSGSAsEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMRTYL 243
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRR-NNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAITSQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 244 LEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQM 323
Cdd:cd01387 159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 324 GIFRILAGILHLGNVVFMSRDSDSctippKHEPLSIFCD--------LMGVDFEELCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd01387 239 SIFRILASVLHLGNVYFHKRQLRH-----GQEGVSVGSDaeiqwvahLLQISPEGLQKALTFKVTETRRERIFTPLTIDQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQE 475
Cdd:cd01387 314 ALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 476 EYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKL-YNTHLNKcaLFEKPRLSNKAFIIQHF 553
Cdd:cd01387 394 EYIREQIDWTEIAFADNQPVINLISKKpVGILHILDDECNFPQATDHSFLEKChYHHALNE--LYSKPRMPLPEFTIKHY 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 554 ADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaisptsatssgRTPLTRTLSKPTKGRpGQTAKEHKK 633
Cdd:cd01387 472 AGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSH-------------RAQTDKAPPRLGKGR-FVTMKPRTP 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 634 TVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVL 713
Cdd:cd01387 538 TVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1542868643 714 MKQKDVLSDRKQTCKNVLEKL--IVDKDKYQFGKTKIFFR 751
Cdd:cd01387 618 VALKLPRPAPGDMCVSLLSRLctVTPKDMYRLGATKVFLR 657
|
|
| 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: 604.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 84 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14873 2 SIMYNLFQRYKRNQ-IYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 163 GESGAGKTVSAKYAMRYFATVS-------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRII 235
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISqqslelsLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 236 GANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLL 315
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 316 GISESHQMGIFRILAGILHLGNVVFMSrdSDSCTIPPKhEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEFIT--AGGAQVSFK-TALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAvKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQE 475
Cdd:cd14873 318 AVDSRDSLAMALYARCFEWVIKKINSRIKGK-EDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 476 EYMKEQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPRLSNKAFIIQHFAD 555
Cdd:cd14873 397 EYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANN-HFYVKPRVAVNNFGVKHYAG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaisptSATSSGRTpltrtlskptkgrPGQTAKEHKKTV 635
Cdd:cd14873 476 EVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHV-------SSRNNQDT-------------LKCGSKHRRPTV 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK 715
Cdd:cd14873 536 SSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMR 615
|
650 660 670
....*....|....*....|....*....|....*.
gi 1542868643 716 QKDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14873 616 NLALPEDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| 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: 601.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMAR----DERNQS 158
Cdd:cd14890 2 SLLHTLRLRY-ERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 159 IIVSGESGAGKTVSAKYAMRYFATVS-----------------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFG 221
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITsgfaqgasgegeaaseaIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 222 KYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTnQGGSPVIEGVDD 301
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYL-RGECSSIPSCDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 302 AKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVVF-MSRDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKL 380
Cdd:cd14890 240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFeSENDTTVLEDATTLQSLKLAAELLGVNEDALEKALLTRQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 381 ATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEK 460
Cdd:cd14890 320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 461 LQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL----GILDLLDeECKMPKGTDdtwAQKLYNTHLNkcA 536
Cdd:cd14890 400 LQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVngkpGIFITLD-DCWRFKGEE---ANKKFVSQLH--A 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 537 LFEKPRLSNKA--------------------FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSkfkmlpelfqdde 596
Cdd:cd14890 474 SFGRKSGSGGTrrgssqhphfvhpkfdadkqFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQS------------- 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 597 kaisptsatssgrtplTRTLskptkgrpgqtakeHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKR 676
Cdd:cd14890 541 ----------------RRSI--------------REVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLD 590
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1542868643 677 AVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLsdrKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14890 591 CLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTAENI---EQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| 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: 594.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAY---SGQNMGD---MDPHIFAVAEEAYKQMARDER- 155
Cdd:cd14901 1 PSILHVLRRRF-AHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehGERRAAGerkLPPHVYAVADKAFRAMLFASRg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 156 ---NQSIIVSGESGAGKTVSAKYAMRYFATVS-------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIE 225
Cdd:cd14901 80 qkcDQSILVSGESGAGKTETTKIIMNYLASVSsatthgqNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 226 IGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPV-IEGVDDAKE 304
Cdd:cd14901 160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDrRDGVDDSVQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 305 MAHTRQACTLLGISESHQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEP-LSIFCDLMGVDFEELCHWLCHRKLATA 383
Cdd:cd14901 240 YAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLAnVRAACDLLGLDMDVLEKTLCTREIRAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 384 TETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQAL--HSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKL 461
Cdd:cd14901 320 GEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIaySESTGASRFIGIVDIFGFEIFATNSLEQLCINFANEKL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 462 QQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNThLNKCALFEK 540
Cdd:cd14901 400 QQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARpTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHASFSV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 541 PRLSN--KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPelfqddekaisptsatssgrtpltrtlsk 618
Cdd:cd14901 479 SKLQQgkRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS----------------------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 619 ptkgrpgqtakehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFP 698
Cdd:cd14901 530 --------------STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYP 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1542868643 699 SRWTYQEFFSRYRVLMKQK-------DVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIF 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: 568.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSgQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14888 1 ASILHSLNLRF-DIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 162 SGESGAGKTVSAKYAMRYFATVsGSASE---ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDK-------- 230
Cdd:cd14888 79 SGESGAGKTESTKYVMKFLACA-GSEDIkkrSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskrmsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 231 -RYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASA----------------------------DLSEFKvlrlgD 281
Cdd:cd14888 158 dRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAreakntglsyeendeklakgadakpisiDMSSFE-----P 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 282 ANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVVF-MSRDSDSCTI--PPKHEPLS 358
Cdd:cd14888 233 HLKFRYLTKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFeNNEACSEGAVvsASCTDDLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 359 IFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQAL-HSAVKQHSFIGVLD 437
Cdd:cd14888 313 KVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIgYSKDNSLLFCGVLD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 438 IYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMP 516
Cdd:cd14888 393 IFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKpLGIFCMLDEECFVP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 517 KGTDDTWAQKLYNTHLNKcALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQdde 596
Cdd:cd14888 473 GGKDQGLCNKLCQKHKGH-KRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFS--- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 597 kaisptsatssgrtpltrtlSKPTKGRPGQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKR 676
Cdd:cd14888 549 --------------------AYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRIS 608
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1542868643 677 AVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkqkdvlsdRKQTCKNVLEklivdkdkYQFGKTKIFFR 751
Cdd:cd14888 609 VNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILL--------NGEGKKQLSI--------WAVGKTLCFFK 667
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
89-751 |
0e+00 |
|
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: 567.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 89 LRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGE--DIINAYSGQNMGDMD-PHIFAVAEEAYKQMARD----ERNQSIIV 161
Cdd:cd14892 7 LRRRY-ERDAIYTFTADILISINPYKSIPLLYDvpGFDSQRKEEATASSPpPHVFSIAERAYRAMKGVgkgqGTPQSIVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 162 SGESGAGKTVSAKYAMRYFATVSGSASEA-----------NVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDK 230
Cdd:cd14892 86 SGESGAGKTEASKYIMKYLATASKLAKGAstskgaanaheSIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 231 RYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQ 310
Cdd:cd14892 166 DGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVDGVDDATEFKQLRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 311 ACTLLGISESHQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEP--LSIFCDLMGVDFEELCHWLCHRKLATATETYI 388
Cdd:cd14892 246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGvnVAKAAGLLGVDAAELMFKLVTQTTSTARGSVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 389 K-PISKLQATNARDALAKHIYAKLFNWIVDHVNqALHSAV-----------KQHSFIGVLDIYGFETFEINSFEQFCINY 456
Cdd:cd14892 326 EiKLTAREAKNALDALCKYLYGELFDWLISRIN-ACHKQQtsgvtggaaspTFSPFIGILDIFGFEIMPTNSFEQLCINF 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 457 ANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMP-KGTDDTWAQKLYNTHLNK 534
Cdd:cd14892 405 TNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKpLGLLPLLEEQMLLKrKTTDKQLLTIYHQTHLDK 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 535 CALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKfkmlpelfqddekaisptsatssgrtpltr 614
Cdd:cd14892 485 HPHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS------------------------------ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 615 tlskptkgrpgqtakehkktvghQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISA 694
Cdd:cd14892 535 -----------------------KFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRR 591
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1542868643 695 AGFPSRWTYQEFFSRYRVLMKQK----------DVLSDRKQTCKNVLEKLivDKDKYQFGKTKIFFR 751
Cdd:cd14892 592 EGFPIRRQFEEFYEKFWPLARNKagvaaspdacDATTARKKCEEIVARAL--ERENFQLGRTKVFLR 656
|
|
| 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: 566.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFIDSkLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd01379 1 DTIVSQLQKRYSRD-QIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 163 GESGAGKTVSAKYAMRYFaTVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTY 242
Cdd:cd01379 80 GESGAGKTESANLLVQQL-TVLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 243 LLEKSRVVFQAEEERNYHIFYQLCASadLSEFKVL---RLGDANNFHYTNQGGspviEGVDDAKEMAHTR------QAC- 312
Cdd:cd01379 159 LLEKSRVVHQAIGERNFHIFYYIYAG--LAEDKKLakyKLPENKPPRYLQNDG----LTVQDIVNNSGNRekfeeiEQCf 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 313 TLLGISESHQMGIFRILAGILHLGNVVFMSRDS-----DSCTIpPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETY 387
Cdd:cd01379 233 KVIGFTKEEVDSVYSILAAILHIGDIEFTEVESnhqtdKSSRI-SNPEALNNVAKLLGIEADELQEALTSHSVVTRGETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 388 IKPISKLQATNARDALAKHIYAKLFNWIVDHVNQAL----HSAVKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQ 463
Cdd:cd01379 312 IRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpdrSASDEPLS-IGILDIFGFENFQKNSFEQLCINIANEQIQY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 464 QFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNthlN-KCALFEKP 541
Cdd:cd01379 391 YFNQHIFAWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKpMGLLALLDEESRFPKATDQTLVEKFHN---NiKSKYYWRP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 542 RLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLpelfqddekaisptsatssgrtpltrtlskptk 621
Cdd:cd01379 468 KSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV--------------------------------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 622 grpgqtakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRW 701
Cdd:cd01379 515 ----------RQTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRI 584
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1542868643 702 TYQEFFSRYRVL---MKQKDVLSdrKQTCKNVLEKLIVdkDKYQFGKTKIFFR 751
Cdd:cd01379 585 LFADFLKRYYFLafkWNEEVVAN--RENCRLILERLKL--DNWALGKTKVFLK 633
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
83-751 |
1.21e-180 |
|
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: 561.13 E-value: 1.21e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14929 1 ASVLHTLRRRY-DHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 163 GESGAGKTVSAKYAMRYFATVSGSASE----ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGAN 238
Cdd:cd14929 80 GESGAGKTVNTKHIIQYFATIAAMIESkkklGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 239 MRTYLLEKSRVVFQAEEERNYHIFYQLCASAdlSEFKVLRLGDAN--NFHYTNQGGSPViEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14929 160 IDIYLLEKSRVIFQQPGERNYHIFYQILSGK--KELRDLLLVSANpsDFHFCSCGAVAV-ESLDDAEELLATEQAMDILG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 317 ISESHQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQA 396
Cdd:cd14929 237 FLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 397 TNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:cd14929 317 TYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 477 YMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKAFIIQ---- 551
Cdd:cd14929 397 YRKEGIDWVSIDFgLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHfelv 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 552 HFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaISPTSATSSGRtpltrtlskptkgrpgqtaKEH 631
Cdd:cd14929 477 HYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENY---ISTDSAIQFGE-------------------KKR 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 632 KKTVGHQFRNSLH-----LLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEF 706
Cdd:cd14929 535 KKGASFQTVASLHkenlnKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADF 614
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1542868643 707 FSRY-----RVLMKQKDVlSDRKQTcKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14929 615 KQRYcilnpRTFPKSKFV-SSRKAA-EELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
83-751 |
3.55e-177 |
|
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: 551.96 E-value: 3.55e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14913 1 PAVLYNLKDRY-TSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 163 GESGAGKTVSAKYAMRYFATVSG---------SASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14913 80 GESGAGKTVNTKRVIQYFATIAAtgdlakkkdSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASA--DLSEFkVLRLGDANNFHYTNQGgSPVIEGVDDAKEMAHTRQA 311
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKkpELIEL-LLITTNPYDYPFISQG-EILVASIDDAEELLATDSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 312 CTLLGISESHQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPI 391
Cdd:cd14913 238 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 392 SKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFK 471
Cdd:cd14913 318 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 472 LEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR-LSNKA-- 547
Cdd:cd14913 398 LEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKvVKGRAea 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 548 -FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaisPTSATSSGrtPLTRTLSKPTKGRPGQ 626
Cdd:cd14913 478 hFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY--------ATFATADA--DSGKKKVAKKKGSSFQ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 627 takehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEF 706
Cdd:cd14913 548 -------TVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDF 620
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1542868643 707 FSRYRVLMKQ---KDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14913 621 KQRYRVLNASaipEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
83-751 |
4.73e-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: 548.39 E-value: 4.73e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14904 1 PSILFNLKKRFAASK-PYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 162 SGESGAGKTVSAKYAMRYFATVSGSASEANVEeKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:cd14904 80 SGESGAGKTETTKIVMNHLASVAGGRKDKTIA-KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 242 YLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQG-GSPVIEGVDDAKEMAHTRQACTLLGISES 320
Cdd:cd14904 159 YLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSlAQMQIPGLDDAKLFASTQKSLSLIGLDND 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 321 HQMGIFRILAGILHLGNVVFMSRDSDSCTIPpKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQATNAR 400
Cdd:cd14904 239 AQRTLFKILSGVLHLGEVMFDKSDENGSRIS-NGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEENR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 401 DALAKHIYAKLFNWIVDHVNQAL---HSAVKQHsfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEY 477
Cdd:cd14904 318 DALAKAIYSKLFDWMVVKINAAIstdDDRIKGQ--IGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 478 MKEQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHL----NKCALFekPRLSNKAFIIQHF 553
Cdd:cd14904 396 IREGLQWDHIEYQDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQtkkdNESIDF--PKVKRTQFIINHY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 554 ADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkAISPTSATSSGRtpltrtlskptkgrpgqtAKEHKK 633
Cdd:cd14904 474 AGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE-APSETKEGKSGK------------------GTKAPK 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 634 TVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVL 713
Cdd:cd14904 535 SLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIM 614
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1542868643 714 MKQKDVLSDRKQTCKNVLEKlIVDKD--KYQFGKTKIFFR 751
Cdd:cd14904 615 FPPSMHSKDVRRTCSVFMTA-IGRKSplEYQIGKSLIYFK 653
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
84-751 |
1.43e-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: 548.02 E-value: 1.43e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14927 2 SVLHNLRRRY-SRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 164 ESGAGKTVSAKYAMRYFATVS-------------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDK 230
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAalgdgpgkkaqflATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 231 RYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLcASADLSEFKVLRLGDAN--NFHYTNQGGSPViEGVDDAKEMAHT 308
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQI-LSGKKPELQDMLLVSMNpyDYHFCSQGVTTV-DNMDDGEELMAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 309 RQACTLLGISESHQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYI 388
Cdd:cd14927 239 DHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 389 KPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMH 468
Cdd:cd14927 319 KGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 469 VFKLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKA 547
Cdd:cd14927 399 MFILEQEEYKREGIEWVFIDFgLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 548 -----FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddEKAISPTSATSsgrtPLTRTLSKPTKG 622
Cdd:cd14927 479 kyeahFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY---ENYVGSDSTED----PKSGVKEKRKKA 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 623 RPGQTAKE-HKKtvghqfrnSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRW 701
Cdd:cd14927 552 ASFQTVSQlHKE--------NLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRI 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1542868643 702 TYQEFFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14927 624 LYADFKQRYRILNPSaipDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
84-751 |
1.64e-175 |
|
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: 547.69 E-value: 1.64e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14920 2 SVLHNLKDRYY-SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 164 ESGAGKTVSAKYAMRYFATVSGS-------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIG 236
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASShkgrkdhNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 237 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPvIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIP-IPGQQDKDNFQETMEAMHIMG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 317 ISESHQMGIFRILAGILHLGNVVFM-SRDSDSCTIpPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14920 240 FSHEEILSMLKVVSSVLQFGNISFKkERNTDQASM-PENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 474
Cdd:cd14920 319 ADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 475 EEYMKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKA-FI 549
Cdd:cd14920 399 EEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAdFC 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 550 IQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLTRTLskptkgrpgQTAK 629
Cdd:cd14920 479 IIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAY---------KTKK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 630 EHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSR 709
Cdd:cd14920 550 GMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1542868643 710 YRVLMKQK--DVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 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 |
1.84e-172 |
|
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: 539.23 E-value: 1.84e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 85 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP---------IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDER 155
Cdd:cd14907 3 LLINLKKRYQQDK-IFTYVGPTLIVMNPYKQIDnlfseevmqMYKEQIIQNGEYFDIKKEPPHIYAIAALAFKQLFENNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 156 NQSIIVSGESGAGKTVSAKYAMRYFATVSG------------------SASEANVEEKVLASNPIMESIGNAKTTRNDNS 217
Cdd:cd14907 82 KQAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevltltssiratSKSTKSIEQKILSCNPILEAFGNAKTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 218 SRFGKYIEIGFDKRYR-IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAD---LSEFKVLRLGDANNFHYTNQGGS 293
Cdd:cd14907 162 SRFGKYVSILVDKKKRkILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADqqlLQQLGLKNQLSGDRYDYLKKSNC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 294 PVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVVFMSR--DSDSCTIPPKHEPLSIFCDLMGVDFEEL 371
Cdd:cd14907 242 YEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDStlDDNSPCCVKNKETLQIIAKLLGIDEEEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 372 CHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQAL--HSAVKQHSF------IGVLDIYGFET 443
Cdd:cd14907 322 KEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpKDEKDQQLFqnkylsIGLLDIFGFEV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 444 FEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTL--IDFYDNQPCINLIES-KLGILDLLDEECKMPKGTD 520
Cdd:cd14907 402 FQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSYTDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 521 DTWAQKLYNTHLNKCALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKais 600
Cdd:cd14907 482 EKLLNKIKKQHKNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGEDG--- 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 601 ptsatssgrtpltrtlSKPTKGRPGQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQ 680
Cdd:cd14907 559 ----------------SQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQ 622
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1542868643 681 LRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkqkdvlsdrkqtcKNVLeklivdkdkyqFGKTKIFFR 751
Cdd:cd14907 623 IRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLK-------------KNVL-----------FGKTKIFMK 669
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
83-751 |
1.59e-170 |
|
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: 534.49 E-value: 1.59e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAY------SGQNM---GDMDPHIFAVAEEAYKQMARD 153
Cdd:cd14908 1 PAILHSLSRRF-FRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYrqegllRSQGIespQALGPHVFAIADRSYRQMMSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 154 ER-NQSIIVSGESGAGKTVSAKYAMRYFATV----------SGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGK 222
Cdd:cd14908 80 IRaSQSILISGESGAGKTESTKIVMLYLTTLgngeegapneGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 223 YIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGD--------ANNFHYTNQGGSP 294
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDgitgglqlPNEFHYTGQGGAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 295 VIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVVFMSRDSDSCTIPPK---HEPLSIFCDLMGVDFEEL 371
Cdd:cd14908 240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEegnEKCLARVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 372 CHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ--HSFIGVLDIYGFETFEINSF 449
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKdiRSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 450 EQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIES-KLGILDLLDEECKMP-KGTDDTWAQKL 527
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAkKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 528 YNTHLNKC--ALFEKPRLSNKA-------FIIQHFADKVEYQCE-GFLEKNKDtvfeeqiKVLKSSKfkmlpELFQDdek 597
Cdd:cd14908 480 YETYLPEKnqTHSENTRFEATSiqktkliFAVRHFAGQVQYTVEtTFCEKNKD-------EIPLTAD-----SLFES--- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 598 aisptsatssgrtpltrtlskptkgrpgqtakehkktvGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRA 677
Cdd:cd14908 545 --------------------------------------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRV 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 678 VQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK--QKDVLS------DRKQTCKNVLEKLIVD------------ 737
Cdd:cd14908 587 TEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPliPEVVLSwsmerlDPQKLCVKKMCKDLVKgvlspamvsmkn 666
|
730
....*....|....*.
gi 1542868643 738 --KDKYQFGKTKIFFR 751
Cdd:cd14908 667 ipEDTMQLGKSKVFMR 682
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
83-751 |
1.79e-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: 534.03 E-value: 1.79e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14909 1 ASVLHNLRQRYY-AKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 163 GESGAGKTVSAKYAMRYFATVSGS-------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRII 235
Cdd:cd14909 80 GESGAGKTENTKKVIAYFATVGASkktdeaaKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 236 GANMRTYLLEKSRVVFQAEEERNYHIFYQLCASA--DLSEFKVLRlGDANNFHYTNQGGSpVIEGVDDAKEMAHTRQACT 313
Cdd:cd14909 160 GADIETYLLEKARVISQQSLERSYHIFYQIMSGSvpGVKEMCLLS-DNIYDYYIVSQGKV-TVPNVDDGEEFSLTDQAFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 314 LLGISESHQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISK 393
Cdd:cd14909 238 ILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 394 LQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLE 473
Cdd:cd14909 318 QQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 474 QEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKA----- 547
Cdd:cd14909 398 QEEYKREGIDWAFIDFgMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGqqaah 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 548 FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRtpltrtlskptkGRPGQT 627
Cdd:cd14909 478 FAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGR------------GKKGGG 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 628 AkehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFF 707
Cdd:cd14909 546 F----ATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFK 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1542868643 708 SRYRVLM-KQKDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14909 622 MRYKILNpAGIQGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| Myo5c_CBD |
cd15476 |
Cargo binding domain of myosin 5C; Class V myosins are well studied unconventional myosins, ... |
1480-1847 |
4.40e-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: 516.64 E-value: 4.40e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1480 EDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNT 1559
Cdd:cd15476 1 EDEAKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRHADYLNDANKLKSLMNAIITGVKQVIKEHQEDFEMLSFWLSNT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1560 CRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmivsgmlehetiqgvsgv 1639
Cdd:cd15476 81 YHFLNCLKQYSGEEEFMKHNTPRQNKNCLKNFDLSEHRQILSDLAIRIYHQFISVMENNLQP------------------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1640 kptglrkrtssiadegtyTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAVTLNNLLLRKDMCSWSKGMQIRY 1719
Cdd:cd15476 143 ------------------TISSILQQLSYFYSTMCQHGMDPELIKQAVKQLFFLIGAVTLNSIFLRKDMCSCRKGMQIRC 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1720 NVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFI 1799
Cdd:cd15476 205 NISYLEEWLKEKNLQNSNAKETLEPLSQAAWLLQVNKTTDDDAKEICERCTELSAVQIVKILNSYTPIDDFEKRVTPSFV 284
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1542868643 1800 RTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGL 1847
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 |
1.95e-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: 526.09 E-value: 1.95e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14911 2 SVLHNIKDRYY-SGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 164 ESGAGKTVSAKYAMRYFATVSGSASEAN----------------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIG 227
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASKPKGSgavphpavnpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 228 FDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPViEGVDDAKEMAH 307
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPV-PGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 308 TRQACTLLGISESHQMGIFRILAGILHLGNVVF-MSRDSDSCTIPPKHEPLSIfCDLMGVDFEELCHWLCHRKLATATET 386
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFrQERNNDQATLPDNTVAQKI-AHLLGLSVTDMTRAFLTPRIKVGRDF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 387 YIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQF 465
Cdd:cd14911 319 VTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 466 NMHVFKLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKPRLS 544
Cdd:cd14911 399 NHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFMKTDFR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 545 NKA-FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSAtssgrtpltrtLSKPTKGr 623
Cdd:cd14911 478 GVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQA-----------LTDTQFG- 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 624 pGQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTY 703
Cdd:cd14911 546 -ARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPF 624
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1542868643 704 QEFFSRYRVLMKQ--KDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14911 625 QEFRQRYELLTPNviPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
85-751 |
4.10e-163 |
|
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: 513.69 E-value: 4.10e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 85 VLHNLRVRFIDSkLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQM----ARDERNQSII 160
Cdd:cd14889 3 LLEVLKVRFMQS-NIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMlgrlARGPKNQCIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 161 VSGESGAGKTVSAKYAMRYFATVSGSASEanVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMR 240
Cdd:cd14889 82 ISGESGAGKTESTKLLLRQIMELCRGNSQ--LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 241 TYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISES 320
Cdd:cd14889 159 EYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYDEVCNAMDMVGFTEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 321 HQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHE-PLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQATNA 399
Cdd:cd14889 239 EEVDMFTILAGILSLGNITFEMDDDEALKVENDSNgWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAEDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 400 RDALAKHIYAKLFNWIVDHVNQALHSAVK---QHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:cd14889 319 RDSIAKVAYGRVFGWIVSKINQLLAPKDDssvELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLMEQKE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 477 YMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLyNTHLNKCALFEKPRLSNKAFIIQHFAD 555
Cdd:cd14889 399 YKKEGIDWKEITYKDNKPILDLFLNKpIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYGKSRSKSPKFTVNHYAG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaisptSATSSGRTPLTRTLSKPTKGRPGQTAKEhKKTV 635
Cdd:cd14889 478 KVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLF----------TATRSRTGTLMPRAKLPQAGSDNFNSTR-KQSV 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK 715
Cdd:cd14889 547 GAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILLC 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 1542868643 716 QKDvLSDRKQTCKNVLEKliVDKDKYQFGKTKIFFR 751
Cdd:cd14889 627 EPA-LPGTKQSCLRILKA--TKLVGWKCGKTRLFFK 659
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
83-751 |
4.67e-163 |
|
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: 513.88 E-value: 4.67e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14917 1 PAVLYNLKERY-ASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 163 GESGAGKTVSAKYAMRYFATVSG---------SASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14917 80 GESGAGKTVNTKRVIQYFAVIAAigdrskkdqTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRL-GDANNFHYTNQGGSPViEGVDDAKEMAHTRQAC 312
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGETTV-ASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 313 TLLGISESHQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPIS 392
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 393 KLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKL 472
Cdd:cd14917 319 VQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 473 EQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR-LSNKA--- 547
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRnIKGKPeah 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 548 FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekaisptsaTSSGRTPLTRTLSKPTKGRPGQt 627
Cdd:cd14917 479 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN----------YAGADAPIEKGKGKAKKGSSFQ- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 628 akehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFF 707
Cdd:cd14917 548 ------TVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFR 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1542868643 708 SRYRVLMKQ---KDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14917 622 QRYRILNPAaipEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
84-751 |
1.95e-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: 509.18 E-value: 1.95e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 84 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14934 2 SVLDNLRQRYTNMR-IYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 164 ESGAGKTVSAKYAMRYFATVSGSASEA-----NVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGAN 238
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSsdgkgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 239 MRTYLLEKSRVVFQAEEERNYHIFYQLCAS--ADLSEfKVLRLGDANNFHYTNQGGSpVIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14934 161 IESYLLEKSRVISQQAAERGYHIFYQILSNkkPELIE-SLLLVPNPKEYHWVSQGVT-VVDNMDDGEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 317 ISESHQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQA 396
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 397 TNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:cd14934 319 NNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 477 YMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKP-----RLSNKAFII 550
Cdd:cd14934 399 YKREGIEWVFIDFgLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPkggkgKGPEAHFEL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 551 QHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFkMLPELFQDDEKAISPTSATSSGRTPLtrtlskptkgrpgqtake 630
Cdd:cd14934 479 VHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSL-GLLALLFKEEEAPAGSKKQKRGSSFM------------------ 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 631 hkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRY 710
Cdd:cd14934 540 ---TVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRY 616
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1542868643 711 RVLmkQKDVLS----DRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14934 617 QVL--NPNVIPqgfvDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
85-751 |
6.18e-161 |
|
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: 506.92 E-value: 6.18e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 85 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDM-DPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14897 3 IVQTLKSRYNKDK-FYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVRSQrPPHLFWIADQAYRRLLETGRNQCILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 164 ESGAGKTVSAKYAMRYFATVSGSASEaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYL 243
Cdd:cd14897 82 ESGAGKTESTKYMIKHLMKLSPSDDS-DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 244 LEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNfHYTNQGGSPVIEGVDDAKEMAHTRQACT-------LLG 316
Cdd:cd14897 161 LEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDC-HRILRDDNRNRPVFNDSEELEYYRQMFHdltnimkLIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 317 ISESHQMGIFRILAGILHLGNVVFMS-RDSDSCTIPPKHePLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14897 240 FSEEDISVIFTILAAILHLTNIVFIPdEDTDGVTVADEY-PLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQH-----SFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14897 319 ANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQimtrgPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 471 KLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLyNTHLNKCALFEKPRLSNKAFI 549
Cdd:cd14897 399 PRERSEYEIEGIEWRDIEYHDNDDVLELFFKKpLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESPRYVASPGNRVAFG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 550 IQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaispTSatssgrtpltrtlskptkgrpgqtak 629
Cdd:cd14897 478 IRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF---------TS-------------------------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 630 ehkktvghQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSR 709
Cdd:cd14897 523 --------YFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKR 594
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1542868643 710 YRVLM-KQKDVLSDRKQTCKNVLEKLivDKDKYQFGKTKIFFR 751
Cdd:cd14897 595 YKEICdFSNKVRSDDLGKCQKILKTA--GIKGYQFGKTKVFLK 635
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
83-751 |
7.02e-161 |
|
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: 508.06 E-value: 7.02e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14916 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 163 GESGAGKTVSAKYAMRYFATVSG----------SASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd14916 80 GESGAGKTVNTKRVIQYFASIAAigdrskkenpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRL-GDANNFHYTNQGgSPVIEGVDDAKEMAHTRQA 311
Cdd:cd14916 160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVSQG-EVSVASIDDSEELLATDSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 312 CTLLGISESHQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPI 391
Cdd:cd14916 239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 392 SKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFK 471
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 472 LEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR----LSNK 546
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRnvkgKQEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 547 AFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAisptSATSSGrtpltrtlskptKGRPGQ 626
Cdd:cd14916 479 HFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASA----DTGDSG------------KGKGGK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 627 TAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEF 706
Cdd:cd14916 543 KKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1542868643 707 FSRYRVL----MKQKDVLSDRKQTCKnVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14916 623 RQRYRILnpaaIPEGQFIDSRKGAEK-LLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
83-751 |
2.47e-160 |
|
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: 505.73 E-value: 2.47e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRF-IDSKLIYTYCGIVLVAINPYEQLPiygEDIINAYSGQNMGDMDPHIFAVAEEAYKQM---ARDERNQS 158
Cdd:cd14891 1 AGILHNLEERSkLDNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMclgSGRMQNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 159 IIVSGESGAGKTVSAKYAMRYFATVS-----------------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFG 221
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAvggkkasgqdieqsskkRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 222 KYIEIGFDKR-YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPVIEGVD 300
Cdd:cd14891 158 KFMKLQFTKDkFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 301 DAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVVFMSRDSDSCTI----PPKHEPLSIFCDLMGVDFEELCHWLC 376
Cdd:cd14891 238 DAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAeiasESDKEALATAAELLGVDEEALEKVIT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 377 HRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEI-NSFEQFCIN 455
Cdd:cd14891 318 QREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFETkNDFEQLLIN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 456 YANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTHL-N 533
Cdd:cd14891 398 YANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPnGILPLLDNEARNPNPSDAKLNETLHKTHKrH 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 534 KCALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKfkmlpelfqddekaisptsatssgrtplt 613
Cdd:cd14891 478 PCFPRPHPKDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASSA----------------------------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 614 rtlskptkgrpgqtakehkktvghQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRIS 693
Cdd:cd14891 529 ------------------------KFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVL 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1542868643 694 AAGFPSRWTYQEFFSRYRVLM----KQKDVLSDRKQTcKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14891 585 KVGLPTRVTYAELVDVYKPVLppsvTRLFAENDRTLT-QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
84-751 |
3.18e-159 |
|
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: 503.79 E-value: 3.18e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14932 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 164 ESGAGKTVSAKYAMRYFATVSGSA-----------SEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQgGSPVIEGVDDAKEMAHTRQAC 312
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSN-GNVTIPGQQDKELFAETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 313 TLLGISESHQMGIFRILAGILHLGNVVF-MSRDSDSCTIPPKHEPLSIfCDLMGVDFEELCHWLCHRKLATATETYIKPI 391
Cdd:cd14932 240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFkKERNSDQASMPDDTAAQKV-CHLLGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 392 SKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14932 319 TQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKP-RLSN 545
Cdd:cd14932 399 ILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQGNN-PKFQKPkKLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 546 KA-FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSsgrtpLTRTLSKPTKGRP 624
Cdd:cd14932 478 DAdFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAG-----MGESLHGAFKTRK 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 625 GQTakehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQ 704
Cdd:cd14932 553 GMF-----RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1542868643 705 EFFSRYRVLMKQK--DVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14932 628 EFRQRYEILTPNAipKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
83-751 |
1.41e-158 |
|
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: 501.95 E-value: 1.41e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14912 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 163 GESGAGKTVSAKYAMRYFATVSGSAS-----------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR 231
Cdd:cd14912 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 232 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLG-DANNFHYTNQGGSPViEGVDDAKEMAHTRQ 310
Cdd:cd14912 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITtNPYDYPFVSQGEISV-ASIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 311 ACTLLGISESHQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKP 390
Cdd:cd14912 239 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 391 ISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14912 319 QTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRL----SN 545
Cdd:cd14912 399 VLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVvkgkAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 546 KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSgrtpltrtlskpTKGrpG 625
Cdd:cd14912 479 AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGA------------KKG--G 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 626 QTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14912 545 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1542868643 706 FFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14912 625 FKQRYKVLNASaipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
83-751 |
5.80e-158 |
|
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: 500.37 E-value: 5.80e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14923 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 163 GESGAGKTVSAKYAMRYFATVS----------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd14923 80 GESGAGKTVNTKRVIQYFATIAvtgdkkkeqqPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLG-DANNFHYTNQGgSPVIEGVDDAKEMAHTRQA 311
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIStNPFDFPFVSQG-EVTVASIDDSEELLATDNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 312 CTLLGISESHQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPI 391
Cdd:cd14923 239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 392 SKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFK 471
Cdd:cd14923 319 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 472 LEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR-LSNKA-- 547
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKpAKGKAea 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 548 -FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaiSPTSATSSGRTPLTRtlskptkgRPGQ 626
Cdd:cd14923 479 hFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLF-------SNYAGAEAGDSGGSK--------KGGK 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 627 TAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEF 706
Cdd:cd14923 544 KKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADF 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1542868643 707 FSRYRVLMKQ---KDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14923 624 KQRYRILNASaipEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
83-751 |
1.06e-157 |
|
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: 499.26 E-value: 1.06e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14918 1 PGVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 163 GESGAGKTVSAKYAMRYFATVSGSAS---------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14918 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASA--DLSEFkVLRLGDANNFHYTNQGgSPVIEGVDDAKEMAHTRQA 311
Cdd:cd14918 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKkpDLIEM-LLITTNPYDYAFVSQG-EITVPSIDDQEELMATDSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 312 CTLLGISESHQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPI 391
Cdd:cd14918 238 IDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 392 SKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFK 471
Cdd:cd14918 318 TVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 472 LEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRL----SNK 546
Cdd:cd14918 398 LEQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVvkgkAEA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 547 AFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRtpltrtlskpTKGRPGQ 626
Cdd:cd14918 478 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAK----------KKGSSFQ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 627 takehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEF 706
Cdd:cd14918 548 -------TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDF 620
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1542868643 707 FSRYRVLMKQ---KDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14918 621 KQRYKVLNASaipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
84-751 |
1.81e-157 |
|
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: 499.16 E-value: 1.81e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14921 2 SVLHNLRERYF-SGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 164 ESGAGKTVSAKYAMRYFATVSGS-------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIG 236
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASShkgkkdtSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 237 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPvIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVP-IPAAQDDEMFQETLEAMSIMG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 317 ISESHQMGIFRILAGILHLGNVVF-MSRDSDSCTIPPKHEPLSIfCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14921 240 FSEEEQLSILKVVSSVLQLGNIVFkKERNTDQASMPDNTAAQKV-CHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 474
Cdd:cd14921 319 ADFAIEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 475 EEYMKEQIPWTLIDF-YDNQPCINLIE---SKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPR-LSNKA-F 548
Cdd:cd14921 399 EEYQREGIEWNFIDFgLDLQPCIELIErpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNH-PKFQKPKqLKDKTeF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 549 IIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLTrTLSKPTKGRpgqta 628
Cdd:cd14921 478 SIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLP-SASKTKKGM----- 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 629 kehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 708
Cdd:cd14921 552 ---FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1542868643 709 RYRVLMKQK--DVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14921 629 RYEILAANAipKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
83-751 |
2.09e-156 |
|
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: 496.18 E-value: 2.09e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14910 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 163 GESGAGKTVSAKYAMRYFATVSGSAS-----------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR 231
Cdd:cd14910 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 232 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASA--DLSEFkVLRLGDANNFHYTNQGgSPVIEGVDDAKEMAHTR 309
Cdd:cd14910 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKkpDLIEM-LLITTNPYDYAFVSQG-EITVPSIDDQEELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 310 QACTLLGISESHQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIK 389
Cdd:cd14910 238 SAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 390 PISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHV 469
Cdd:cd14910 318 GQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 470 FKLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKA- 547
Cdd:cd14910 398 FVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKv 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 548 ---FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaisptsatsSGRTPLTRTLSKPTKGrp 624
Cdd:cd14910 478 eahFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLF--------------SGAAAAEAEEGGGKKG-- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 625 GQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQ 704
Cdd:cd14910 542 GKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYA 621
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1542868643 705 EFFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14910 622 DFKQRYKVLNASaipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
83-751 |
2.46e-155 |
|
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: 493.09 E-value: 2.46e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14915 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 163 GESGAGKTVSAKYAMRYFATVSGSAS-----------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR 231
Cdd:cd14915 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeaasgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 232 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLG-DANNFHYTNQGgSPVIEGVDDAKEMAHTRQ 310
Cdd:cd14915 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITtNPYDFAFVSQG-EITVPSIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 311 ACTLLGISESHQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKP 390
Cdd:cd14915 239 AVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 391 ISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14915 319 QTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSN-KA- 547
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKgKAe 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 548 --FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGrtpltrtlskptkgrpG 625
Cdd:cd14915 479 ahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGGGKKG----------------G 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 626 QTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14915 543 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1542868643 706 FFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14915 623 FKQRYKVLNASaipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
85-749 |
3.57e-155 |
|
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: 492.06 E-value: 3.57e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 85 VLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAY-SGQNMGDMDPHIFAVAEEAYK--QMARDERNQSII 160
Cdd:cd14880 3 VLRCLQARYT-ADTFYTNAGCTLVALNPFKPVPqLYSPELMREYhAAPQPQKLKPHIFTVGEQTYRnvKSLIEPVNQSIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 161 VSGESGAGKTVSAKYAMRYFATVSGSAS--EAN-----VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14880 82 VSGESGAGKTWTSRCLMKFYAVVAASPTswESHkiaerIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTnqggsPVIEGVDDAKEMAHTRQACT 313
Cdd:cd14880 162 MTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWL-----PNPERNLEEDCFEVTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 314 LLGISESHQMGIFRILAGILHLGNVVFMSRDSDSCTIPPK---HEPLSIFCDLMGVDFEELCHWLCHRKLATATE--TYI 388
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMddtKESVRTSALLLKLPEDHLLETLQIRTIRAGKQqqVFK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 389 KPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNM 467
Cdd:cd14880 317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 468 HVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIE-SKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNK 546
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKLSRE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 547 -AFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLTRTLSKptkgrpg 625
Cdd:cd14880 477 pSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQSRAPVLTVVSK------- 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 626 qtakehkktvghqFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14880 550 -------------FKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQN 616
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1542868643 706 FFSRYRVLMKqkdvLSDRKQTCKNVLEKLIVDKDKYQFGKTKIF 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 |
4.16e-154 |
|
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: 489.60 E-value: 4.16e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14919 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 164 ESGAGKTVSAKYAMRYFATVSGS----ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANM 239
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASShkskKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 240 RTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQgGSPVIEGVDDAKEMAHTRQACTLLGISE 319
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSN-GHVTIPGQQDKDMFQETMEAMRIMGIPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 320 SHQMGIFRILAGILHLGNVVF-MSRDSDSCTIPPKHEPLSIfCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQATN 398
Cdd:cd14919 240 EEQMGLLRVISGVLQLGNIVFkKERNTDQASMPDNTAAQKV-SHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 399 ARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEY 477
Cdd:cd14919 319 AIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 478 MKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYN---THLNkcalFEKPR-LSNKA-F 548
Cdd:cd14919 399 QREGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQeqgTHPK----FQKPKqLKDKAdF 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 549 IIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLtrtlskptkgrPG--Q 626
Cdd:cd14919 475 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETAL-----------PGafK 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 627 TAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEF 706
Cdd:cd14919 544 TRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEF 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1542868643 707 FSRYRVLMKQK--DVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14919 624 RQRYEILTPNSipKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
83-751 |
1.95e-153 |
|
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: 489.08 E-value: 1.95e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGediINAYSGQNMGDMD--PHIFAVAEEAYKQMAR------- 152
Cdd:cd14895 1 PAFVDYLAQRYGVDQ-VYCRSGAVLIAVNPFKHIPgLYD---LHKYREEMPGWTAlpPHVFSIAEGAYRSLRRrlhepga 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 153 DERNQSIIVSGESGAGKTVSAKYAMRYFA--------TVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYI 224
Cdd:cd14895 77 SKKNQTILVSGESGAGKTETTKFIMNYLAesskhttaTSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 225 EIGF-----DKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGD--ANNFHYTNQGGSPVI- 296
Cdd:cd14895 157 RMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELlsAQEFQYISGGQCYQRn 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 297 EGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVVFMS-------RDSDSCTIPPK-----------HEPLS 358
Cdd:cd14895 237 DGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVAssedegeEDNGAASAPCRlasaspssltvQQHLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 359 IFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQAlhSAVKQHS------- 431
Cdd:cd14895 317 IVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSA--SPQRQFAlnpnkaa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 432 ------FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LG 504
Cdd:cd14895 395 nkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRpSG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 505 ILDLLDEECKMPKGTDDTWAQKLYNThLNKCALFEKPRL--SNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKS 582
Cdd:cd14895 475 IFSLLDEECVVPKGSDAGFARKLYQR-LQEHSNFSASRTdqADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGK 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 583 SKFKMLPELFqdDEKAISPTSATSSGRTPLTRTLSKPTkgrpgqtakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIK 662
Cdd:cd14895 554 TSDAHLRELF--EFFKASESAELSLGQPKLRRRSSVLS-----------SVGIGSQFKQQLASLLDVVQQTQTHYIRCIK 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 663 PNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLSdrkQTCKNVLEKLIVdkDKYQ 742
Cdd:cd14895 621 PNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASD---ATASALIETLKV--DHAE 695
|
....*....
gi 1542868643 743 FGKTKIFFR 751
Cdd:cd14895 696 LGKTRVFLR 704
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
83-751 |
1.36e-152 |
|
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: 487.09 E-value: 1.36e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAY--------SGQNMGDMDPHIFAVAEEAYKQMARD 153
Cdd:cd14902 1 AALLQALSERF-EHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFGGLLKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 154 ER-NQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEANVE--------EKVLASNPIMESIGNAKTTRNDNSSRFGKYI 224
Cdd:cd14902 80 ERrNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEgsdaveigKRILQTNPILESFGNAQTIRNDNSSRFGKFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 225 EIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGS----PVIEGVD 300
Cdd:cd14902 160 KIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGPsfarKRAVADK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 301 DAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVVFM---SRDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCH 377
Cdd:cd14902 240 YAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTaenGQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 378 RKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIV-------DHVNQALHSAVKQHSF--IGVLDIYGFETFEINS 448
Cdd:cd14902 320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVrrlsdeiNYFDSAVSISDEDEELatIGILDIFGFESLNRNG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 449 FEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKL 527
Cdd:cd14902 400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSnGLFSLLDQECLMPKGSNQALSTKF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 528 YNTHLNKcalfekprlsnKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQdDEKAISPTSATSS 607
Cdd:cd14902 480 YRYHGGL-----------GQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGA-DENRDSPGADNGA 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 608 GRTPLTRTLSKPtkgrpgqtakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVL 687
Cdd:cd14902 548 AGRRRYSMLRAP--------------SVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVL 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 688 ETIRISAAGFPSRWTYQEF---FSRYRVLMKQKD----------------------VLSDRKQTCKNVLEKLIVDKDKY- 741
Cdd:cd14902 614 EAVRIARHGYSVRLAHASFielFSGFKCFLSTRDraakmnnhdlaqalvtvlmdrvLLEDGVEREEKNPGALTAVTGDGs 693
|
730 740
....*....|....*....|...
gi 1542868643 742 -------------QFGKTKIFFR 751
Cdd:cd14902 694 gtafendcrrkdvQVGRTLVFCK 716
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
84-751 |
2.94e-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: 476.48 E-value: 2.94e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd15896 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 164 ESGAGKTVSAKYAMRYFATVSGS-----------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQgGSPVIEGVDDAKEMAHTRQAC 312
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSN-GNVTIPGQQDKDLFTETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 313 TLLGISESHQMGIFRILAGILHLGNVVF-MSRDSDSCTIPPKHEPLSIfCDLMGVDFEELCHWLCHRKLATATETYIKPI 391
Cdd:cd15896 240 RIMGIPEDEQIGMLKVVASVLQLGNMSFkKERHTDQASMPDNTAAQKV-CHLMGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 392 SKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd15896 319 TQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIE---SKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNK 546
Cdd:cd15896 399 ILEQEEYQREGIEWSFIDFgLDLQPCIDLIEkpaSPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 547 A-FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPltrtlskptkgRPG 625
Cdd:cd15896 479 AdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSEMP-----------GAF 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 626 QTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd15896 548 KTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1542868643 706 FFSRYRVLMKQK--DVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 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 |
7.00e-149 |
|
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: 475.35 E-value: 7.00e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14930 2 SVLHNLRERYY-SGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 164 ESGAGKTVSAKYAMRYFATVSGSAS-------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIG 236
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKgrkepgvPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 237 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGgsPVIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG--PSSSPGQERELFQETLESLRVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 317 ISESHQMGIFRILAGILHLGNVVF-MSRDSDSCTIpPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14930 239 FSHEEITSMLRMVSAVLQFGNIVLkRERNTDQATM-PDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 474
Cdd:cd14930 318 ADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 475 EEYMKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKPR-LSNKA-F 548
Cdd:cd14930 398 EEYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRhLRDQAdF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 549 IIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGrtpltrtlSKPTKGRPgqtA 628
Cdd:cd14930 477 SVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLG--------DGPPGGRP---R 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 629 KEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 708
Cdd:cd14930 546 RGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1542868643 709 RYRVLMKQK--DVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14930 626 RYEILTPNAipKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
85-725 |
1.91e-148 |
|
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: 472.48 E-value: 1.91e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 85 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAY---------SGQNMGD--MDPHIFAVAEEAYKQMAR 152
Cdd:cd14900 3 ILSALETRFYAQK-IYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssSTRNKGSdpMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 153 ----DERNQSIIVSGESGAGKTVSAKYAMRYFA---------TVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSR 219
Cdd:cd14900 82 glngVMSDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaaSVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 220 FGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAsadlsefkvlrlgdannfhytnqGGSPVIEGV 299
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAI-----------------------GASEAARKR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 300 DDAKEMAhtrQACTLLGISESHQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHE--PLSIF-----CDLMGVDFEELC 372
Cdd:cd14900 219 DMYRRVM---DAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDlaPSSIWsrdaaATLLSVDATKLE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 373 HWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALH--SAVKQHS---FIGVLDIYGFETFEIN 447
Cdd:cd14900 296 KALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKmdDSSKSHGglhFIGILDIFGFEVFPKN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 448 SFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQK 526
Cdd:cd14900 376 SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRpTGILSLIDEECVMPKGSDTTLASK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 527 LYnTHLNKCALFEKPRLSNKA--FIIQHFADKVEYQCEGFLEKNKDTVFEEQIkvlksskfkmlpELFQDdekaisptsa 604
Cdd:cd14900 456 LY-RACGSHPRFSASRIQRARglFTIVHYAGHVEYSTDGFLEKNKDVLHQEAV------------DLFVY---------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 605 tssgrtpltrtlskptkgrpgqtakehkktvGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRAC 684
Cdd:cd14900 513 -------------------------------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCN 561
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1542868643 685 GVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLSDRKQ 725
Cdd:cd14900 562 GVMEAVRVARAGFPIRLLHDEFVARYFSLARAKNRLLAKKQ 602
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
34-803 |
8.95e-143 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 463.73 E-value: 8.95e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 34 GDKVLLLQLEDGKDLEYRLDPKtkelpHLRNPDILVGEN---DLTALSYLHEPAVLHNLRVRFIdSKLIYTYCGIVLVAI 110
Cdd:PTZ00014 63 GEKLTLKQIDPPTNSTFEVKPE-----HAFNANSQIDPMtygDIGLLPHTNIPCVLDFLKHRYL-KNQIYTTADPLLVAI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 111 NPYEQLPIYGEDIINAY-SGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASE 189
Cdd:PTZ00014 137 NPFKDLGNTTNDWIRRYrDAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMD 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 190 ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASA 269
Cdd:PTZ00014 217 LKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 270 DLSEFKVLRLGDANNFHYTNQGgSPVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVVFMSRDSD--- 346
Cdd:PTZ00014 297 NDEMKEKYKLKSLEEYKYINPK-CLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGglt 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 347 --SCTIPPKHEPLSIFCDLMGVDFEELCHWLchrklaTATETYI------KPISKLQATNARDALAKHIYAKLFNWIVDH 418
Cdd:PTZ00014 376 daAAISDESLEVFNEACELLFLDYESLKKEL------TVKVTYAgnqkieGPWSKDESEMLKDSLSKAVYEKLFLWIIRN 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 419 VNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINL 498
Cdd:PTZ00014 450 LNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDL 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 499 IESKL-GILDLLDEECKMPKGTDD----TWAQKLYNthlNKCALFEKpRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVF 573
Cdd:PTZ00014 530 LCGKGkSVLSILEDQCLAPGGTDEkfvsSCNTNLKN---NPKYKPAK-VDSNKNFVIKHTIGDIQYCASGFLFKNKDVLR 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 574 EEQIKVLKSSKFKMLPELFQDDEkaisptsatssgrtpLTRtlskptkgrpGQTAKehKKTVGHQFRNSLHLLMETLNAT 653
Cdd:PTZ00014 606 PELVEVVKASPNPLVRDLFEGVE---------------VEK----------GKLAK--GQLIGSQFLNQLDSLMSLINST 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 654 TPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRV--LMKQKDVLSDRKQTCKNVL 731
Cdd:PTZ00014 659 EPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYldLAVSNDSSLDPKEKAEKLL 738
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1542868643 732 EKLIVDKDKYQFGKTKIFFRAGQVAYLEKLRADKLRA--ACIRIqktIRGWLLRKKYLR-MRKAAITVQR---YVRGH 803
Cdd:PTZ00014 739 ERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAAwePLVSV---LEALILKIKKKRkVRKNIKSLVRiqaHLRRH 813
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
83-751 |
1.94e-142 |
|
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: 456.55 E-value: 1.94e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14896 1 SSVLLCLKKRF-HLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 163 GESGAGKTVSAKYAMRYFATVSGSASEANVE--EKVLasnPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMR 240
Cdd:cd14896 80 GHSGSGKTEAAKKIVQFLSSLYQDQTEDRLRqpEDVL---PILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 241 TYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISES 320
Cdd:cd14896 156 HYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 321 HQMGIFRILAGILHLGNVVFMSRDSDSctippkHEPLSIFCD--------LMGVDFEELCHWLCHRKLATATETYIKPIS 392
Cdd:cd14896 236 ELTAIWAVLAAILQLGNICFSSSERES------QEVAAVSSWaeihtaarLLQVPPERLEGAVTHRVTETPYGRVSRPLP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 393 KLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSF--IGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14896 310 VEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 471 KLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPRLSNKAFI 549
Cdd:cd14896 390 AQEEEECQRELLPWVPIPQPPRESCLDLLVDQPhSLLSILDDQTWLSQATDHTFLQKCHYHHGDH-PSYAKPQLPLPVFT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 550 IQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQddekaisptsatssgrtpltrtlskptKGRPGQTAK 629
Cdd:cd14896 469 VRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQ---------------------------EAEPQYGLG 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 630 EHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSR 709
Cdd:cd14896 522 QGKPTLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLAR 601
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1542868643 710 YRVLMKQK-DVLSDRKQtCKNVLEKLI-VDKDKYQFGKTKIFFR 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 |
7.43e-138 |
|
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: 446.73 E-value: 7.43e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 85 VLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQN-MGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14906 3 ILNNLGKRYK-SDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINqNKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 163 GESGAGKTVSAKYAMRYFATVSGSASEAN---------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR-Y 232
Cdd:cd14906 82 GESGSGKTEASKTILQYLINTSSSNQQQNnnnnnnnnsIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 233 RIIGANMRTYLLEKSRVVFQAEEER-NYHIFYQLCASADLSEFKVLRL-GDANNFHYTN-------------QGGSPVIE 297
Cdd:cd14906 162 KIDGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLnNDPSKYRYLDarddvissfksqsSNKNSNHN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 298 GVDDAKE-MAHTRQACTLLGISESHQMGIFRILAGILHLGNVVFmSRDSDSCTI----PPKHEPLSIFCDLMGVDFEELC 372
Cdd:cd14906 242 NKTESIEsFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEF-EEDSDFSKYayqkDKVTASLESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 373 HWLCHRKLATATE--TYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQ-----------ALHSAVKQHSFIGVLDIY 439
Cdd:cd14906 321 QALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRkfnqntqsndlAGGSNKKNNLFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 440 GFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKG 518
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKsDGILSLLDDECIMPKG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 519 TDDTWAQKlYNTHLNKCALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKA 598
Cdd:cd14906 481 SEQSLLEK-YNKQYHNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQITS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 599 ISPTSATSSGRTpltrtlskptkgrpgqtakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAV 678
Cdd:cd14906 560 TTNTTKKQTQSN-----------------------TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVL 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 679 QQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLSDRKQTCKNVLEKLIV---------------------- 736
Cdd:cd14906 617 SQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIqsklktmgisnnkkknnsnsns 696
|
730
....*....|....*..
gi 1542868643 737 ----DKDKYQFGKTKIF 749
Cdd:cd14906 697 nttnDKPLFQIGKTKIF 713
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
83-749 |
1.92e-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: 442.89 E-value: 1.92e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSG-QNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14876 1 PCVLDFLKHRYLKNQ-IYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 162 SGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:cd14876 80 SGESGAGKTEATKQIMRYFASAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 242 YLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNqGGSPVIEGVDDAKEMAHTRQACTLLGISESH 321
Cdd:cd14876 160 FLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLN-PKCLDVPGIDDVADFEEVLESLKSMGLTEEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 322 QMGIFRILAGILHLGNVVFMSRD----SDSCTIPPkhEPLSIF---CDLMGVDFEELCHWLChRKLATATETYIK-PISK 393
Cdd:cd14876 239 IDTVFSIVSGVLLLGNVKITGKTeqgvDDAAAISN--ESLEVFkeaCSLLFLDPEALKRELT-VKVTKAGGQEIEgRWTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 394 LQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLE 473
Cdd:cd14876 316 DDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 474 QEEYMKEQIPWTLIDFYDNQPCIN-LIESKLGILDLLDEECKMPKGTDD----TWAQKLYNthlNKCALFEKpRLSNKAF 548
Cdd:cd14876 396 SKLYKDEGIPTAELEYTSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEkfvsACVSKLKS---NGKFKPAK-VDSNINF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 549 IIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekaisptsatssgrTPLTRtlskptkgrpGQTA 628
Cdd:cd14876 472 IVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEG---------------VVVEK----------GKIA 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 629 KehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 708
Cdd:cd14876 527 K--GSLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLY 604
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1542868643 709 RYRVL-MKQKDVLSDRKQT-CKNVLEKLIVDKDKYQFGKTKIF 749
Cdd:cd14876 605 QFKFLdLGIANDKSLDPKVaALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
84-736 |
4.64e-129 |
|
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: 422.20 E-value: 4.64e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYS---GQNMGDM-------DPHIFAVAEEAYKQMAR 152
Cdd:cd14899 2 SILNALRLRY-ERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhNSQFGDRvtstdprEPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 153 DERNQSIIVSGESGAGKTVSAKYAMRYFATVSG----------------SASEANVEEKVLASNPIMESIGNAKTTRNDN 216
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGtgnnnltnsesisppaSPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 217 SSRFGKYIEIGF-DKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQL------CASADLSEFKVLRlGDANNFHYTN 289
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELlsadnnCVSKEQKQVLALS-GGPQSFRLLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 290 QG-GSPVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVVFM--------------SRDSDSCTIPPKH 354
Cdd:cd14899 240 QSlCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEqiphkgddtvfadeARVMSSTTGAFDH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 355 epLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVK------ 428
Cdd:cd14899 320 --FTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASapwgad 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 429 ---------QHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLI 499
Cdd:cd14899 398 esdvddeedATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 500 ESK-LGILDLLDEECKMPKGTDDTWAQKLY--------NTHLNKCALFEKprlsNKAFIIQHFADKVEYQCEGFLEKNKD 570
Cdd:cd14899 478 EHRpIGIFSLTDQECVFPQGTDRALVAKYYlefekknsHPHFRSAPLIQR----TTQFVVAHYAGCVTYTIDGFLAKNKD 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 571 TVFEEQIKVLKSSKFKMLPELfqddekAISPTSATSSGRTPLTRTLSKPTKGRPGQTAkehKKTVGHQFRNSLHLLMETL 650
Cdd:cd14899 554 SFCESAAQLLAGSSNPLIQAL------AAGSNDEDANGDSELDGFGGRTRRRAKSAIA---AVSVGTQFKIQLNELLSTV 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 651 NATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYR----VLMKQKDVLSDRKQT 726
Cdd:cd14899 625 RATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYRrvllSLYKWGDNDFERQMR 704
|
730
....*....|
gi 1542868643 727 CKNVLEKLIV 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 |
4.48e-125 |
|
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: 408.51 E-value: 4.48e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 85 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMG-----DMDPHIFAVAEEAYKQMARDERNQS 158
Cdd:cd14886 3 VIDILRDRFAKDK-IYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 159 IIVSGESGAGKTVSAKYAMRYFAtVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGAN 238
Cdd:cd14886 82 CIVSGESGAGKTETAKQLMNFFA-YGHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 239 MRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLgIS 318
Cdd:cd14886 161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKL-FS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 319 ESHQMGIFRILAGILHLGNVVFMSRDS---DSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14886 240 KNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQE 475
Cdd:cd14886 320 AEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEIQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 476 EYMKEQIPWTLIDFYDNQPCINLIES-KLGILDLLDEECKMPKGTDDTWAQKLyNTHLNKcALFEKPRLSNKAFIIQHFA 554
Cdd:cd14886 400 EYEIEGIDHSMITFTDNSNVLAVFDKpNLSIFSFLEEQCLIQTGSSEKFTSSC-KSKIKN-NSFIPGKGSQCNFTIVHTA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 555 DKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekaisptsatssgrtpltrtlskptkgRPGQTAKEHKKT 634
Cdd:cd14886 478 ATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSD----------------------------IPNEDGNMKGKF 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 635 VGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLM 714
Cdd:cd14886 530 LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILI 609
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1542868643 715 KQKDVL----SDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 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 |
1.13e-122 |
|
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: 402.27 E-value: 1.13e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 85 VLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAY-SGQNMGDMDPHIFAVAEEAYKQM-ARDERNQSIIVS 162
Cdd:cd14875 3 LLHCIKERFEKLHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 163 GESGAGKTVSAKYAMRYFATVS----GSASEANVEEKVLA----SNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRI 234
Cdd:cd14875 83 GESGSGKTENAKMLIAYLGQLSymhsSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPTSGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 235 -IGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVL-RLGDANNFHYTNQGGSPVIEGVD-----DAKEMAH 307
Cdd:cd14875 163 mVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTFVRRGVDgktldDAHEFQN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 308 TRQACTLLGISESHQMGIFRILAGILHLGNVVFMSRDSDSCTIPpKHEPLSIFCDLMGVDFEEL--CHWLchrKLATATE 385
Cdd:cd14875 243 VRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIA-DETPFLTACRLLQLDPAKLreCFLV---KSKTSLV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 386 TYIKpiSKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHS--FIGVLDIYGFETFEINSFEQFCINYANEKLQQ 463
Cdd:cd14875 319 TILA--NKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCSGckYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 464 QFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR 542
Cdd:cd14875 397 HYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKrTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPYFVLPK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 543 --LSNKaFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSkfkmlpelfqDDEkaisptsatssgrtpLTRTLSKPT 620
Cdd:cd14875 477 stIPNQ-FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNS----------TDE---------------FIRTLLSTE 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 621 KGrpgqtAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSR 700
Cdd:cd14875 531 KG-----LARRKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVR 605
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 701 WTYQEFFSRYRVLM--------KQKDvLSDRKQTCKNVLEKLIV-DKDKYQFGKTKIFFR 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 |
1.23e-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: 376.55 E-value: 1.23e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 84 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQlpIYGEDIINAYSgQNMGDMDPHIFAVAEEAYKQMARdERNQSIIVSG 163
Cdd:cd14898 2 ATLEILEKRYASGK-IYTKSGLVFLALNPYET--IYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 164 ESGAGKTVSAKYAMRYFatVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRyrIIGANMRTYL 243
Cdd:cd14898 77 ESGSGKTENAKLVIKYL--VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFDGK--ITGAKFETYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 244 LEKSRVVFQAEEERNYHIFYQLCASADLSEfkvlrlgdANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQm 323
Cdd:cd14898 153 LEKSRVTHHEKGERNFHIFYQFCASKRLNI--------KNDFIDTSSTAGNKESIVQLSEKYKMTCSAMKSLGIANFKS- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 324 gIFRILAGILHLGNVVFmsrDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATEtYIKPISKL-QATNARDA 402
Cdd:cd14898 224 -IEDCLLGILYLGSIQF---VNDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGE-TIEVFNTLkQARTIRNS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 403 LAKHIYAKLFNWIVDHVNQALhSAVKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQI 482
Cdd:cd14898 299 MARLLYSNVFNYITASINNCL-EGSGERS-ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEGI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 483 PWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKL--YNTHlnkcalFEKPRLSNKaFIIQHFADKVEYQ 560
Cdd:cd14898 377 EWPDVEFFDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIkkYLNG------FINTKARDK-IKVSHYAGDVEYD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 561 CEGFLEKNKDtvfEEQIKVLKSskfkmlpelfqddekaisptsatssgrtpltrtlskptkgrPGQTAKEHKKTVGHQFR 640
Cdd:cd14898 450 LRDFLDKNRE---KGQLLIFKN-----------------------------------------LLINDEGSKEDLVKYFK 485
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1542868643 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 |
4.97e-110 |
|
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: 365.72 E-value: 4.97e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 84 AVLHNLRVRFIdSKLIYTYCGI-VLVAINPYEQLPI--------YGEDIINAYSGQNMGDMdPHIFAVAEEAYKQMARDE 154
Cdd:cd14879 5 AITSHLASRFR-SDLPYTRLGSsALVAVNPYKYLSSnsdaslgeYGSEYYDTTSGSKEPLP-PHAYDLAARAYLRMRRRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 155 RNQSIIVSGESGAGKTVSAKYAMRYFATVSGSAS-EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14879 83 EDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKkGTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYT---NQGGSPVIEGVDDAKEMAHTRQ 310
Cdd:cd14879 163 LIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasyGCHPLPLGPGSDDAEGFQELKT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 311 ACTLLGISESHQMGIFRILAGILHLGNVVFM---SRDSDSCTIPPKHEpLSIFCDLMGVDFEELCHWL------CHRKLA 381
Cdd:cd14879 243 ALKTLGFKRKHVAQICQLLAAILHLGNLEFTydhEGGEESAVVKNTDV-LDIVAAFLGVSPEDLETSLtyktklVRKELC 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 382 TateTYIKPIsklQATNARDALAKHIYAKLFNWIVDHVNQALhSAVKQ--HSFIGVLDIYGFETF---EINSFEQFCINY 456
Cdd:cd14879 322 T---VFLDPE---GAAAQRDELARTLYSLLFAWVVETINQKL-CAPEDdfATFISLLDFPGFQNRsstGGNSLDQFCVNF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 457 ANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECK-MPKGTDDTWAQKLYNTHLNK 534
Cdd:cd14879 395 ANERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKpGGLLGILDDQTRrMPKKTDEQMLEALRKRFGNH 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 535 CALFEKPRLSNK----AFIIQHFADKVEYQCEGFLEKNKDTVfeeqikvlkSSKFKMLpelfqddekaISPTsatssgrt 610
Cdd:cd14879 475 SSFIAVGNFATRsgsaSFTVNHYAGEVTYSVEGFLERNGDVL---------SPDFVNL----------LRGA-------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 611 pltrtlskptkgrpgqtakehkktvgHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETI 690
Cdd:cd14879 528 --------------------------TQLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELA 581
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 691 RISAAGFPSRWTYQEFFSRYrvlmKQKDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFF 750
Cdd:cd14879 582 ARLRVEYVVSLEHAEFCERY----KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
85-751 |
6.74e-97 |
|
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: 329.27 E-value: 6.74e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 85 VLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 164
Cdd:cd01386 3 VLHTLRQRY-GANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 165 SGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 244
Cdd:cd01386 82 SGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 245 EKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRL---GDANNFhytnqGGSPVIEGVD---DAKEMAHTRQACTLLGIS 318
Cdd:cd01386 162 ERSRVARRPEGESNFNVFYYLLAGADAALRTELHLnqlAESNSF-----GIVPLQKPEDkqkAAAAFSKLQAAMKTLGIS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 319 ESHQMGIFRILAGILHLGNvvfmsrdSDSCTIPP-------KHEPLSIFCDLMGVDFEELCHWLCHRKL------ATATE 385
Cdd:cd01386 237 EEEQRAIWSILAAIYHLGA-------AGATKAASagrkqfaRPEWAQRAAYLLGCTLEELSSAIFKHHLsggpqqSTTSS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 386 TYIKPIS------KLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFE------INSFEQFC 453
Cdd:cd01386 310 GQESPARsssggpKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAhsgsqrGATFEDLC 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 454 INYANEKLQQQFNMHVFKLEQEEYMKEQIPwtlIDFYDNQPC----INLI---------------ESKLGILDLLDEECK 514
Cdd:cd01386 390 HNYAQERLQLLFHERTFVAPLERYKQENVE---VDFDLPELSpgalVALIdqapqqalvrsdlrdEDRRGLLWLLDEEAL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 515 MPKGTDDTWAQKLYnTHLNKCALFEKPRLSNKA-----FIIQHF--ADKVEYQCEGFLEKNKDTVFEEQikvlksskfkm 587
Cdd:cd01386 467 YPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSegplqFVLGHLlgTNPVEYDVSGWLKAAKENPSAQN----------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 588 LPELFQDDEKaisptsatssgrtpltrtlskptkgrpgQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPN--- 664
Cdd:cd01386 535 ATQLLQESQK----------------------------ETAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQhna 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 665 ---DFKFPFTFDEKRAVQ------QLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK-------QKDVLSDRKQTCK 728
Cdd:cd01386 587 gkdERSTSSPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPpltkklgLNSEVADERKAVE 666
|
730 740
....*....|....*....|...
gi 1542868643 729 NVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd01386 667 ELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
84-751 |
3.32e-96 |
|
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: 326.39 E-value: 3.32e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 84 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAY---SGQNMGDMDPHIFAVAEEAYKQMARDERNQSII 160
Cdd:cd14878 2 SLLYEIQKRFGNNQ-IYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 161 VSGESGAGKTVSAKYAMRYFATVSGSaSEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGF-DKRYRIIGANM 239
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASS-SRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 240 RTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQG---GSPVIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14878 160 YTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmreDVSTAERSLNREKLAVLKQALNVVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 317 ISESHQMGIFRILAGILHLGNVVFMS-RDSDSCTIpPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14878 240 FSSLEVENLFVILSAILHLGDIRFTAlTEADSAFV-SDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSF----IGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFK 471
Cdd:cd14878 319 AEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 472 LEQEEYMKEQIPW----------TLIDFYDNQPcinlieskLGILDLLDEECKMPKGTDDTWAQKLY----NTHLNKCAL 537
Cdd:cd14878 399 QEQTECVQEGVTMetayspgnqtGVLDFFFQKP--------SGFLSLLDEESQMIWSVEPNLPKKLQslleSSNTNAVYS 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 538 FEK-------PRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQddekaisptsatssgrt 610
Cdd:cd14878 471 PMKdgngnvaLKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ----------------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 611 pltrtlSKPTkgrpgqtakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETI 690
Cdd:cd14878 534 ------SKLV-------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMV 594
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1542868643 691 RISAAGFPSRWTYQEFFSRYRVLMKQkdVLSDRKQT-----CKNVLEKliVDKDKYQFGKTKIFFR 751
Cdd:cd14878 595 KIFRYGYPVRLSFSDFLSRYKPLADT--LLGEKKKQsaeerCRLVLQQ--CKLQGWQMGVRKVFLK 656
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
83-751 |
5.87e-95 |
|
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: 324.68 E-value: 5.87e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFI-------DSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDER 155
Cdd:cd14887 1 PNLLENLYQRYNkayinkeNRNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 156 NQSIIVSGESGAGKTVSAKYAMRYFATVS---GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSdrrHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYtnqggspviegvddakEMAHTRQAC 312
Cdd:cd14887 161 KLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPEST----------------DLRRITAAM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 313 TLLGISESHQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHR---KLATATETYIK 389
Cdd:cd14887 225 KTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSVSVGCEETAADRSHSSEVKCLSsglKVTEASRKHLK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 390 PISKL--------------------------------QATNARDALAKHIYAKLFNWIVDHVNQALHSAVK--------- 428
Cdd:cd14887 305 TVARLlglppgvegeemlrlalvsrsvretrsffdldGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsded 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 429 -----QHSFIGVLDIYGFETFE---INSFEQFCINYANEKLqqqfnmHVFKLEQ-----------EEYMKEQI------- 482
Cdd:cd14887 385 tpsttGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERL------HCFLLEQlilnehmlytqEGVFQNQDcsafpfs 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 483 ----------PWTLIDF-----------YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKP 541
Cdd:cd14887 459 fplastltssPSSTSPFsptpsfrsssaFATSPSLPSSLSSLSSSLSSSPPVWEGRDNSDLFYEKLNKNIINSAKYKNIT 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 542 R---LSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEqikvlksskfkmLPELFqddekaisptsatSSGRTPLTRTLSK 618
Cdd:cd14887 539 PalsRENLEFTVSHFACDVTYDARDFCRANREATSDE------------LERLF-------------LACSTYTRLVGSK 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 619 PTKGRpgQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFP 698
Cdd:cd14887 594 KNSGV--RAISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFP 671
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1542868643 699 SRWTYQEFFSRY--RVLMKQKDVLSDrKQTCKNVLEKLIVDKDKYQFGKTKIFFR 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 |
1.61e-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: 320.81 E-value: 1.61e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 85 VLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYgediINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 164
Cdd:cd14937 3 VLNMLALRY-KKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 165 SGAGKTVSAKYAMRYFatVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 244
Cdd:cd14937 78 SGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 245 EKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGgSPVIEGVDDAKEMAHTRQACTLLGISESHQmG 324
Cdd:cd14937 156 ENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNK-NVVIPEIDDAKDFGNLMISFDKMNMHDMKD-D 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 325 IFRILAGILHLGNVVFMSRDS---DSCTIPPKH--EPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQATNA 399
Cdd:cd14937 234 LFLTLSGLLLLGNVEYQEIEKggkTNCSELDKNnlELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 400 RDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 479
Cdd:cd14937 314 CKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYKA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 480 EQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTwaqkLYNTHLNKCALFEK----PRLSNKAFIIQHFAD 555
Cdd:cd14937 394 EDILIESVKYTTNESIIDLLRGKTSIISILEDSCLGPVKNDES----IVSVYTNKFSKHEKyastKKDINKNFVIKHTVS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkaisptSATSSGRtpltrtlskptkgrpgqtakehKKTV 635
Cdd:cd14937 470 DVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE------VSESLGR----------------------KNLI 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAgFPSRWTYQEFFSRYRVL-- 713
Cdd:cd14937 522 TFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNISFF-FQYKYTFDVFLSYFEYLdy 600
|
650 660 670
....*....|....*....|....*....|....*...
gi 1542868643 714 MKQKDVLSDRKQTCKNVLEKlIVDKDKYQFGKTKIFFR 751
Cdd:cd14937 601 STSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
84-750 |
1.22e-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: 312.05 E-value: 1.22e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 84 AVLHNLRVRFIDSKLiYTYCGIVLVAINPYEqlpiygeDIINAY---SGQNMGDMdPHIFAVAEEAYKQMARDERNQSII 160
Cdd:cd14881 2 AVMKCLQARFYAKEF-FTNVGPILLSVNPYR-------DVGNPLtltSTRSSPLA-PQLLKVVQEAVRQQSETGYPQAII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 161 VSGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKryriiGANMR 240
Cdd:cd14881 73 LSGTSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-----GALYR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 241 T----YLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLG--DANNFHYTNQgGSPVIEGVDDAKEMAHTRQACTL 314
Cdd:cd14881 148 TkihcYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgySPANLRYLSH-GDTRQNEAEDAARFQAWKACLGI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 315 LGISESHQMgifRILAGILHLGNVVFMsrDSDSCTIPPKHE-PLSIFCDLMGVDFEELchwlcHRKLATATET----YIK 389
Cdd:cd14881 227 LGIPFLDVV---RVLAAVLLLGNVQFI--DGGGLEVDVKGEtELKSVAALLGVSGAAL-----FRGLTTRTHNargqLVK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 390 PISKLQATNA-RDALAKHIYAKLFNWIVDHVN--QALHSAVKQHS---FIGVLDIYGFETFEINSFEQFCINYANEKLQQ 463
Cdd:cd14881 297 SVCDANMSNMtRDALAKALYCRTVATIVRRANslKRLGSTLGTHAtdgFIGILDMFGFEDPKPSQLEHLCINLCAETMQH 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 464 QFNMHVFKLEQEEYMKEQIPWTL-IDFYDNQPCINLIES-KLGILDLLDEECKmPKGTDDTWAQKLYNTHLNKCALFEKP 541
Cdd:cd14881 377 FYNTHIFKSSIESCRDEGIQCEVeVDYVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 542 RLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVL--KSSKFKMLPELfQDdekaisptsatssgrtpltrtlskp 619
Cdd:cd14881 456 PQDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFykQNCNFGFATHT-QD------------------------- 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 620 tkgrpgqtakehkktvghqFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPS 699
Cdd:cd14881 510 -------------------FHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPH 570
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1542868643 700 RWTYQEFFSRYRVL--MKQKDVLSDRKQTCKNVLEKLIVDKDK---------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 |
1.98e-90 |
|
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: 310.30 E-value: 1.98e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYS-------GQNMGDMDPHIFAVAEEAYKQMARDE 154
Cdd:cd14884 1 PNVLQNLKNRYLKNK-IYTFHASLLLALNPYKPLKeLYDQDVMNVYLhkksnsaASAAPFPKAHIYDIANMAYKNMRGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 155 RNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR--- 231
Cdd:cd14884 80 KRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVent 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 232 ------YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQL---CASADLSE---------FKVLRL-------GDANNFH 286
Cdd:cd14884 160 qknmfnGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVlrgLSDEDLARrnlvrncgvYGLLNPdeshqkrSVKGTLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 287 YTNQGGSPVIEGVD-DAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNvvfmsrDSDSCTippkheplsifCDLMG 365
Cdd:cd14884 240 LGSDSLDPSEEEKAkDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGN------RAYKAA-----------AECLQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 366 VDFEELCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQAL------------HSAVKQHSFI 433
Cdd:cd14884 303 IEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdesdneDIYSINEAII 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 434 GVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESklgILDLLDEEC 513
Cdd:cd14884 383 SILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAK---IFRRLDDIT 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 514 KMP----KGTDDTWAQKLYNTHlNKCALFEK-------PRL---SNKA-------FIIQHFADKVEYQCEGFLEKNKDTV 572
Cdd:cd14884 460 KLKnqgqKKTDDHFFRYLLNNE-RQQQLEGKvsygfvlNHDadgTAKKqnikkniFFIRHYAGLVTYRINNWIDKNSDKI 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 573 feeqikvlksskfkmlpelfqddEKAISPTSATSSGRTpLTRTLSKPTKGrpgqtakeHKKTVGHQFRNSLHLLMETLNA 652
Cdd:cd14884 539 -----------------------ETSIETLISCSSNRF-LREANNGGNKG--------NFLSVSKKYIKELDNLFTQLQS 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 653 TTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkQKDVLSDRKQTCKNVLE 732
Cdd:cd14884 587 TDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKETAAALKEQI-AKELEKCNSNTDIEYQR 665
|
730
....*....|....*...
gi 1542868643 733 KLIVDKDKYQFGKTKIFF 750
Cdd:cd14884 666 RLAALDVQFIPDGRLYAF 683
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
97-751 |
3.95e-90 |
|
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: 308.94 E-value: 3.95e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 97 KLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSgQNMGdMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKY 175
Cdd:cd14905 14 EIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN-QRRG-LPPHLFALAAKAISDMQDFRRDQLIFIGGESGSGKSENTKI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 176 AMRYFATVSGSASEAnVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEE 255
Cdd:cd14905 92 IIQYLLTTDLSRSKY-LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQNKG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 256 ERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHL 335
Cdd:cd14905 171 ERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFIIIL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 336 GNVVFMSRDSDSctiPPKHEPLsifcdlmgvdFEELCHWLCHRklATATETYI---KPISKLQATNARDALAKHIYAKLF 412
Cdd:cd14905 251 GNVTFFQKNGKT---EVKDRTL----------IESLSHNITFD--STKLENILisdRSMPVNEAVENRDSLARSLYSALF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 413 NWIVDHVNQALHSAVKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPW-TLIDFYD 491
Cdd:cd14905 316 HWIIDFLNSKLKPTQYSHT-LGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWmTPISFKD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 492 NQPCINLIESklgILDLLDEECKMPKGTDDTWAQKLYNtHLNKCALF-EKPrlsNKaFIIQHFADKVEYQCEGFLEKNKD 570
Cdd:cd14905 395 NEESVEMMEK---IINLLDQESKNINSSDQIFLEKLQN-FLSRHHLFgKKP---NK-FGIEHYFGQFYYDVRGFIIKNRD 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 571 TVFEEQIKVLKSSKFKMLpeLFQDDEKAISPTSA---------TSSGRTPLT--RTLSKPTKGRPGQTAKEHKKTVG--- 636
Cdd:cd14905 467 EILQRTNVLHKNSITKYL--FSRDGVFNINATVAelnqmfdakNTAKKSPLSivKVLLSCGSNNPNNVNNPNNNSGGggg 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 637 --------------HQFRNSLHLLMETLNATTpHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWT 702
Cdd:cd14905 545 ggnsgggsgsggstYTTYSSTNKAINNSNCDF-HFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYN 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1542868643 703 YQEFFSRYRVLMKQkdvlsdrKQTCKNVLEKLI---VDKDK-----YQFGKTKIFFR 751
Cdd:cd14905 624 NKIFFDRFSFFFQN-------QRNFQNLFEKLKendINIDSilpppIQVGNTKIFLR 673
|
|
| Myo5-like_CBD |
cd14945 |
Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied ... |
1480-1803 |
1.82e-85 |
|
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: 281.59 E-value: 1.82e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1480 EDEQKLVKNLILELKPRGVAVNLipgLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNT 1559
Cdd:cd14945 1 SEEDSLLRGIVTDFEPSSGDHKL---TPAYILYLCIRHAASNGLTGQSTSLLNKVLKTIQQVVQQHNDDMQLLAFWLSNA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1560 CRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmivsgmlehetiqgvsgv 1639
Cdd:cd14945 78 SELLYFLKQDSKLYGAAGEAPQKEEEQKLTVSDLNELKQDLEAVSIKIYQQALKYLNKNLQP------------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1640 kptglrkrtssiadegtyTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAVTLNNLLLRKDMCSWSKGMQIRY 1719
Cdd:cd14945 140 ------------------KIRDIVKFLNSFLDLLKSFHVHPEIRSQVFTQLFSFINARLFNQLITKKDALSWSRGMQIRA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1720 NVSQLEEWLRDKNLmNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFI 1799
Cdd:cd14945 202 NISRLEEWCEGRGL-EHLAVDFLSKLIQAVQLLQLKKYTQEDIEILCELCPSLNPAQLQAILTQYQPANYGESPVPKEIL 280
|
....
gi 1542868643 1800 RTIQ 1803
Cdd:cd14945 281 RTLA 284
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
84-751 |
5.05e-84 |
|
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: 289.85 E-value: 5.05e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYsgqnmgdmdpHIFAVAEEAYKQMARDERN-QSIIVS 162
Cdd:cd14874 2 GIAQNLHERF-KKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 163 GESGAGKTVSAKYAMRYFATVSGSASEAnveEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMR-T 241
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTT---KHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLNLKyT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 242 YLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSpvIEGV-DDAKEMAHTRQACTLLGISES 320
Cdd:cd14874 147 VPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNS--TENIqSDVNHFKHLEDALHVLGFSDD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 321 HQMGIFRILAGILHLGNVVFMSR-----DSDSCTIPPKHEpLSIFCDLMGVDFEELCHWLchrklaTATETYIKPISKLQ 395
Cdd:cd14874 225 HCISIYKIISTILHIGNIYFRTKrnpnvEQDVVEIGNMSE-VKWVAFLLEVDFDQLVNFL------LPKSEDGTTIDLNA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 396 ATNARDALAKHIYAKLFNWIVD----HVNQALHSAVkqhsfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFK 471
Cdd:cd14874 298 ALDNRDSFAMLIYEELFKWVLNriglHLKCPLHTGV-----ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFH 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 472 LEQEEYMKEQIPwtlIDF-----YDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCAlFEKPRLSN 545
Cdd:cd14874 373 DQLVDYAKDGIS---VDYkvpnsIENGKTVELLFKKpYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS-YGKARNKE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 546 K-AFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQddekaiSPTSATSsgrtpltrtlskptkgrp 624
Cdd:cd14874 449 RlEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE------SYSSNTS------------------ 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 625 gqtakEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQ 704
Cdd:cd14874 505 -----DMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKT 579
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1542868643 705 EFFSRYRVLMKqKDV--LSDRKQTCKNVLEKLIVD-KDKYQFGKTKIFFR 751
Cdd:cd14874 580 TFARQYRCLLP-GDIamCQNEKEIIQDILQGQGVKyENDFKIGTEYVFLR 628
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
86-750 |
5.21e-74 |
|
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: 263.76 E-value: 5.21e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 86 LHNLRVRF-IDSklIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQN----------MGDMDPHIFAVAEEAYKQMARDE 154
Cdd:cd14893 4 LYTLRARYrMEQ--VYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSReqtplyekdtVNDAPPHVFALAQNALRCMQDAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 155 RNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEAN-----------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKY 223
Cdd:cd14893 82 EDQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPdsegasgvlhpIGQQILHAFTILEAFGNAATRQNRNSSRFAKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 224 IEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASA--DLSEFKVLRLGD-ANNFHYTNQGGSPVIEGVD 300
Cdd:cd14893 162 ISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVqhDPTLRDSLEMNKcVNEFVMLKQADPLATNFAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 301 DAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVVFMS----------------RDSDSCTIppkHEPLSIF--CD 362
Cdd:cd14893 242 DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPdpeggksvggansttvSDAQSCAL---KDPAQILlaAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 363 LMGVDFEELCHWLCHRKL----ATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQAL---------HSAVKQ 429
Cdd:cd14893 319 LLEVEPVVLDNYFRTRQFfskdGNKTVSSLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdryekSNIVIN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 430 HSFIGVLDIYGFETFE--INSFEQFCINYANEKLQQQF-------NMHVFKLEQEEYMKEQIPWTLIDF-YDNQPCINLI 499
Cdd:cd14893 399 SQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvqntlaiNFSFLEDESQQVENRLTVNSNVDItSEQEKCLQLF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 500 ESK-LGILDLLDEECKMPKGTDDTWAQKLYN--------THLNKCALFEKPRLSNKA-----FIIQHFADKVEYQCEGFL 565
Cdd:cd14893 479 EDKpFGIFDLLTENCKVRLPNDEDFVNKLFSgneavgglSRPNMGADTTNEYLAPSKdwrllFIVQHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 566 EKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGrtplTRTLSKPTKGRPGQTAKEHKKTVGH----QFRN 641
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAAKQT----EERGSTSSKFRKSASSARESKNITDsaatDVYN 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 642 SLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYrvlmkqKDVLS 721
Cdd:cd14893 635 QADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY------KNVCG 708
|
730 740 750
....*....|....*....|....*....|...
gi 1542868643 722 DRKqTCKNVLEKL----IVDKDKYQFGKTKIFF 750
Cdd:cd14893 709 HRG-TLESLLRSLsaigVLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
85-751 |
2.42e-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: 232.32 E-value: 2.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 85 VLHNLRVRfIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 164
Cdd:cd14882 3 ILEELRHR-YLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 165 SGAGKTVSAKYAMRYFATVSGSASeaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 244
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNR--GATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 245 EKSRVVFQAEEERNYHIFYQLCASADLSE-FKVLRLGDANNFHY----TNQGGSPVIEGVDD----AKEMAHTRQACTLL 315
Cdd:cd14882 160 EKLRVSTTDGNQSNFHIFYYFYDFIEAQNrLKEYNLKAGRNYRYlripPEVPPSKLKYRRDDpegnVERYKEFEEILKDL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 316 GISESHQMGIFRILAGILHLGNVVFmsRDSDSCTIPPKHEPLSIFCDLMGVDFEELCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14882 240 DFNEEQLETVRKVLAAILNLGEIRF--RQNGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHTTEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 396 ATNARDALAKHIYAKLFNWIVDHVNQALH--SAV--KQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFK 471
Cdd:cd14882 318 ARDARDVLASTLYSRLVDWIINRINMKMSfpRAVfgDKYS-ISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYNQRIFI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 472 LEQEEYMKEQIPWTLIDFYDNQPCI-NLIESKLGILDLLDEECKMPKGtddtwAQKLYNTHLNKCALFEKPrLSNKAFII 550
Cdd:cd14882 397 SEMLEMEEEDIPTINLRFYDNKTAVdQLMTKPDGLFYIIDDASRSCQD-----QNYIMDRIKEKHSQFVKK-HSAHEFSV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 551 QHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkaisptsatssgrtplTRTLskptkgrpgqtake 630
Cdd:cd14882 471 AHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQ----------------VRNM-------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 631 hkKTVGHQFRNSLHLLMETL----NATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEF 706
Cdd:cd14882 521 --RTLAATFRATSLELLKMLsigaNSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEF 598
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1542868643 707 FSRYRVLMKQKDVLSD-RKQTCKNVLEKLIVdkDKYQFGKTKIFFR 751
Cdd:cd14882 599 LRRYQFLAFDFDETVEmTKDNCRLLLIRLKM--EGWAIGKTKVFLK 642
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
106-229 |
8.13e-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: 8.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 106 VLVAINPYEQLPIYGED-IINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVS 184
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1542868643 185 GSASEAN--------------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFD 229
Cdd:cd01363 81 FNGINKGetegwvylteitvtLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLD 139
|
|
| DIL |
pfam01843 |
DIL domain; The DIL domain has no known function. |
1685-1788 |
8.87e-42 |
|
DIL domain; The DIL domain has no known function.
Pssm-ID: 460359 [Multi-domain] Cd Length: 103 Bit Score: 148.89 E-value: 8.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1685 QVVKQMFYIVGAVTLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLmNSGAKETLEPLIQAAQLLQVKKKTDDDAEA 1764
Cdd:pfam01843 1 QLFSQLFYFINAELFNRLLLRKKYCSWSKGMQIRYNLSRLEEWARSNGL-ESEARDHLAPLIQAAQLLQLRKSTLEDLDS 79
|
90 100
....*....|....*....|....
gi 1542868643 1765 ICSMCNALTTAQIVKVLNLYTPVN 1788
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 |
1.69e-39 |
|
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: 158.85 E-value: 1.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 83 PAVLHNLRVRFIDSKLiYTYCGIVLVAINPYEQLPIYGEDIINAYSGQN-MGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14938 1 PSVLYHLKERFKNNKF-YTKMGPLLIFINPKINNNINNEETIEKYKCIDcIEDLSLNEYHVVHNALKNLNELKRNQSIII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 162 SGESGAGKTVSAKYAMRYFA-TVSGSASEA---------------------NVEEKVLASNPIMESIGNAKTTRNDNSSR 219
Cdd:cd14938 80 SGESGSGKSEIAKNIINFIAyQVKGSRRLPtnlndqeednihneentdyqfNMSEMLKHVNVVMEAFGNAKTVKNNNSSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 220 FGKYIEIGFDKRyRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASADLSEFKVLRLGDANNFHYTNQGGSPVIEGV 299
Cdd:cd14938 160 FSKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 300 DDAKEMAHTRQACTLLGISESHQMgIFRILAGILHLGNV----------VFMSR-----------------DSDSCTIPP 352
Cdd:cd14938 239 YSGKILELLKSLNYIFDDDKEIDF-IFSVLSALLLLGNTeivkafrkksLLMGKnqcgqninyetilseleNSEDIGLDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 353 KHEPLSIFCDLMGVDFEELCHWLCHRKLATATeTYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQ---ALHSAVKQ 429
Cdd:cd14938 318 NVKNLLLACKLLSFDIETFVKYFTTNYIFNDS-ILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEkctQLQNININ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 430 HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTL-IDFYDNQPCIN-LIESKLGILD 507
Cdd:cd14938 397 TNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNlLVGPTEGSLF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 508 LLDEECKMPKGTDDTwaqKLYNTHLNKCA-----LFEKPRLSN-KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLK 581
Cdd:cd14938 477 SLLENVSTKTIFDKS---NLHSSIIRKFSrnskyIKKDDITGNkKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVK 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 582 SSKFKMLPELFQ----DDEKAISPTSATSSGRTPLtrTLSKPTKGRPGQTAKEhkktvghQFRNSLHLLMETLNATTPHY 657
Cdd:cd14938 554 QSENEYMRQFCMfynyDNSGNIVEEKRRYSIQSAL--KLFKRRYDTKNQMAVS-------LLRNNLTELEKLQETTFCHF 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 658 VRCIKPNDFK-FPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkqkdvlSDRKQTCKNVLEKLIV 736
Cdd:cd14938 625 IVCMKPNESKrELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKN------EDLKEKVEALIKSYQI 698
|
730
....*....|...
gi 1542868643 737 DKDKYQFGKTKIF 749
Cdd:cd14938 699 SNYEWMIGNNMIF 711
|
|
| Myo5p-like_CBD_DIL_ANK |
cd15473 |
cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ... |
1506-1835 |
2.68e-31 |
|
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: 126.13 E-value: 2.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1506 LPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNTCRFLHCLKQysgEEGFmkhntsrqne 1585
Cdd:cd15473 32 VPANLLFLCARYAHYHCSPELLEDLLLGALDRIEDVVEANPWDMTLLAFWLSNVTLLLHYLKK---DAGL---------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1586 hcltNFDLAEYRQVLSDLAIQIYQQLVRVLEnilqpmivsgmlehetiqgvsgvkptglrKRTSSIADEGTYTLDSIlrq 1665
Cdd:cd15473 99 ----VEATPEFQQELAELINEIFVLIIRDAE-----------------------------RRIDKLLDASPRNITSL--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1666 LNSFHSVMCQHGMDPELIKQVVKQMFYIVGAVTLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLM-------NSGA 1738
Cdd:cd15473 143 LSSTLYVLELYDVHPAIIIQALSQLFYWLGCELFNRILTNKKYLCRSKAMQIRMNLSALEDWARSNNLQpekgespPRIA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1739 KETLEPLIQAAQLLQVKKKTDDDAEAICSM--CNALTTAQIVKVLNLYTP-VNefEERVSVSFIRTIQMRLRDRKDSpql 1815
Cdd:cd15473 223 RSHLAPVIQLLQWLQCLSSLDDFESLIATIqqLDALNPLQLLRAVKDYRYeVN--EGRMPEECVKYLAQLQKDWLDS--- 297
|
330 340
....*....|....*....|
gi 1542868643 1816 lmdaKHIFPVTFPFNPSSLA 1835
Cdd:cd15473 298 ----RYMLPFSLPTDTEMLV 313
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
196-734 |
3.07e-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: 127.17 E-value: 3.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 196 VLASNPIMESIGNAKTTRNDNSSRFGKY--IEIGFDK---RYRIIGANMRTYLLEKSRVVFQA------EEERNYHIFYQ 264
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLhpwEFQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 265 LCASADLSEF-----KVLRLG--DANNFHYTNQGGSPVIEGVD-------DAKEMAHTRQACTLLGISESHQMGIFRILA 330
Cdd:cd14894 329 MVAGVNAFPFmrllaKELHLDgiDCSALTYLGRSDHKLAGFVSkedtwkkDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 331 GILHLGNVVFMSRDSDSCTIPPK----HEPLSIFCDLMGVDFEELCHWLCHRK--LATATETYIKPISKLQATNARDALA 404
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSStgalNAPQKVVELLELGSVEKLERMLMTKSvsLQSTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 405 KHIYAKLFNWIVDHVNQALH-----------------SAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQqfnm 467
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEATKmsalstdgnkhqmdsnaSAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYA---- 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 468 hvfKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKLGILDLLdEECKMPKGTDDTWAQ------KLYNTHL---NKCALF 538
Cdd:cd14894 565 ---REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASL-EELTILHQSENMNAQqeekrnKLFVRNIydrNSSRLP 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 539 EKPRLSNKA------------FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekaisptsATS 606
Cdd:cd14894 641 EPPRVLSNAkrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNE---------SSQ 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 607 SGRTPLT-RTLSKPTKGRPGQTakehKKTVGhQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACG 685
Cdd:cd14894 712 LGWSPNTnRSMLGSAESRLSGT----KSFVG-QFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQR 786
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1542868643 686 V---LETIRISAAGFPS-RWTYQEFFSRYRVLMKQKDVLSDRKQTCKNVLEKL 734
Cdd:cd14894 787 LirqMEICRNSSSSYSAiDISKSTLLTRYGSLLREPYILDDVAGDNSNLMNWL 839
|
|
| Myo5p-like_CBD_fungal |
cd15474 |
cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin ... |
1485-1829 |
4.29e-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: 120.60 E-value: 4.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1485 LVKNLILELKPRGVAVN----LIPGLPAYILFMCVRHADYLNDDQKVRSL--LTSTINSIKKVLKKRgDDFETVSFWLSN 1558
Cdd:cd15474 11 LKSVEVLELKDISDEVSgdnlLFLGHVNFLIYSQMWKSLLELLTQSERFLshVLSYIASIVDSLPKK-ETIPDGAFWLAN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1559 TCRFLHCL--KQYSGEEGFMKHNTSRQNEHCLTNFDlaEYRQVLSdlaiQIYQQLVRVLENILQPMIVSGMLEHETIQGV 1636
Cdd:cd15474 90 LHELRSFVvyLLSLIEHSSSDEFSKESEEYWNTLFD--KTLKHLS----NIYSTWIDKLNKHLSPKIEGAVLVLLTSLDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1637 SGvkptgLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAVTLNNLLLRKDMCSWSKGMQ 1716
Cdd:cd15474 164 SE-----LIDLNKEFFNKPKKKMADLITFLNEVYDLLQSFSVQPELLNAIVSSTLQYINVEAFNSLITKRSALSWKRGSQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1717 IRYNVSQLEEWLRDKNLmnSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNeFEERVSV 1796
Cdd:cd15474 239 ISYNVSRLKEWCHQHGL--SDANLQLEPLIQASKLLQLRKDDENDFKIILSVCYALNPAQIQKLLDKYQPAN-YEAPVPK 315
|
330 340 350
....*....|....*....|....*....|....
gi 1542868643 1797 SFIRTI-QMRLRDRKDSPQLLMDAKHIFPVTFPF 1829
Cdd:cd15474 316 EFLNALeKLIKKENLSLPGRKNNSKMEIPESSNF 349
|
|
| fMyo2p_CBD |
cd15480 |
cargo binding domain of fungal myosin 2; Yeast myosin V travels along actin cables, actin ... |
1658-1853 |
6.27e-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: 120.38 E-value: 6.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1658 TLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAVTLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNlMNSG 1737
Cdd:cd15480 167 TMDDILNFFNKVYKSMKSYYIEESVIRQVVTELLKLIGVTAFNDLLMRRNFLSWKRGLQINYNITRLEEWCKSHD-IPEG 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1738 AkETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTpVNEFEERVSVSFIRTIQMRLR--DRKDSPQL 1815
Cdd:cd15480 246 T-LQLEHLMQATKLLQLKKATLEDIEIIYDVCWILTPAQIQKLISQYY-VADYENPISPEILKAVAARVKpeDKSDHLLL 323
|
170 180 190
....*....|....*....|....*....|....*...
gi 1542868643 1816 LMDAKHIFPVTFPFNPSSLALETIqIPASLGLGFISRV 1853
Cdd:cd15480 324 IPLVEEVGPFEDPFPREIAGLEAY-IPAWLNLPHIRRL 360
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
902-1281 |
6.21e-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: 84.34 E-value: 6.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 902 KRELKKLKIEARSVERYKKLHigmeNKIMQLQRKVdeQNKDYKCLMEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKIA 981
Cdd:TIGR02168 199 ERQLKSLERQAEKAERYKELK----AELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 982 TGRVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQekevlnhriVEQAKEMTETMEKKLV 1061
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE---------LESKLDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1062 EETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmvnvpkpghKRTDSTHSSNESEYTFSSEI----AETEDIP 1137
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLE----------TLRSKVAQLELQIASLNNEIerleARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1138 SRTEEPSEKKVPLDMSL----FLKLQKRVTELEQEKQVMQDELDRKEEQvlrskaKEEERPQIRGAELEYESLKRQELES 1213
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLeeaeLKELQAELEELEEELEELQEELERLEEA------LEELREELEEAEQALDAAERELAQL 487
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1542868643 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 ... |
1507-1786 |
1.30e-15 |
|
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: 80.05 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1507 PAYILFMCVRH---ADYLNDD------QKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNTCRFLHCLKQysgeegfmk 1577
Cdd:cd15471 25 PAYTLYLAARYrlsTHYRPELtpteraHKLTAFLNKIASLIQQVIQEQRNIAGALAFWMANASELLNFLKQ--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1578 hntsrqnEHCLTNFDLaEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSGVKPTglrkrtssiadegTY 1657
Cdd:cd15471 96 -------DRDLSAFSV-QAQDVLAEAVQSAFSYLVRCLQEELERSLPAFLDSLVSLDDEPAIGDV-------------LH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1658 TLDSILRQLNsfhsvmcQHGMDPELIKQVVKQMFYIVGAVTLNNLLLRKD--MCSWSKGMQIRYNVSQLEEWLrDKNLMN 1735
Cdd:cd15471 155 TLSSAMRLLR-------RCRVNAALTIQLFSQLFHFINAWLFNSLVSNPDsgLCTRYWGKRLRQRLAHVEAWA-ERQGLE 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1542868643 1736 SGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTP 1786
Cdd:cd15471 227 LAADCHLDRIVQAANLLTAPKYSAEDVANLSSTCFKLNSLQLRALLSHYQP 277
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
902-1286 |
7.45e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.28 E-value: 7.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 902 KRELKKLKIEARSVERYKKLHIGMEnkimqlQRKVDEQNKDYKCLMEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKIA 981
Cdd:COG1196 199 ERQLEPLERQAEKAERYRELKEELK------ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 982 TGRVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVSNLKEentlLKQEKEVLNHRIVEQAKEMTETMEKKLV 1061
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE----LEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1062 EETK--QLELDLNDERLRYQNLLNEFSRLEERYDDLKEEmtlmvnvpkpghkrtdstHSSNESEytfSSEIAETEDIPSR 1139
Cdd:COG1196 349 AEEEleEAEAELAEAEEALLEAEAELAEAEEELEELAEE------------------LLEALRA---AAELAAQLEELEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1140 TEEpsekkvpldmslflKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEErpqiRGAELEYESLKRQELESENKKLK 1219
Cdd:COG1196 408 AEE--------------ALLERLERLEEELEELEEALAELEEEEEEEEEALEE----AAEEEAELEEEEEALLELLAELL 469
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1542868643 1220 NELNELRKALSEKSAPEVTApgAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKDDK 1286
Cdd:COG1196 470 EEAALLEAALAELLEELAEA--AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEA 534
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
957-1231 |
2.33e-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: 75.86 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 957 YNSETEKLRSDLERLQLSEEEAKIATGRVLS----LQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQL---VSNLKE 1029
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKeleeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLeerIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1030 ENTLLKQEKEVLNHRIVEQAKEMTETMEK--KLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMtlmvnvpk 1107
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEieELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL-------- 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1108 pghkrtdsthssNESEYTFSSEIAETEDIPSRTEEPSEKkvpldmslFLKLQKRVTELEQEKQVMQDELDRKEEQvlrsK 1187
Cdd:TIGR02168 827 ------------ESLERRIAATERRLEDLEEQIEELSED--------IESLAAEIEELEELIEELESELEALLNE----R 882
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1542868643 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 |
4.40e-13 |
|
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: 75.10 E-value: 4.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 902 KRELKKLKIEARSVERYKKLHI---------------GMENKIMQLQRKVDEQNKDykclMEKLTNLEGIYNSETEKLRS 966
Cdd:TIGR02169 197 RQQLERLRREREKAERYQALLKekreyegyellkekeALERQKEAIERQLASLEEE----LEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 967 DLErlQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTQSekkSIEEHADRYKQETEQLVsNLKEENTLLKQEKEVLNHRIV 1046
Cdd:TIGR02169 273 LLE--ELNKKIKDLGEEEQLRVKEKIGELEAEIASLER---SIAEKERELEDAEERLA-KLEAEIDKLLAEIEELEREIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1047 EQAKEMTETME--KKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMtlmvnvpkpghkrtdsthssNESEY 1124
Cdd:TIGR02169 347 EERKRRDKLTEeyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI--------------------NELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1125 TFSSEIAETEDIPSRTEEpsekkvpLDMSLFLKLQKrVTELEQEKQVMQDELDRKEEQVLRSKA-KEEERPQIRGAELEY 1203
Cdd:TIGR02169 407 ELDRLQEELQRLSEELAD-------LNAAIAGIEAK-INELEEEKEDKALEIKKQEWKLEQLAAdLSKYEQELYDLKEEY 478
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1542868643 1204 eslkrQELESENKKLKNELNELRKalsEKSAPEVTAPGAPAyrvlmeqltsVSEELDVRKEEVLILRSQLVSQKEAIQ 1281
Cdd:TIGR02169 479 -----DRVEKELSKLQRELAEAEA---QARASEERVRGGRA----------VEEVLKASIQGVHGTVAQLGSVGERYA 538
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
901-1443 |
1.15e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.56 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 901 AKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGiynsETEKLRSDLERL--------Q 972
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELRE----ELEKLEKEVKELeelkeeieE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 973 LSEEEAKIaTGRVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQ-----ETEQLVSNLKEENTLLKQEKEVLNHRIVE 1047
Cdd:PRK03918 243 LEKELESL-EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaEEYIKLSEFYEEYLDELREIEKRLSRLEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1048 QAKEMtetmeKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVNVPKpghkrtdstHSSNESEYTFS 1127
Cdd:PRK03918 322 EINGI-----EERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELER---------LKKRLTGLTPE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1128 SEIAETEDIPSRTEEPSEKkvpldmslFLKLQKRVTELEQEKQVMQDELDRKEEQ-----VLRSKAKEEERPQIRG---A 1199
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEE--------ISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEeytA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1200 ELEYESLKRQELESENKKLKNELNELRKALSEKsaPEVTapgapAYRVLMEQLTSVSEELDVR---------------KE 1264
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKE--SELI-----KLKELAEQLKELEEKLKKYnleelekkaeeyeklKE 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1265 EVLILRSQLVSQKEAIQPKDD-KNTMTDSTILLEDVQKMKDKGEIAQAYIGLkETNRLLESQLQSQKRSH---------E 1334
Cdd:PRK03918 533 KLIKLKGEIKSLKKELEKLEElKKKLAELEKKLDELEEELAELLKELEELGF-ESVEELEERLKELEPFYneylelkdaE 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1335 NEAEALRGEIQSLKEENNRQQQLLAQNlqlppEARIEaSLQHEITRLtnENLYFEELYADDPKKYQSYRiSLYKRMIDLM 1414
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAET-----EKRLE-ELRKELEEL--EKKYSEEEYEELREEYLELS-RELAGLRAEL 682
|
570 580 590
....*....|....*....|....*....|...
gi 1542868643 1415 EQLEKQ----DKTVRKLKKQLKVFAKKIGELEV 1443
Cdd:PRK03918 683 EELEKRreeiKKTLEKLKEELEEREKAKKELEK 715
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
942-1442 |
3.57e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.55 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 942 DYKCLMEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKqETE 1021
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-ELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1022 QLVSNLKEENTLLKQEKEVLNHRIVEqakemTETMEKKLVEETKQLEldlndERLRYqnlLNEFSRLEERYDDLKEEMTL 1101
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRE-----LEERIEELKKEIEELE-----EKVKE---LKELKEKAEEYIKLSEFYEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1102 MVNVPKPGHKRTDSTHSSNESeytFSSEIAETEDIPSRTEEPSEKKVpldmslflKLQKRVTELEQEKQVMQDELDRKEE 1181
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEING---IEERIKELEEKEERLEELKKKLK--------ELEKRLEELEERHELYEEAKAKKEE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1182 -QVLRSKAKEEERPQIRgAELEYESLKRQELESENKK-------LKNELNELRKALSEKSAPEVTAP--GAP-------- 1243
Cdd:PRK03918 374 lERLKKRLTGLTPEKLE-KELEELEKAKEEIEEEISKitarigeLKKEIKELKKAIEELKKAKGKCPvcGRElteehrke 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1244 ---AYRVLMEQLTSVSEELDVRKEEVLI----LRSQLVSQKEAIQPKddknTMTDSTILLEDVQKMKDKGEIAQA---YI 1313
Cdd:PRK03918 453 lleEYTAELKRIEKELKEIEEKERKLRKelreLEKVLKKESELIKLK----ELAEQLKELEEKLKKYNLEELEKKaeeYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1314 GLKETNRLLESQLQSQKRS------HENEAEALRGEIQSLKEEnnrqqqllaqnlqlppeariEASLQHEITRLTNENLY 1387
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKElekleeLKKKLAELEKKLDELEEE--------------------LAELLKELEELGFESVE 588
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1542868643 1388 FEELYADDPKKYQSYRISLYKRMIDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1442
Cdd:PRK03918 589 ELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
898-1436 |
5.14e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.17 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 898 RMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGIYnSETEKLRSDLE--RLQLSE 975
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV-KELEELKEEIEelEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 976 EEAKIAT--GRVLSLQEEIAKLRK---DLEQTQSEKKSIEEHADRY------KQETEQLVSNLKEENTLLKQEKEVLNHR 1044
Cdd:PRK03918 250 LEGSKRKleEKIRELEERIEELKKeieELEEKVKELKELKEKAEEYiklsefYEEYLDELREIEKRLSRLEEEINGIEER 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1045 IVEqakemTETMEKKLVEETKQLEldlnderlryqNLLNEFSRLEERYDDLKEEMTLMVNVPKpghkrtdstHSSNESEY 1124
Cdd:PRK03918 330 IKE-----LEEKEERLEELKKKLK-----------ELEKRLEELEERHELYEEAKAKKEELER---------LKKRLTGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1125 TFSSEIAETEDIPSRTEEPSEKkvpldmslFLKLQKRVTELEQEKQVMQDELDRKEEQ-----VLRSKAKEEERPQIRG- 1198
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEE--------ISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEe 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1199 --AELEYESLKRQELESENKKLKNELNELRKALSEKsaPEVTApgapaYRVLMEQLTSVSEELDVR-------------- 1262
Cdd:PRK03918 457 ytAELKRIEKELKEIEEKERKLRKELRELEKVLKKE--SELIK-----LKELAEQLKELEEKLKKYnleelekkaeeyek 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1263 -KEEVLILRSQLVSQKEAIQPKDD-KNTMTDSTILLEDVQ--------KMKDKG---------------EIAQAYIGLKE 1317
Cdd:PRK03918 530 lKEKLIKLKGEIKSLKKELEKLEElKKKLAELEKKLDELEeelaellkELEELGfesveeleerlkelePFYNEYLELKD 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1318 TNRLLESQLQSQKRShENEAEALRGEIQSLKEENNRQqqllaqnlqlppEARIEASL----QHEITRLTNENLYFEELYA 1393
Cdd:PRK03918 610 AEKELEREEKELKKL-EEELDKAFEELAETEKRLEEL------------RKELEELEkkysEEEYEELREEYLELSRELA 676
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1542868643 1394 ---DDPKKYQSYRISLYKRMIDLMEQLEKQDKTVRKLKKQLKVFAK 1436
Cdd:PRK03918 677 glrAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALER 722
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
957-1350 |
8.18e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.37 E-value: 8.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 957 YNSETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTQSEKksiEEHADRYKQETEQLvSNLKEENTLLKQ 1036
Cdd:PRK02224 225 YEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERER---EELAEEVRDLRERL-EELEEERDDLLA 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1037 EKEV--LNHRIVEQAKemtETMEKKLVEetkqLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmvnvpkpgHKRTD 1114
Cdd:PRK02224 301 EAGLddADAEAVEARR---EELEDRDEE----LRDRLEECRVAAQAHNEEAESLREDADDLEERAE---------ELREE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1115 SThssneseyTFSSEIAET-EDIPSRTEEPSEkkvpldmslflkLQKRVTELEQEKQVMQDELDRKEEqvlRSKAKEEER 1193
Cdd:PRK02224 365 AA--------ELESELEEArEAVEDRREEIEE------------LEEEIEELRERFGDAPVDLGNAED---FLEELREER 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1194 PQIRGaeleyeslKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVlmeqltsvsEELDVRKEEVLILRSQL 1273
Cdd:PRK02224 422 DELRE--------REAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHV---------ETIEEDRERVEELEAEL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1274 VSQKEAIQPKDDKNTMTDSTILLED-VQKMKDKGEIAQAYIGLKET----NRLLESQLQSQKRSHENEAEALRGEIQSLK 1348
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVEAEDrIERLEERREDLEELIAERREtieeKRERAEELRERAAELEAEAEEKREAAAEAE 564
|
..
gi 1542868643 1349 EE 1350
Cdd:PRK02224 565 EE 566
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
902-1209 |
9.34e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 9.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 902 KRELKKLKIEARS-VERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLE-GIYNSETE--KLRSDLERLQ----- 972
Cdd:TIGR02169 697 LRRIENRLDELSQeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEqEIENVKSElkELEARIEELEedlhk 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 973 ----LSEEEAKIATGRVLSLQEEIAKLRK----------DLEQTQSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEK 1038
Cdd:TIGR02169 777 leeaLNDLEARLSHSRIPEIQAELSKLEEevsriearlrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1039 EVLNHRiveqaKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEmtlmVNVPKPGHKRTDSTHS 1118
Cdd:TIGR02169 857 ENLNGK-----KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ----IEKKRKRLSELKAKLE 927
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1119 sneseyTFSSEIAETEDIPSRTEEPSEKKVPLDmslflKLQKRVTELEQEKQVMQ-------DELDRKEEQVLRSKAK-- 1189
Cdd:TIGR02169 928 ------ALEEELSEIEDPKGEDEEIPEEELSLE-----DVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKra 996
|
330 340
....*....|....*....|..
gi 1542868643 1190 --EEERPQIRGAELEYESLKRQ 1209
Cdd:TIGR02169 997 klEEERKAILERIEEYEKKKRE 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
904-1305 |
2.28e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 904 ELKKLKIEARSVERYKKlHIGMENKIMQLQRKVDEQNK--DYKCLMEKLTNLEGIYNSETEKLRSDleRLQLSEEEAKIA 981
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKK-KAEEKKKADEAKKKAEEAKKadEAKKKAEEAKKAEEAKKKAEEAKKAD--EAKKKAEEAKKA 1485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 982 TgRVLSLQEEIAKLRKDLEQTQSEKKSIEE--HADRYKQETEQLVSNLKEENTLLKQEKEVLNHRIVEQAKEMTETMEKK 1059
Cdd:PTZ00121 1486 D-EAKKKAEEAKKKADEAKKAAEAKKKADEakKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK 1564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1060 LVEETKQLELDLNDERLRYQNLLN-EFSRLEERYDDLKEEmtlmvnvpkpghKRTDSTHSSNESEYTFSSEiaetediPS 1138
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEE------------KKMKAEEAKKAEEAKIKAE-------EL 1625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1139 RTEEPSEKKVPLDMSLFLKLQKRVTEL---EQEKQVMQDELDRKEEQVLRS-----KAKEEERPQIRGAELEYESLKRQE 1210
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELkkaEEENKIKAAEEAKKAEEDKKKaeeakKAEEDEKKAAEALKKEAEEAKKAE 1705
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1211 lesENKKLKNElnELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEvlilRSQLVSQKEAIQPKDDKNTMT 1290
Cdd:PTZ00121 1706 ---ELKKKEAE--EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE----KKKIAHLKKEEEKKAEEIRKE 1776
|
410
....*....|....*
gi 1542868643 1291 DSTILLEDVQKMKDK 1305
Cdd:PTZ00121 1777 KEAVIEEELDEEDEK 1791
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
926-1442 |
5.89e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 64.27 E-value: 5.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 926 ENKIMQLQRKVDEQNKDYKCLMEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTQSE 1005
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1006 KKSIEEHADRYKQETEQLvSNLKEENTLLKQEKEVLNHRIVEQAKEMTETMEK--KLVEETKQLELDLNDERLRYQNLLN 1083
Cdd:TIGR04523 203 LSNLKKKIQKNKSLESQI-SELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQlnQLKDEQNKIKKQLSEKQKELEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1084 EFSRLEERYDDLKEEMTLMVNVPKPG-HKRTDSTHSSNESEYT-FSSEIAETEDIPSRTEEPSEKkvpldmslflkLQKR 1161
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQKEQDwNKELKSELKNQEKKLEeIQNQISQNNKIISQLNEQISQ-----------LKKE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1162 VTELEQEKQVMQDELDRKEEQV-----------------------LRSKAKEEER------PQIRGAELEYESLKR--QE 1210
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIeklkkenqsykqeiknlesqindLESKIQNQEKlnqqkdEQIKKLQQEKELLEKeiER 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1211 LESENKKLKNELNELRKALSEKSApevtapgapAYRVLMEQLTSVSEELDVRKEEVLILRSQL-VSQKEAIQPKDDKNTM 1289
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKEL---------IIKNLDNTRESLETQLKVLSRSINKIKQNLeQKQKELKSKEKELKKL 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1290 TDSTILLEdvQKMKD-KGEIAQayigLKETnrllESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQlppEA 1368
Cdd:TIGR04523 502 NEEKKELE--EKVKDlTKKISS----LKEK----IEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEK---NK 568
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1542868643 1369 RIEaSLQHEITRLTNENLYFEELYaddpKKYQsyrislyKRMIDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1442
Cdd:TIGR04523 569 EIE-ELKQTQKSLKKKQEEKQELI----DQKE-------KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
902-1493 |
7.41e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 64.22 E-value: 7.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 902 KRELKKLKIEARSVERYKKLHigMENKIMQLQRKVDEQNKDYKclmEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKia 981
Cdd:pfam02463 196 KLQELKLKEQAKKALEYYQLK--EKLELEEEYLLYLDYLKLNE---ERIDLLQELLRDEQEEIESSKQEIEKEEEKLA-- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 982 tgRVLSLQEEIAKLRKdleqtqsekksieehadryKQETEQLVSNLKEENTLLKQEKEVLNHRIVEQAKEMTETMEKKLV 1061
Cdd:pfam02463 269 --QVLKENKEEEKEKK-------------------LQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1062 EETKQLELdlndERLRYQNLLNEFSRLEERYDDLKEEMTLmvnvpkpghKRTDSTHSSNESEYTFSSEIAETEDIPSRTE 1141
Cdd:pfam02463 328 KELKKEKE----EIEELEKELKELEIKREAEEEEEEELEK---------LQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1142 EpsekkvplDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQELESENKKLKNE 1221
Cdd:pfam02463 395 E--------ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELE 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1222 LNELRKALseksapevtapgaPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPkddKNTMTDSTILLEDVQK 1301
Cdd:pfam02463 467 LKKSEDLL-------------KETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA---LIKDGVGGRIISAHGR 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1302 MKDKGEIAQAYIGLKETNRLLES----QLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQHE 1377
Cdd:pfam02463 531 LGDLGVAVENYKVAISTAVIVEVsataDEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDK 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1378 ITRLTNENLYFEELYADDPK-KYQSYRISLYKRMIDL---MEQLEKQDKTVRKLKKQLKVFAKKIGELEVGQMENISPGQ 1453
Cdd:pfam02463 611 ATLEADEDDKRAKVVEGILKdTELTKLKESAKAKESGlrkGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1542868643 1454 IIDEPIRPVNIPRKEKDFQGMLEYKKEDEQKLVKNLILEL 1493
Cdd:pfam02463 691 KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEA 730
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
957-1350 |
1.64e-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: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 957 YNSETEKLRSDLERLQLSEEEAKIAtgrvlslqeeIAKLRKDLEQTQSEKksieEHADRY------KQETEQLVSnLKEE 1030
Cdd:TIGR02169 168 FDRKKEKALEELEEVEENIERLDLI----------IDEKRQQLERLRRER----EKAERYqallkeKREYEGYEL-LKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1031 NTLLKQEKEVLNHRiveqakemtETMEKKLVEETKQLElDLNDERLRYQNLLNEfsrLEERYDDLKEEMTLMVNvpkpgh 1110
Cdd:TIGR02169 233 EALERQKEAIERQL---------ASLEEELEKLTEEIS-ELEKRLEEIEQLLEE---LNKKIKDLGEEEQLRVK------ 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1111 KRTDSTHSsneseytfssEIAETEDIPSRTEEPSEKkvpldmslfLKLQKRVTELEQEKQVMQ-DELDRKEEQVLRSKAK 1189
Cdd:TIGR02169 294 EKIGELEA----------EIASLERSIAEKERELED---------AEERLAKLEAEIDKLLAEiEELEREIEEERKRRDK 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1190 EEERPQIRGAELEYESLKRQELESENKKLKNELNELRKALSEksapevtapgapayrvLMEQLTSVSEELDVRKEEVLIL 1269
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK----------------LKREINELKRELDRLQEELQRL 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1270 RSQLVSQKEAIQPKDDKNTMTDSTilLEDVQKmkdkgEIAQAYIGLKETNRLLESqLQSQKRSHENEAEALRGEIQSLKE 1349
Cdd:TIGR02169 419 SEELADLNAAIAGIEAKINELEEE--KEDKAL-----EIKKQEWKLEQLAADLSK-YEQELYDLKEEYDRVEKELSKLQR 490
|
.
gi 1542868643 1350 E 1350
Cdd:TIGR02169 491 E 491
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
900-1232 |
1.64e-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: 63.07 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 900 MAKRELKKLKIEARSVERYKKLHIGMEN-KIMQLQRKVDEQNKDYKCLMEKLTNLEGIYNSETEKLRSDLERLQLSEEEA 978
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEELKKLKLEAEElLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 979 KiatgrvlSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVSN--LKEENTLLKQEKEVLNHRIVEQAKEMTETM 1056
Cdd:pfam02463 774 K-------ELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAelLEEEQLLIEQEEKIKEEELEELALELKEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1057 EKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmvnvpKPGHKRTDSTHSSNESEYTFSSEIAETEDI 1136
Cdd:pfam02463 847 KLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELES------KEEKEKEEKKELEEESQKLNLLEEKENEIE 920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1137 PSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQvlrsKAKEEERPQIRGAELEYESLK--RQELESE 1214
Cdd:pfam02463 921 ERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLL----LAKEELGKVNLMAIEEFEEKEerYNKDELE 996
|
330
....*....|....*...
gi 1542868643 1215 NKKLKNELNELRKALSEK 1232
Cdd:pfam02463 997 KERLEEEKKKLIRAIIEE 1014
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
897-1484 |
3.28e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.47 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 897 RRMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGIYNSETEKlrsDLERLQLSEE 976
Cdd:PTZ00121 1224 KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKK---KADEAKKAEE 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 977 EAKIatgrvlslqEEIAKLRKDLEQTQSEKKSIEEH---ADRYKQETEQlvsnlKEENTLLKQEKEVLNHRIVEQAKEMT 1053
Cdd:PTZ00121 1301 KKKA---------DEAKKKAEEAKKADEAKKKAEEAkkkADAAKKKAEE-----AKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1054 ETMEKKLVEETKQLEL--DLNDERLRYQNLLNEFSRLEERYDDLK---EEMTLMVNVPKPGHKRTDSTHSSNESEYTFSS 1128
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAakKKAEEKKKADEAKKKAEEDKKKADELKkaaAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA 1446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1129 EIAETEDIPSRTEEPSEKKVpldmslflKLQKRVTELEQ--EKQVMQDELDRKEEQVLR----SKAKEEERPQIRGAELE 1202
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKA--------EEAKKADEAKKkaEEAKKADEAKKKAEEAKKkadeAKKAAEAKKKADEAKKA 1518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1203 YESLKRQELESENKKLKNElnELRKALSEKSAPEVTAPgapayrvlmEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQP 1282
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKAD--EAKKAEEKKKADELKKA---------EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK 1587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1283 KDDKNTMTDSTILLEDVQKMK-------DKGEIAQAYIGLKETNRLLESQLQSQKRSHENEAEALRGEiqslKEENNRQQ 1355
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKaeeakkaEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA----EEENKIKA 1663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1356 QLLAQNLQLPPEARIEASLQHEITRLTNENLYFEELYADDPKKYQSYRISLYKRMIDLMEQLEKQDKTVRKLKKQLKVFA 1435
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK 1743
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1542868643 1436 KKIGELEVGQMENISPGQIIDEPIRPVNIPRKEKDFQGMLEYKKEDEQK 1484
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKR 1792
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
845-1339 |
4.23e-09 |
|
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: 61.91 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 845 QSYLRGYLARNRYHKILREHKAVIIQkwvrgwLARTC-YRRSIHAIIYLQCCFRRMMAKRE-LKKLKIEARSVERYKKLH 922
Cdd:TIGR00618 419 FRDLQGQLAHAKKQQELQQRYAELCA------AAITCtAQCEKLEKIHLQESAQSLKEREQqLQTKEQIHLQETRKKAVV 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 923 IGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGiynseteklrsDLERLQLSEEEAKiatgrvlSLQEEIAKLRKDLEQT 1002
Cdd:TIGR00618 493 LARLLELQEEPCPLCGSCIHPNPARQDIDNPGP-----------LTRRMQRGEQTYA-------QLETSEEDVYHQLTSE 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1003 QSEKKSIEEHADRYKQETE---QLVSNLKEENTLLKQEKEVLNHRIVEQAKEmtetmEKKLVEETKQLELDLNDERLRYQ 1079
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSiltQCDNRSKEDIPNLQNITVRLQDLTEKLSEA-----EDMLACEQHALLRKLQPEQDLQD 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1080 NLLNEFSRLEERYDDLKEEMTLMVNVPKpghkrtdsthsSNESEYTFSSEIAETEDIPSRTEEPSEKKvpldmSLFLKLQ 1159
Cdd:TIGR00618 630 VRLHLQQCSQELALKLTALHALQLTLTQ-----------ERVREHALSIRVLPKELLASRQLALQKMQ-----SEKEQLT 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1160 KRVTELEQekqvmQDELDRKEEQVLrskakEEERPQIRGAELEYESLKrQELESENKKLKNELNELRKALSEK-----SA 1234
Cdd:TIGR00618 694 YWKEMLAQ-----CQTLLRELETHI-----EEYDREFNEIENASSSLG-SDLAAREDALNQSLKELMHQARTVlkartEA 762
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1235 PEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKDDKN----TMTDSTILLEDVQ-------KMK 1303
Cdd:TIGR00618 763 HFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDedilNLQCETLVQEEEQflsrleeKSA 842
|
490 500 510
....*....|....*....|....*....|....*.
gi 1542868643 1304 DKGEIAQAYIGLKETNRLLESQLQSQKRSHENEAEA 1339
Cdd:TIGR00618 843 TLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
917-1442 |
5.06e-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: 61.19 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 917 RYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLR 996
Cdd:TIGR04523 23 GYKNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 997 KDLEQTQSEKKSieehadrykqETEQLVSNLKEENTLLKQEKEVlnhriveqakemtETMEKKLVEETKQLELDLNDERL 1076
Cdd:TIGR04523 103 SDLSKINSEIKN----------DKEQKNKLEVELNKLEKQKKEN-------------KKNIDKFLTEIKKKEKELEKLNN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1077 RYQNLLNEFSRLEERYDDLKEEMTlmvnvpKPGHKRTDSTHSSNESEYTFSSEIAETEDIPSRTEEPSEKKvpldmSLFL 1156
Cdd:TIGR04523 160 KYNDLKKQKEELENELNLLEKEKL------NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELK-----KQNN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1157 KLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEE---RPQIRGAELEYESLKRQELESENKKLKNELNELRKalsEKS 1233
Cdd:TIGR04523 229 QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKikkQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN---QKE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1234 ApevtapgapayrvlmEQLTSVSEELDVRKEEVLILRSQLVSQKEAI-----QPKDDKNTMTDSTI--------LLEDVQ 1300
Cdd:TIGR04523 306 Q---------------DWNKELKSELKNQEKKLEEIQNQISQNNKIIsqlneQISQLKKELTNSESensekqreLEEKQN 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1301 KMKDKGEIAQAYiglKETNRLLESQ---LQSQKRSHENEAEALRGEIQSLKEENNRQqqllaqnlqlppEARIE------ 1371
Cdd:TIGR04523 371 EIEKLKKENQSY---KQEIKNLESQindLESKIQNQEKLNQQKDEQIKKLQQEKELL------------EKEIErlketi 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1542868643 1372 ASLQHEITRLTNENLYFEELYA--DDPKKYQSYRISLYKRMIDLMEQ-LEKQDKTVRKLKKQLKVFAKKIGELE 1442
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSVKELIIKnlDNTRESLETQLKVLSRSINKIKQnLEQKQKELKSKEKELKKLNEEKKELE 509
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
903-1334 |
6.40e-09 |
|
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: 60.89 E-value: 6.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 903 RELKKLKIE-ARSVERYKKLHIGME---NKIMQL----QRKVDEQNKDYKCLMEKLTNLEGIYNSETEKLRSDLERLQLS 974
Cdd:pfam05483 296 KELEDIKMSlQRSMSTQKALEEDLQiatKTICQLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 975 EEEAKIATgrvlslqeeiaklrKDLEQTQSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEvlnhriVEQAKEMTE 1054
Cdd:pfam05483 376 EDQLKIIT--------------MELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQ------FEKIAEELK 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1055 TMEKKLVEETKQLELDLNDERLRyqnlLNEFSRLEERYddLKEEMTLMVNVPKPGHKRTDSTHSSNESEYTFSSEIAETE 1134
Cdd:pfam05483 436 GKEQELIFLLQAREKEIHDLEIQ----LTAIKTSEEHY--LKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEAS 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1135 DIPSRTEEPSE------KKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQirgaELEYESLKR 1208
Cdd:pfam05483 510 DMTLELKKHQEdiinckKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENAR----SIEYEVLKK 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1209 qelESENKKLKNELNELRKALSEKSapEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKDD--K 1286
Cdd:pfam05483 586 ---EKQMKILENKCNNLKKQIENKN--KNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDnyQ 660
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1542868643 1287 NTMTDSTI----LLEDVQKMK---DKGEIAQAYIGLKETNRLLESQLQSQKRSHE 1334
Cdd:pfam05483 661 KEIEDKKIseekLLEEVEKAKaiaDEAVKLQKEIDKRCQHKIAEMVALMEKHKHQ 715
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
901-1267 |
1.22e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 901 AKRELKKLKIEARSVErykKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKI 980
Cdd:COG1196 251 LEAELEELEAELAELE---AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 981 ATGRVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVSNLKEentllkQEKEVLNHRIVEQAKEMTETMEKKL 1060
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE------AEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1061 VEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEmtlmvnvpkpghkrtdsthsSNESEYTFSSEIAETEdipsrt 1140
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEE--------------------EEEALEEAAEEEAELE------ 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1141 eepsekkvpldmSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEE-ERPQIRGAELEYESLKRQELESENKKLK 1219
Cdd:COG1196 456 ------------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLlLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1542868643 1220 NELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVL 1267
Cdd:COG1196 524 GAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA 571
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
896-1258 |
2.10e-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: 59.37 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 896 FRRMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGIynsETEKLRSDLERLQLSE 975
Cdd:pfam17380 293 FEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI---RQEERKRELERIRQEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 976 EEAKIATGRVL-----SLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEVLNHrivEQAK 1050
Cdd:pfam17380 370 IAMEISRMRELerlqmERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE---ERAR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1051 EMTETMEKKLvEETKQLELDLNDERLRYQNLLnEFSRlEERYDDLKEEMTLMVnVPKPGHKRTDSTHSSNESEYTFSSEI 1130
Cdd:pfam17380 447 EMERVRLEEQ-ERQQQVERLRQQEEERKRKKL-ELEK-EKRDRKRAEEQRRKI-LEKELEERKQAMIEEERKRKLLEKEM 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1131 AETEDipsrteepsekkvpldmSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKakeEERPQIRGAELEYEsLKRQE 1210
Cdd:pfam17380 523 EERQK-----------------AIYEEERRREAEEERRKQQEMEERRRIQEQMRKAT---EERSRLEAMERERE-MMRQI 581
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1542868643 1211 LESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEE 1258
Cdd:pfam17380 582 VESEKARAEYEATTPITTIKPIYRPRISEYQPPDVESHMIRFTTQSPE 629
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
901-1098 |
3.82e-08 |
|
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: 58.54 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 901 AKRELKKL-KIEARSVERYKKLhigmENKIMQLQRKVDEQNKDYKCLMEKLTNLEgiynSETEKLRSDLERLqlsEEEAK 979
Cdd:TIGR02169 313 KERELEDAeERLAKLEAEIDKL----LAEIEELEREIEEERKRRDKLTEEYAELK----EELEDLRAELEEV---DKEFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 980 IATGRVLSLQEEiaklrkdLEQTQSEKKSIEEHADRYKQETEQLVSNLKEentlLKQEKEVLNHRIVEQAKEMTETME-- 1057
Cdd:TIGR02169 382 ETRDELKDYREK-------LEKLKREINELKRELDRLQEELQRLSEELAD----LNAAIAGIEAKINELEEEKEDKALei 450
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1542868643 1058 KKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEE 1098
Cdd:TIGR02169 451 KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
896-1440 |
4.42e-08 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 58.21 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 896 FRRMMAKRELKKLKIEarsverYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGIYNSETEKLRSDLERLQL-- 973
Cdd:pfam05557 9 ARLSQLQNEKKQMELE------HKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 974 ----------SEEEAKIATGR--VLSLQEEIAKLRK-------DLEQTQSEKKSIEEHADRYK---QETEQLVSNL-KEE 1030
Cdd:pfam05557 83 kylealnkklNEKESQLADARevISCLKNELSELRRqiqraelELQSTNSELEELQERLDLLKakaSEAEQLRQNLeKQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1031 NTLLKQEKEV--LNHRIVEQA--KEMTETMEKKLVEETkqlELDLNDERLRYQN-----------LLNE----FSRLEER 1091
Cdd:pfam05557 163 SSLAEAEQRIkeLEFEIQSQEqdSEIVKNSKSELARIP---ELEKELERLREHNkhlnenienklLLKEevedLKRKLER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1092 YDDLKEEM-TLMVNVPKPGHK-----RTDSTHSSN-ESEYTFSSEIaetEDIPSRTEEPSEKKVPLDMSLfLKLQKRVTE 1164
Cdd:pfam05557 240 EEKYREEAaTLELEKEKLEQElqswvKLAQDTGLNlRSPEDLSRRI---EQLQQREIVLKEENSSLTSSA-RQLEKARRE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1165 LEQEKQVMQDELDrkEEQVLRSKAKE-EERPQIRGAELEYE-SLKRQELESENKKLKNELNELRKALSEKSAPEVTApga 1242
Cdd:pfam05557 316 LEQELAQYLKKIE--DLNKKLKRHKAlVRRLQRRVLLLTKErDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQ--- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1243 pAYRVLMEqltSVSEELDVRKEEVLILRSQLVSQKEAIQPKDDKNTMTDSTILLEDVQKMKDKGEIAQAYIG-LKETNRL 1321
Cdd:pfam05557 391 -KMQAHNE---EMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLELERQrLREQKNE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1322 LESQLQSQ------------------------KRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEAslqhe 1377
Cdd:pfam05557 467 LEMELERRclqgdydpkktkvlhlsmnpaaeaYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMN----- 541
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1542868643 1378 itrltnenlyfeelyaddpkkyqsyrislYKRMIDLMEQLEKQDKTVRKLKkqlKVFAKKIGE 1440
Cdd:pfam05557 542 -----------------------------FKEVLDLRKELESAELKNQRLK---EVFQAKIQE 572
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
900-1281 |
5.19e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 900 MAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGIYN-----SETEKLRSDLERLQLS 974
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 975 EEEAKIATGRVLSLQEEIAKLRKDLEQTQSEkksIEEHADRYKQETEQLVSNLKEENTLLKQEKEVLNHRIvEQAKEMTE 1054
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEE---LEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL-EEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1055 TMEKKLVEETKQLELDLNDERLRYQN-----------LLNEFSRLEERYDDLKEEMTLMVNVPKPGHKRTDSTHSSNESE 1123
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1124 YTFSSEIAETEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERP--QIRGAEL 1201
Cdd:COG4717 304 AEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1202 EYESLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQ 1281
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELE 463
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
901-1099 |
7.59e-08 |
|
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: 57.76 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 901 AKRELKKLKIEARSVERYKKlhiGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGiynsETEKLRSDLERLqlsEEEAKI 980
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLE---SLERRIAATERRLEDLEEQIEELSEDIESLAA----EIEELEELIEEL---ESELEA 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 981 ATGRVLSLQEEIAKLRKDLEQTQSEKKSIEEH---ADRYKQETEQLVSNLKEENTLLKQEKEVLNHRIVEQAK---EMTE 1054
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESKrseLRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSltlEEAE 957
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1542868643 1055 TMEKKLVEETKQLELDLNDERLRYQNL-------LNEFSRLEERYDDLKEEM 1099
Cdd:TIGR02168 958 ALENKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQK 1009
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
963-1350 |
8.81e-08 |
|
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: 57.39 E-value: 8.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 963 KLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTQSE-KKSIEEhadrYKQETEQLVSNLKEENTLLKQEKEVL 1041
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDaSRKIGE----IEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1042 nhRIVEQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLlnEFSRLEERYDDLKEEMtlmvnvpkpghKRTDSTHSSNE 1121
Cdd:TIGR02169 747 --SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EARLSHSRIPEIQAEL-----------SKLEEEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1122 seytfsseiaetedipSRTEEpsekkvpldmslflkLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEErpqiRGAEL 1201
Cdd:TIGR02169 812 ----------------ARLRE---------------IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS----IEKEI 856
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1202 EYESLKRQELESENKKLKNELNELRKALSEKSAPEvtapgapayRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQ 1281
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRDLESRLGDLKKER---------DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1282 PKDDKNTMTDSTIL-----------LEDVQKMKDKgeIAQAYIGLKETN------------RLLEsqLQSQKRSHENEAE 1338
Cdd:TIGR02169 928 ALEEELSEIEDPKGedeeipeeelsLEDVQAELQR--VEEEIRALEPVNmlaiqeyeevlkRLDE--LKEKRAKLEEERK 1003
|
410
....*....|..
gi 1542868643 1339 ALRGEIQSLKEE 1350
Cdd:TIGR02169 1004 AILERIEEYEKK 1015
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
925-1392 |
9.85e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 925 MENKIMQLQRKVDEQNKDYKCLMEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTQS 1004
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1005 EKKSIEEHADRYKQETEQlvsnLKEENTLLKQEKEVLNHRIvEQAKEMTETMEKKLVEetkqLELDLNDERLRYQNLLNE 1084
Cdd:PRK02224 336 AAQAHNEEAESLREDADD----LEERAEELREEAAELESEL-EEAREAVEDRREEIEE----LEEEIEELRERFGDAPVD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1085 FSRLEERYDDLKEEmtlmvnvpkpghkRTDSTHSSNESEYTFSSE---IAETED------------------IPSRTEEP 1143
Cdd:PRK02224 407 LGNAEDFLEELREE-------------RDELREREAELEATLRTArerVEEAEAlleagkcpecgqpvegspHVETIEED 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1144 SEKKVPLDMSL------FLKLQKRVTELEQEKQVmQDELDRKEEQVLRSkakeEERPQIRGAELEYESLKRQELESENKK 1217
Cdd:PRK02224 474 RERVEELEAELedleeeVEEVEERLERAEDLVEA-EDRIERLEERREDL----EELIAERRETIEEKRERAEELRERAAE 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1218 LKNELNELRKALSEksAPEVTAPGAPAYRVLMEQLTSVSEELDV--RKEEVLILRSQLVSQKEAIQPK-DDKNTMTDsti 1294
Cdd:PRK02224 549 LEAEAEEKREAAAE--AEEEAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEIERLREKrEALAELND--- 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1295 llEDVQKMKDKGEIAQAYIGLKETNRLleSQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNlqlppEARIE--A 1372
Cdd:PRK02224 624 --ERRERLAEKRERKRELEAEFDEARI--EEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAV-----ENELEelE 694
|
490 500
....*....|....*....|
gi 1542868643 1373 SLQHEITRLTNENLYFEELY 1392
Cdd:PRK02224 695 ELRERREALENRVEALEALY 714
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
902-1280 |
1.21e-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: 57.05 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 902 KRELKKLKIEarsVERYKKLHIGMENKIM-QLQRKVDE-QNKDYKclMEKLTNLEGIYNSETEKLRSDLERLQLS----E 975
Cdd:pfam15921 418 RRELDDRNME---VQRLEALLKAMKSECQgQMERQMAAiQGKNES--LEKVSSLTAQLESTKEMLRKVVEELTAKkmtlE 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 976 EEAKIATGRVLSLQE----------EIAKLRK--DLE-QTQSEKKSIEEHADRYKQETEQLVSNLKEENT---LLKQEKE 1039
Cdd:pfam15921 493 SSERTVSDLTASLQEkeraieatnaEITKLRSrvDLKlQELQHLKNEGDHLRNVQTECEALKLQMAEKDKvieILRQQIE 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1040 VLNHRIVEQAKemteTMEKKLVEETkQLELDLNDERLRYQNLL-------NEFSRLEERYDDLKEEMTLMVNVpkpGHKR 1112
Cdd:pfam15921 573 NMTQLVGQHGR----TAGAMQVEKA-QLEKEINDRRLELQEFKilkdkkdAKIRELEARVSDLELEKVKLVNA---GSER 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1113 TDSTHSSNESEYTFSSEIAETE-DIPSRTEE----------PSEKKVPLDMSLFLKLQKRVTELEQEKQVMQ--DELDRK 1179
Cdd:pfam15921 645 LRAVKDIKQERDQLLNEVKTSRnELNSLSEDyevlkrnfrnKSEEMETTTNKLKMQLKSAQSELEQTRNTLKsmEGSDGH 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1180 EEQVLRSKAKE--EERPQIRGAELEYESLkrQELESENKKLKNELNELRKALSeksapevtapgapayrvlmEQLTSVSE 1257
Cdd:pfam15921 725 AMKVAMGMQKQitAKRGQIDALQSKIQFL--EEAMTNANKEKHFLKEEKNKLS-------------------QELSTVAT 783
|
410 420
....*....|....*....|...
gi 1542868643 1258 ELDVRKEEVLILRSQLVSQKEAI 1280
Cdd:pfam15921 784 EKNKMAGELEVLRSQERRLKEKV 806
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
928-1259 |
1.27e-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: 57.00 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 928 KIMQLQRKVDEQNKDYKCLMEKLTNLEGIYNSETEKLrSDLERlQLSEEEAKIAtgrvlSLQEEIAKLRKDLEQTQSEKK 1007
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL-SDASR-KIGEIEKEIE-----QLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1008 SIEEHADRYKQETEQLVSNLKEENTLLKQEKEVLN--------HRIVEQAKEMTETME--KKLVEETKQLELDLNDERLR 1077
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNdlearlshSRIPEIQAELSKLEEevSRIEARLREIEQKLNRLTLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1078 YQNLLNEFSRLEERYDDLKEEMtlmvnvpkpghkrtdsthssNESEYTFSSEIAETEDIPSRTEEpsekkvpldmslflk 1157
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQI--------------------KSIEKEIENLNGKKEELEEELEE--------------- 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1158 LQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEErpqirgAELEYEsLKRQELESENKKLKNELNELRKALSEKSAPEV 1237
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEE------LEAQIE-KKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
330 340
....*....|....*....|..
gi 1542868643 1238 TAPGAPAYRVLMEQLTSVSEEL 1259
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRVEEEI 967
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
902-1226 |
1.74e-07 |
|
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: 56.18 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 902 KRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKdykclmEKLTNLEGIYNSETEKLRSDLERL--QLSEEEAK 979
Cdd:TIGR04523 263 NKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN------QKEQDWNKELKSELKNQEKKLEEIqnQISQNNKI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 980 IAtgrvlSLQEEIAKLRKD--------------LEQTQSEKKSIEEHADRYKQETEQLVSNLKE-ENTLLKQEKEvlnhr 1044
Cdd:TIGR04523 337 IS-----QLNEQISQLKKEltnsesensekqreLEEKQNEIEKLKKENQSYKQEIKNLESQINDlESKIQNQEKL----- 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1045 iveqakemtetmEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmvnVPKPGHKRTDSTHSSNESEY 1124
Cdd:TIGR04523 407 ------------NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS----VKELIIKNLDNTRESLETQL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1125 -TFSSEIAETEdipsRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELD--RKEEQVLRSKAKEEERpQIRGAEL 1201
Cdd:TIGR04523 471 kVLSRSINKIK----QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISslKEKIEKLESEKKEKES-KISDLED 545
|
330 340
....*....|....*....|....*....
gi 1542868643 1202 EYES----LKRQELESENKKLKNELNELR 1226
Cdd:TIGR04523 546 ELNKddfeLKKENLEKEIDEKNKEIEELK 574
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
959-1232 |
2.22e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 55.64 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 959 SETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTQSEKKSIEEHADR------------YKQETEQLVSN 1026
Cdd:pfam02029 50 LKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENneeeensswekeEKRDSRLGRYK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1027 LKEENTLLKQEKEVLNHRIVEQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEfsrLEERYDDLK---------- 1096
Cdd:pfam02029 130 EEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKE---KKVKYESKVfldqkrghpe 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1097 ---EEMTLMVNVPKPGHKRTDSTHSSNESEYTFSSEIAETEdipSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEkqvmQ 1173
Cdd:pfam02029 207 vksQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAE---QKLEELRRRRQEKESEEFEKLRQKQQEAELE----L 279
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1542868643 1174 DELDRKEEQvlRSKAKEEERPQiRGAEleyESLKRQELESENKKLKNELNELRKALSEK 1232
Cdd:pfam02029 280 EELKKKREE--RRKLLEEEEQR-RKQE---EAERKLREEEEKRRMKEEIERRRAEAAEK 332
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
992-1278 |
2.35e-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: 55.90 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 992 IAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKE---VLNHRIVEQAKEMTETMEK-KLVEETKQL 1067
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKArqaEMDRQAAIYAEQERMAMEReRELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1068 ELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVNVPKPGHKRTDSTHSSNESEYTFSSEIAETEDIPSRTEEPSEKK 1147
Cdd:pfam17380 357 ERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1148 VPLDMSLFLKLQKRVTELEQEKQ-----VMQDELDRKEEQVLRSKAK------EEERPQIrgAELEYESLKRQELESENK 1216
Cdd:pfam17380 437 VRRLEEERAREMERVRLEEQERQqqverLRQQEEERKRKKLELEKEKrdrkraEEQRRKI--LEKELEERKQAMIEEERK 514
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1542868643 1217 K--LKNELNELRKALSEKSAPEV------TAPGAPAYRVLMEQLTSVSEE---LDVRKEEVLILRSQLVSQKE 1278
Cdd:pfam17380 515 RklLEKEMEERQKAIYEEERRREaeeerrKQQEMEERRRIQEQMRKATEErsrLEAMEREREMMRQIVESEKA 587
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
904-1486 |
2.53e-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: 55.88 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 904 ELKKLKIEARSVERYKKLHIGMENKIMQLQR---------------KVDEQNKDYKCLMEKLTNLEGIYNSETEKLRSDL 968
Cdd:pfam05483 89 KIKKWKVSIEAELKQKENKLQENRKIIEAQRkaiqelqfenekvslKLEEEIQENKDLIKENNATRHLCNLLKETCARSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 969 ERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQ--TQSEKKSIEEHAdRYKQETEQlVSNLKEENTLLKQEKEVLNHRIV 1046
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEElrVQAENARLEMHF-KLKEDHEK-IQHLEEEYKKEINDKEKQVSLLL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1047 EQAKEMTETMEKK--LVEETKQLELDLNDE-RLRYQNLlnefSRLEERYDDLKEEMTLMvnvpKPGHKRTDSTHSSNESE 1123
Cdd:pfam05483 247 IQITEKENKMKDLtfLLEESRDKANQLEEKtKLQDENL----KELIEKKDHLTKELEDI----KMSLQRSMSTQKALEED 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1124 YTFSSEI--AETEDIPSRTEEPSEKKVPLDMSlflklqkrVTELEQEKQVMQdELDRKEEQVLRskaKEEERPQIRGAEL 1201
Cdd:pfam05483 319 LQIATKTicQLTEEKEAQMEELNKAKAAHSFV--------VTEFEATTCSLE-ELLRTEQQRLE---KNEDQLKIITMEL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1202 EYESLKRQELESENKKLKNELNELRKALSEKsapEVTAPGAPAYRVLMEQLTSVSEE----LDVRKEEVLILRSQLVSQK 1277
Cdd:pfam05483 387 QKKSSELEEMTKFKNNKEVELEELKKILAED---EKLLDEKKQFEKIAEELKGKEQEliflLQAREKEIHDLEIQLTAIK 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1278 EAIQ--PKDDKNTMTDstilLEDvQKMKDKGEIAQAYIGLKETNRLLES------QLQSQKRSHEN---EAEALRGEIQS 1346
Cdd:pfam05483 464 TSEEhyLKEVEDLKTE----LEK-EKLKNIELTAHCDKLLLENKELTQEasdmtlELKKHQEDIINckkQEERMLKQIEN 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1347 LKEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNENLYFEELYADDPKKYQSYRISLYKRMID----LMEQLEKQDK 1422
Cdd:pfam05483 539 LEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEnknkNIEELHQENK 618
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1542868643 1423 TVRKL----KKQLKVFAKKIGELEvgqMENISPGQIIDEPIrpvniprkeKDFQGMLEYKKEDEQKLV 1486
Cdd:pfam05483 619 ALKKKgsaeNKQLNAYEIKVNKLE---LELASAKQKFEEII---------DNYQKEIEDKKISEEKLL 674
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
900-1066 |
2.82e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 55.17 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 900 MAKRELKKLKIEARSVERYKKLHIgmENKIMQLQRKVDEQNKDYKclmEKLTNLEGIYNSETEKLRSDLERLQLSEEEAK 979
Cdd:PRK12704 39 EAKRILEEAKKEAEAIKKEALLEA--KEEIHKLRNEFEKELRERR---NELQKLEKRLLQKEENLDRKLELLEKREEELE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 980 IATGRVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQE--TEQLVSNLKEEntlLKQEKEVLNHRIVEQAKEMTETME 1057
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEeaKEILLEKVEEE---ARHEAAVLIKEIEEEAKEEADKKA 190
|
....*....
gi 1542868643 1058 KKLVEETKQ 1066
Cdd:PRK12704 191 KEILAQAIQ 199
|
|
| Myo5p-like_CBD_Rasip1 |
cd15472 |
cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 ... |
1507-1786 |
5.51e-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: 53.82 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1507 PAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVL----KKRGD---------------------DFETVSFWLSNTCR 1561
Cdd:cd15472 25 PAFLLCLCIQHSATHFEPGHFGKLLLKIAKRIQEIVwektKELAEkqpehqdpaslsllsiaelapDLQPLLFWMSNSIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1562 FLHCLKQ----YSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmIVSGMLE-----HET 1632
Cdd:cd15472 105 LLYFIQQkvplYEQSMEEELDVGSKESLLSSTLTASEEAMTVLEEVIMYTFQQCVYYLTKTLYV-ALPALLDsnpftAEE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1633 IQGVSG--VKPTGLRkRTSSIADEgtyTLDsILRQLnsfhsvmCQHgmdPELIKQVVKQMFYIVGAVTLNNLLLRKDMCS 1710
Cdd:cd15472 184 RESWSGgsRLPEGVR-RVLEIYQA---TLD-LLRQY-------QVH---PEIASQMFAYLFFFSNASLFNQLMEKGSGGG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1711 ---WSKGMQIRYNVSQLEEWLRDKNLmNSGAKETLEPLIQAAQLLQVKKKTDDDAE--AICSMCNALTTAQIVKVLNLYT 1785
Cdd:cd15472 249 ffqWSRGVQIRANLDLLLDWLQGAGL-GDLAEEFFRKLSSTVNLLATPKEQLLQMSwsSLRAEFPALNPAQLHHLLRQYQ 327
|
.
gi 1542868643 1786 P 1786
Cdd:cd15472 328 L 328
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
813-835 |
5.54e-07 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 47.32 E-value: 5.54e-07
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
882-1494 |
9.38e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.21 E-value: 9.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 882 YRRSIHAIIYLQCCFRRMmaKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGIYNSET 961
Cdd:pfam02463 222 EEEYLLYLDYLKLNEERI--DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELK 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 962 EKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEVL 1041
Cdd:pfam02463 300 SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1042 NHRIVEQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEErydDLKEEMTLMVNVPKPGHKRTDSTHssnE 1121
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEE---LEILEEEEESIELKQGKLTEEKEE---L 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1122 SEYTFSSEIAETEDIPSRTEEPSEKKVPLDMslflKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAEL 1201
Cdd:pfam02463 454 EKQELKLLKDELELKKSEDLLKETQLVKLQE----QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHG 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1202 EYESLKRQELESENKKLKNELNELRKA-----LSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQ 1276
Cdd:pfam02463 530 RLGDLGVAVENYKVAISTAVIVEVSATadeveERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLD 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1277 KEAIQPKDDKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETNRLLESQLQSQKRSHENeaEALRGEIQSLKEENNRQQQ 1356
Cdd:pfam02463 610 KATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASL--SELTKELLEIQELQEKAES 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1357 LLAQNLQLPPEARIEASLQHEITRLTNENLYFEELYADdpKKYQSYRISLYKRMIDLMEQLEKQDKTVRKLKKQLKVFAK 1436
Cdd:pfam02463 688 ELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLAD--RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEE 765
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1542868643 1437 KIGELEVGQMENISPGQIIDEPIRPVNIP---RKEKDFQGMLEYKKEDEQKLVKNLILELK 1494
Cdd:pfam02463 766 KSELSLKEKELAEEREKTEKLKVEEEKEEklkAQEEELRALEEELKEEAELLEEEQLLIEQ 826
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
911-1350 |
1.04e-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: 53.67 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 911 EARSVERYKKLHIGMENKIMQL----QRKVDE-------------QNKDYK----CLMEKLTNLE---GIYNSETEKLRS 966
Cdd:pfam10174 273 EIKQMEVYKSHSKFMKNKIDQLkqelSKKESEllalqtkletltnQNSDCKqhieVLKESLTAKEqraAILQTEVDALRL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 967 DLER-----------LQLSEEEAKIATG--------------RVLSLQEEIAKLrkdLEQTQSEKKSIEEHADRYKqETE 1021
Cdd:pfam10174 353 RLEEkesflnkktkqLQDLTEEKSTLAGeirdlkdmldvkerKINVLQKKIENL---QEQLRDKDKQLAGLKERVK-SLQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1022 QLVSNLKEENTLLKQ---EKEvlnhRIVEQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEE 1098
Cdd:pfam10174 429 TDSSNTDTALTTLEEalsEKE----RIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEH 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1099 MTlmvNVPKPGHKRtDSTHSSNEseytfsSEIAETEDIPSRTEEPSEKKVPLDMSLFLK--LQKRVTELEQEKQVMQDEL 1176
Cdd:pfam10174 505 AS---SLASSGLKK-DSKLKSLE------IAVEQKKEECSKLENQLKKAHNAEEAVRTNpeINDRIRLLEQEVARYKEES 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1177 DRKEEQV------LRSKAKEEERPQIRGAELeyESLKRQELESENKK---LKNELNELRK---ALSEKSAPEVTAPGAPA 1244
Cdd:pfam10174 575 GKAQAEVerllgiLREVENEKNDKDKKIAEL--ESLTLRQMKEQNKKvanIKHGQQEMKKkgaQLLEEARRREDNLADNS 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1245 YRVLMEQLTsvsEELDVRKEEVLILRSQLVSQKEAIQPKDD--KNTMTDSTILLEDVQKMKDkgEIAQAYIGLKETNRLL 1322
Cdd:pfam10174 653 QQLQLEELM---GALEKTRQELDATKARLSSTQQSLAEKDGhlTNLRAERRKQLEEILEMKQ--EALLAAISEKDANIAL 727
|
490 500 510
....*....|....*....|....*....|..
gi 1542868643 1323 ESQLQSQKRSHENEAEALRGE----IQSLKEE 1350
Cdd:pfam10174 728 LELSSSKKKKTQEEVMALKREkdrlVHQLKQQ 759
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
980-1244 |
1.63e-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: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 980 IATGRVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVSNLKE-ENTLLKQEKEVlnhRIVEQAKEMTETMEK 1058
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAlERRIAALARRI---RALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1059 KLVEETKQLELDLNDERLRYQNLLNEFSRLEERyddlkEEMTLMVNVPKPghkrTDSTHSSNESEYTFSSEIAETEDIPS 1138
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYRLGRQ-----PPLALLLSPEDF----LDAVRRLQYLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1139 RTEEpsekkvpldmslflkLQKRVTELEQEKQVMQDELDRKEEQVLR-SKAKEEERPQIRGAELEYESLKRQ--ELESEN 1215
Cdd:COG4942 158 DLAE---------------LAALRAELEAERAELEALLAELEEERAAlEALKAERQKLLARLEKELAELAAElaELQQEA 222
|
250 260
....*....|....*....|....*....
gi 1542868643 1216 KKLKNELNELRKALSEKSAPEVTAPGAPA 1244
Cdd:COG4942 223 EELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
925-1353 |
1.95e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.20 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 925 MENKIMQLQRKVDEQNKDYKCLMEKLTNLEGIYNSETEKLRSdlERLQLSEEEAKI------------ATGRVLSLQEE- 991
Cdd:pfam15921 322 LESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEART--ERDQFSQESGNLddqlqklladlhKREKELSLEKEq 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 992 --------------IAKLRKDLEQTQSEKKSIEEHADRYKQE----TEQLVSNLKEENTLLKQ----------EKEVLnH 1043
Cdd:pfam15921 400 nkrlwdrdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSEcqgqMERQMAAIQGKNESLEKvssltaqlesTKEML-R 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1044 RIVEQ--AKEMT-ETMEKKLVEETKQLEldlndERLRYQNLLN-EFSRLEERYDDLKEEMTlmvnvpkpgHKRTDSTHSS 1119
Cdd:pfam15921 479 KVVEEltAKKMTlESSERTVSDLTASLQ-----EKERAIEATNaEITKLRSRVDLKLQELQ---------HLKNEGDHLR 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1120 N---ESEyTFSSEIAETEDIPSRTEEPSEkkvplDMSLFLKLQKR------VTELEQEKQVMQDELDRKEEQVLRSKAKE 1190
Cdd:pfam15921 545 NvqtECE-ALKLQMAEKDKVIEILRQQIE-----NMTQLVGQHGRtagamqVEKAQLEKEINDRRLELQEFKILKDKKDA 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1191 EERP-QIRGAELEYESLKRQELESEN----KKLKNE----LNELRKALSEKSAPevtapgAPAYRVLMEQLTSVSEELDV 1261
Cdd:pfam15921 619 KIRElEARVSDLELEKVKLVNAGSERlravKDIKQErdqlLNEVKTSRNELNSL------SEDYEVLKRNFRNKSEEMET 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1262 RKEEvliLRSQLVS-QKEAIQPKDDKNTMTDStilleDVQKMKDKGEIAQAYIGLKETNRLLESQLQSQKRSHENEAEal 1340
Cdd:pfam15921 693 TTNK---LKMQLKSaQSELEQTRNTLKSMEGS-----DGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANK-- 762
|
490
....*....|...
gi 1542868643 1341 rgEIQSLKEENNR 1353
Cdd:pfam15921 763 --EKHFLKEEKNK 773
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
984-1353 |
2.76e-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: 52.67 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 984 RVLSLQ--EEIAKLRKDLEQTQSE--------KKSIEEHADRYKQETEQLVSNLKEENTLLKQEKevlnhRIVEQAKEMT 1053
Cdd:pfam02463 136 NFLVQGgkIEIIAMMKPERRLEIEeeaagsrlKRKKKEALKKLIEETENLAELIIDLEELKLQEL-----KLKEQAKKAL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1054 ETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEErydDLKEEMTLMVNVPKPGHKRTDSTHSSNESEYTFSSEIAET 1133
Cdd:pfam02463 211 EYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR---DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1134 EDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQELES 1213
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1214 ENKKLKNELNELRKALSEKSAPEvtapgapayRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKDDKNTMTDST 1293
Cdd:pfam02463 368 LEQLEEELLAKKKLESERLSSAA---------KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEES 438
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1294 ILLEDVQKMKDKGEIaqayigLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNR 1353
Cdd:pfam02463 439 IELKQGKLTEEKEEL------EKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSR 492
|
|
| 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 1542868643 639 FRNSLHLLMETLNATTPHYVRCIKP 663
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| fMyo4p_CBD |
cd15479 |
cargo binding domain of fungal myosin 4; Yeast myosin V travels along actin cables, actin ... |
1666-1794 |
4.75e-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: 50.74 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1666 LNSFHSVMCQHGMDPELIKQVVKQMFYIVGAVTLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKnlmNSGAKETLEPL 1745
Cdd:cd15479 168 LNEFDAVLCKFQVVDSMHTKIFNDTLKYLNVMLFNDLITKCPALNWKYGYEVDRNIERLVSWFEPR---IEDVRPNLIQI 244
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1542868643 1746 IQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERV 1794
Cdd:cd15479 245 IQAVKILQLKISNLNEFKLLFDFWYALNPAQIQAILLKYKPANKGEAGV 293
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1129-1270 |
5.94e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.40 E-value: 5.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1129 EIAETEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLR-----SKAKEEERPQIRgAELEY 1203
Cdd:COG2433 389 ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERlerelSEARSEERREIR-KDREI 467
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1542868643 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 ... |
1156-1441 |
7.18e-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: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1156 LKLQKRVTELEQEKQVMQDELDrKEEQVLRSKAKEEERPQIRGAELEYESlKRQELESENKKLKNELNELRKALSEKSAP 1235
Cdd:TIGR02168 205 LERQAEKAERYKELKAELRELE-LALLVLRLEELREELEELQEELKEAEE-ELEELTAELQELEEKLEELRLEVSELEEE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1236 EVTAPGApayrvlMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKDDKNTmTDSTILLEDVQKMKDK-----GEIAQ 1310
Cdd:TIGR02168 283 IEELQKE------LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE-SKLDELAEELAELEEKleelkEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1311 AYIGLKETNRLLEsQLQSQKRSHENEAEALRGEIQSLKEE----NNRQQQLlaqnlqlppEARIEaSLQHEITRLTNENL 1386
Cdd:TIGR02168 356 LEAELEELEAELE-ELESRLEELEEQLETLRSKVAQLELQiaslNNEIERL---------EARLE-RLEDRRERLQQEIE 424
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1542868643 1387 YFEELYADDPKKYQSYRISLYKRMI--------DLMEQLEKQDKTVRKLKKQLKVFAKKIGEL 1441
Cdd:TIGR02168 425 ELLKKLEEAELKELQAELEELEEELeelqeeleRLEEALEELREELEEAEQALDAAERELAQL 487
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
892-1273 |
7.88e-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: 50.66 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 892 LQCCFRR---MMAKRELKKLKIEaRSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGIYnSETEKLRSDL 968
Cdd:pfam07888 36 LEECLQEraeLLQAQEAANRQRE-KEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKY-KELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 969 --ERLQLSEEEAKiATGRVLSLQEEIaklrkdleQTQSEKK-SIEEHADRYKQETEQLVSNLKEENTLLKQEKEVLNHRI 1045
Cdd:pfam07888 114 seEKDALLAQRAA-HEARIRELEEDI--------KTLTQRVlERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1046 VEQAKEMTETME-KKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMvnvpkpghkrTDSTHSSNESEY 1124
Cdd:pfam07888 185 EELRSLSKEFQElRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSL----------QERLNASERKVE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1125 TFSSEIAETEDIPSRTE--------EPSEKKVPL-DMSLFLKLQKrvTELEQEKQVMQdeldrkeeqvlRSKAKEEERPQ 1195
Cdd:pfam07888 255 GLGEELSSMAAQRDRTQaelhqarlQAAQLTLQLaDASLALREGR--ARWAQERETLQ-----------QSAEADKDRIE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1196 IRGAELEYESLKRQELESENKKLKNEL------NELRKALSEKSAPEVTApgapAYRVLMEQltsvSEELDVRKEEVLIL 1269
Cdd:pfam07888 322 KLSAELQRLEERLQEERMEREKLEVELgrekdcNRVQLSESRRELQELKA----SLRVAQKE----KEQLQAEKQELLEY 393
|
....
gi 1542868643 1270 RSQL 1273
Cdd:pfam07888 394 IRQL 397
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
900-1225 |
1.03e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 50.74 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 900 MAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLegIYNSETEKLRSDLERLQLSEEEAK 979
Cdd:TIGR00618 602 KLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTL--TQERVREHALSIRVLPKELLASRQ 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 980 IATGRVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEVLNHRIVE-------QAKEM 1052
Cdd:TIGR00618 680 LALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKElmhqartVLKAR 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1053 TETMEKKLVEETKQLELDLNDERLRyQNLLNEFSRLEERYDDLKE-EMTLMVNVPKPGHKRTDSTHSSNESEYTFSSEIA 1131
Cdd:TIGR00618 760 TEAHFNNNEEVTAALQTGAELSHLA-AEIQFFNRLREEDTHLLKTlEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLE 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1132 ETE----DIPSRTEEPSEKKVPLDMSlfLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKE--EERPQIRGAELEYES 1205
Cdd:TIGR00618 839 EKSatlgEITHQLLKYEECSKQLAQL--TQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEitLYANVRLANQSEGRF 916
|
330 340
....*....|....*....|
gi 1542868643 1206 LKRQELESENKKLKNELNEL 1225
Cdd:TIGR00618 917 HGRYADSHVNARKYQGLALL 936
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
902-1231 |
1.07e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 902 KRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKia 981
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYE-- 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 982 tgrvlSLQEEIAKLRKDLEQTQSEKKSIEEhadrYKQETEQLVSNLKEentlLKQEKEVLNHRIVEQAKEMTETMEKKL- 1060
Cdd:PRK03918 529 -----KLKEKLIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLDE----LEEELAELLKELEELGFESVEELEERLk 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1061 -VEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVNVPKPGHKRTdsthssNESEYTFSSEiaetedipsR 1139
Cdd:PRK03918 596 eLEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL------EELEKKYSEE---------E 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1140 TEEPSEKKVPLDMSLFlKLQKRVTELEQEKQVMQDELDRKEEQvlrskaKEEerpqIRGAELEYESLKR-----QELESE 1214
Cdd:PRK03918 661 YEELREEYLELSRELA-GLRAELEELEKRREEIKKTLEKLKEE------LEE----REKAKKELEKLEKalervEELREK 729
|
330
....*....|....*..
gi 1542868643 1215 NKKLKNELNElrKALSE 1231
Cdd:PRK03918 730 VKKYKALLKE--RALSK 744
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
926-1432 |
1.45e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 50.35 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 926 ENKIMQLQRKVD---EQNKDYKCLMEKLTNLEGiyNSETEKLRSDLERLQLSEEEAKIatgrVLSlQEEIAKLRKDLEQT 1002
Cdd:TIGR00618 378 TQHIHTLQQQKTtltQKLQSLCKELDILQREQA--TIDTRTSAFRDLQGQLAHAKKQQ----ELQ-QRYAELCAAAITCT 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1003 QSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEVlnHRIVEQAKEMTETMEKKLVEETKQLELDLNDERL------ 1076
Cdd:TIGR00618 451 AQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRK--KAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNpgpltr 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1077 RYQNLLNEFSRLEERYDDLKEEMTLMVN---VPKPGHKRTDSTHSSNESEYTFSSEIAE-----TEDIPSRTEEPSEKKV 1148
Cdd:TIGR00618 529 RMQRGEQTYAQLETSEEDVYHQLTSERKqraSLKEQMQEIQQSFSILTQCDNRSKEDIPnlqniTVRLQDLTEKLSEAED 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1149 PLdmSLFLKLQKRVTELEQEKQ-VMQDELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQELESEnkKLKNELNELRK 1227
Cdd:TIGR00618 609 ML--ACEQHALLRKLQPEQDLQdVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKE--LLASRQLALQK 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1228 ALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEvliLRSQLVSQKEAIQPKDDkntmtdstiLLEDVqkmkdkge 1307
Cdd:TIGR00618 685 MQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE---IENASSSLGSDLAARED---------ALNQS-------- 744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1308 iaqayigLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNlqlppeaRIEASLQHEITRLTNEnly 1387
Cdd:TIGR00618 745 -------LKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFN-------RLREEDTHLLKTLEAE--- 807
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1542868643 1388 FEELYADDPKKYQSYRISLYKRMIDLMEQLEKQDKTVRKLKKQLK 1432
Cdd:TIGR00618 808 IGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLL 852
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
931-1434 |
1.92e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.84 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 931 QLQRKVDEQNKDYKCLMEKLTNLEGIYNSETEKLRSDLERL--QLSEEEAKIATGRVLSLQEEiaklRKDLEQTQSEKKS 1008
Cdd:pfam12128 351 SWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDiaGIKDKLAKIREARDRQLAVA----EDDLQALESELRE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1009 IEEHADR-YKQETEQLVSNLKEENTLLKQ----EKEVLNhriVEQAKEMTETMEKKLVEETKQLElDLNDERLRYQNLLN 1083
Cdd:pfam12128 427 QLEAGKLeFNEEEYRLKSRLGELKLRLNQatatPELLLQ---LENFDERIERAREEQEAANAEVE-RLQSELRQARKRRD 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1084 EFS--------RLEERYDDLKEEMTLMVnvPKPGH-------------------------KRTD----STHSSNESEYTF 1126
Cdd:pfam12128 503 QASealrqasrRLEERQSALDELELQLF--PQAGTllhflrkeapdweqsigkvispellHRTDldpeVWDGSVGGELNL 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1127 ------------SSEIAETEDIPSR---------TEEPSEKKVPLDMSLF-LKLQKRVTELEQEKQ-------------- 1170
Cdd:pfam12128 581 ygvkldlkridvPEWAASEEELRERldkaeealqSAREKQAAAEEQLVQAnGELEKASREETFARTalknarldlrrlfd 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1171 VMQDELDRKEEQVLRSKAKEEERpqirgaeleyeslkRQELESENKKLKNELNELRKALSEKSApEVTAPGAPAYRVLME 1250
Cdd:pfam12128 661 EKQSEKDKKNKALAERKDSANER--------------LNSLEAQLKQLDKKHQAWLEEQKEQKR-EARTEKQAYWQVVEG 725
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1251 QLtsvSEELDVRKEEVLILRSQLVSQKEAIQpKDDKNTMTDSTILLEDVQKMK---------------DKGEIAQAYIGL 1315
Cdd:pfam12128 726 AL---DAQLALLKAAIAARRSGAKAELKALE-TWYKRDLASLGVDPDVIAKLKreirtlerkieriavRRQEVLRYFDWY 801
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1316 KETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNENLYFEELYADD 1395
Cdd:pfam12128 802 QETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANS 881
|
570 580 590
....*....|....*....|....*....|....*....
gi 1542868643 1396 pkkyQSYRISLYKRMIDLMEQLEKQDKTVRKLKKQLKVF 1434
Cdd:pfam12128 882 ----EQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHF 916
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
905-1100 |
1.98e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 905 LKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGIyNSETEKLRSDLERLQ--LSEEEAKIAT 982
Cdd:PRK03918 587 VEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAET-EKRLEELRKELEELEkkYSEEEYEELR 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 983 GRVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQEteqlvsnlKEENTLLKQEKEVLnhrivEQAKEMTETMEKKLve 1062
Cdd:PRK03918 666 EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE--------LEEREKAKKELEKL-----EKALERVEELREKV-- 730
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1542868643 1063 etkqleldlnderLRYQNLLNE--FSRLEERYDDLKEEMT 1100
Cdd:PRK03918 731 -------------KKYKALLKEraLSKVGEIASEIFEELT 757
|
|
| IQ |
pfam00612 |
IQ calmodulin-binding motif; Calmodulin-binding motif. |
815-835 |
2.55e-05 |
|
IQ calmodulin-binding motif; Calmodulin-binding motif.
Pssm-ID: 459869 Cd Length: 21 Bit Score: 42.30 E-value: 2.55e-05
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
972-1336 |
2.69e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 972 QLSEEEAKIATGRVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEVLNhriveqake 1051
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA--------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1052 mtetmekKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVNVPKPGHKRTDSTHssneseytfsseia 1131
Cdd:COG4372 98 -------QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE-------------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1132 etEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQEL 1211
Cdd:COG4372 157 --EQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1212 ESENKKLKNELNELRKALsEKSAPEVTAPGAPAYRVLMEQLTSVSE--ELDVRKEEVLILRSQLVSQKEAIQPKDDKNTM 1289
Cdd:COG4372 235 LSALLDALELEEDKEELL-EEVILKEIEELELAILVEKDTEEEELEiaALELEALEEAALELKLLALLLNLAALSLIGAL 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1542868643 1290 TDSTILLEDVQKMKDKGEIAQAYIGLKETNRLLESQLQSQKRSHENE 1336
Cdd:COG4372 314 EDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLS 360
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
926-1098 |
3.39e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 926 ENKIMQLQRKVDEQNKDYKCLMEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLE----- 1000
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1001 -QTQSEK----------KSIEEHADRYKQeTEQLVSNLKEENTLLKQEKEVLNHRI--VEQAKEMTETMEKKLVEETKQL 1067
Cdd:COG3883 95 lYRSGGSvsyldvllgsESFSDFLDRLSA-LSKIADADADLLEELKADKAELEAKKaeLEAKLAELEALKAELEAAKAEL 173
|
170 180 190
....*....|....*....|....*....|.
gi 1542868643 1068 ELDLNDERLRYQNLLNEFSRLEERYDDLKEE 1098
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
926-1347 |
3.73e-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: 49.02 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 926 ENKIMQLQRKVDEQNKDYKCLMEKLTNLEGiYNSEtekLRSDLERLQLSEEEAkiaTGRVLSLQEEIAKLRKDLEQTQSE 1005
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEA-QISE---LQEDLESERAARNKA---EKQRRDLGEELEALKTELEDTLDT 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1006 KKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEVLNHRIVEQAKEMTETME-----KKLVEETKQ-LELDLND------ 1073
Cdd:pfam01576 315 TAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEqakrnKANLEKAKQaLESENAElqaelr 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1074 ---------ERLR------YQNLLNEFSRLEERYDDLKEEMTLMVNvpkpghkRTDS-THSSNESE----------YTFS 1127
Cdd:pfam01576 395 tlqqakqdsEHKRkklegqLQELQARLSESERQRAELAEKLSKLQS-------ELESvSSLLNEAEgkniklskdvSSLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1128 SEIAETEDIpsRTEEPSEKkvpldmslfLKLQKRVTELEQEKQVMQDELDrKEEQVLRSKAKEEERPQIRGAE----LEY 1203
Cdd:pfam01576 468 SQLQDTQEL--LQEETRQK---------LNLSTRLRQLEDERNSLQEQLE-EEEEAKRNVERQLSTLQAQLSDmkkkLEE 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1204 ESLKRQELESENKKLKNELNELRKALSEKSApevtapgapAYRVLMEQLTSVSEELDVRKEEVLILRsQLVSQKEAIQPK 1283
Cdd:pfam01576 536 DAGTLEALEEGKKRLQRELEALTQQLEEKAA---------AYDKLEKTKNRLQQELDDLLVDLDHQR-QLVSNLEKKQKK 605
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1542868643 1284 DDKNTMTDSTIlledVQKMKDKGEIAQAYIGLKET-----NRLLEsQLQSQKRSHENEAEALRGEIQSL 1347
Cdd:pfam01576 606 FDQMLAEEKAI----SARYAEERDRAEAEAREKETralslARALE-EALEAKEELERTNKQLRAEMEDL 669
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
926-1098 |
3.77e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 926 ENKIMQLQRKVDEQNKDYKCLMEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTQSE 1005
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1006 ----------------------KKSIEEHADR------YKQETEQLVSNLKEENTLLKQEKEVLnhrivEQAKEMTETME 1057
Cdd:COG4942 106 laellralyrlgrqpplalllsPEDFLDAVRRlqylkyLAPARREQAEELRADLAELAALRAEL-----EAERAELEALL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1542868643 1058 KKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEE 1098
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
904-1301 |
3.93e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 48.53 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 904 ELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEqnkdykcLMEKLTNLEGI---YNSETEKLRSDLERLQLSEEEAKI 980
Cdd:pfam05622 36 ENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQ-------LQEENFRLETArddYRIKCEELEKEVLELQHRNEELTS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 981 ATGRVLSLQEEIAKLR------KDLEQT-QSEKKSIEEHADRYKQeteqlVSNLKEENTLLKQEKEVLNhrivEQAKEMT 1053
Cdd:pfam05622 109 LAEEAQALKDEMDILRessdkvKKLEATvETYKKKLEDLGDLRRQ-----VKLLEERNAEYMQRTLQLE----EELKKAN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1054 ------ETMEKKLVEetkqLELDLNDERLRYQNLLNEFSRLEERYDDL-KEEMTLMVnvpkpghkRTDSTHSSNE----- 1121
Cdd:pfam05622 180 alrgqlETYKRQVQE----LHGKLSEESKKADKLEFEYKKLEEKLEALqKEKERLII--------ERDTLRETNEelrca 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1122 --SEYTFSSEIAETEDIPSRTEEPSEKKVPLDmslflkLQKRVTELEQEKQVMQdeldrkeeqvLRSKAKEEERPQIRGA 1199
Cdd:pfam05622 248 qlQQAELSQADALLSPSSDPGDNLAAEIMPAE------IREKLIRLQHENKMLR----------LGQEGSYRERLTELQQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1200 ELEYESLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQltsvseELDVRKEEVLILRSQLVSQKEA 1279
Cdd:pfam05622 312 LLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQ------KLEEHLEKLHEAQSELQKKKEQ 385
|
410 420
....*....|....*....|....*
gi 1542868643 1280 I---QPKDDKNTMTDSTILLEDVQK 1301
Cdd:pfam05622 386 IeelEPKQDSNLAQKIDELQEALRK 410
|
|
| MyosinXI_CBD |
cd15475 |
cargo binding domain of myosin XI; Class XI myosins are a plant specific group, homologous to ... |
1531-1784 |
4.15e-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: 47.95 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1531 LTSTINSIKKVlkkrGDDFETVSFWLSNTCRFLhCLKQysgeegfmkhntsrqneHCLTnfdlaeyrqvlsdlAIQIYQQ 1610
Cdd:cd15475 52 IIQTIGSAIED----QDNNDHLAYWLSNTSTLL-FLLQ-----------------RSLP--------------ALLFKQQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1611 LVRVLENILqPMI-------VSGMLEhETIQGVSGVKPTGLRKRTSSIADEGTYTL---DSILRQLNSFHSVMCQHGMDP 1680
Cdd:cd15475 96 LTAYVEKIY-GIIrdnlkkeLSPLLS-LCIQAPRTSRGSSSKSSSSANSLGQQSPSshwQSIIKSLNSLLSTLKENHVPP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1681 ELIKQVVKQMFYIVGAVTLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDknlmnsgAKET--------LEPLIQAAQLL 1752
Cdd:cd15475 174 FLVQKIFTQVFSFINVQLFNSLLLRRECCSFSNGEYVKAGLAELELWCSQ-------ATEEyagsswdeLKHIRQAVGFL 246
|
250 260 270
....*....|....*....|....*....|...
gi 1542868643 1753 QVKKKTDDDAEAICS-MCNALTTAQIVKVLNLY 1784
Cdd:cd15475 247 VIHQKSRKSYDEITNdLCPVLSVQQLYRICTMY 279
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
971-1099 |
4.67e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 971 LQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEVLNHRIVEQAK 1050
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1542868643 1051 ------------------------EMTETM---EKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEM 1099
Cdd:COG3883 98 sggsvsyldvllgsesfsdfldrlSALSKIadaDADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
897-1234 |
5.69e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.50 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 897 RRMMAKRELKKLKIEARSVERYKKlhiGMENKIMQLQRKVD---EQNKDYKCLME------KLTNLEGIYNSETEKLRSD 967
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQEKT---ELLVEQGRLQLQADrhqEHIRARDSLIQslatrlELDGFERGPFSERQIKNFH 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 968 LERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTQSEKK----SIEEHADRYKQETEQLVSNLKEENTLLKQEKEVL-- 1041
Cdd:TIGR00606 397 TLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKglgrTIELKKEILEKKQEELKFVIKELQQLEGSSDRILel 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1042 NHRIVEQAKEMTETMEKKLVEETKQLELDLNDERLryqNLLNEFSRLEERYDDLKEEMTLMVNVPKPGHKRTDSTHSSNE 1121
Cdd:TIGR00606 477 DQELRKAERELSKAEKNSLTETLKKEVKSLQNEKA---DLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRK 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1122 SEYTFSSE-IAETEDIP-----SRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKeeerpq 1195
Cdd:TIGR00606 554 IKSRHSDElTSLLGYFPnkkqlEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDK------ 627
|
330 340 350
....*....|....*....|....*....|....*....
gi 1542868643 1196 irgaelEYESLKRQELESENKKLKNELNELRKALSEKSA 1234
Cdd:TIGR00606 628 ------LFDVCGSQDEESDLERLKEEIEKSSKQRAMLAG 660
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
929-1212 |
7.38e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 929 IMQLQRKVDEQNKDYKCLMEKLTNLegiyNSETEKLRSDLER----LQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTQS 1004
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQL----REELEQAREELEQleeeLEQARSELEQLEEELEELNEQLQAAQAELAQAQE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1005 EKKSIEEHADRYKQETEQL---VSNLKEENTLLKQEKEVLNHRIVEQAKEMTETMEKKLVEETKQLELDLNDERLRYQNL 1081
Cdd:COG4372 102 ELESLQEEAEELQEELEELqkeRQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1082 LNEFSRLEERYDDLKEEMTLMVNVPKPGHKRTDSTHSSNESEYTFSSEIAETEDIPSRTEEPSEKKvpLDMSLFLKLQKR 1161
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEED--KEELLEEVILKE 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1542868643 1162 VTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQELE 1212
Cdd:COG4372 260 IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
959-1423 |
7.79e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 7.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 959 SETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRkdlEQTQSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEK 1038
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLT---LRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1039 EVLNH----RIVEQAKEMTETMEKKLVEETKQLE-----LDLNDERLRYQ----NLLNEFSRL-------EERYDDLKEE 1098
Cdd:TIGR00618 240 QSHAYltqkREAQEEQLKKQQLLKQLRARIEELRaqeavLEETQERINRArkaaPLAAHIKAVtqieqqaQRIHTELQSK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1099 MTLMVNVPKPGHKRTDSTHSSNESEYTFSSEIAETEDIPSRTEEPSEKKVPLDMSL-----FLKLQKRVTELEQEKQVMQ 1173
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHtltqhIHTLQQQKTTLTQKLQSLC 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1174 DELDRKEEQVLRSKAKEEERPQIRG----------AELEYESLKRQELESENKKLKNE---LNELRKALSEKSAPEVTAp 1240
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDLQGqlahakkqqeLQQRYAELCAAAITCTAQCEKLEkihLQESAQSLKEREQQLQTK- 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1241 gapayRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKddkntMTDSTILLEDVQKMKdkgEIAQAYIGLKETNR 1320
Cdd:TIGR00618 479 -----EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPA-----RQDIDNPGPLTRRMQ---RGEQTYAQLETSEE 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1321 LLESQLQS---QKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEAR--IEASLQHEITRLTNENLYFEELyadd 1395
Cdd:TIGR00618 546 DVYHQLTSerkQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQdlTEKLSEAEDMLACEQHALLRKL---- 621
|
490 500
....*....|....*....|....*...
gi 1542868643 1396 PKKYQSYRISLYKRMIDLMEQLEKQDKT 1423
Cdd:TIGR00618 622 QPEQDLQDVRLHLQQCSQELALKLTALH 649
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
909-1273 |
9.17e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 9.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 909 KIEARSVERYK---KLHIGMENKIMQLQRKVDE---QNKDYKCLMEKLTNLEGIYN---SETEKLRSDLERLQLsEEEAK 979
Cdd:COG4717 50 RLEKEADELFKpqgRKPELNLKELKELEEELKEaeeKEEEYAELQEELEELEEELEeleAELEELREELEKLEK-LLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 980 IATGRVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEVLNHRIVEQAKEMTEtmekk 1059
Cdd:COG4717 129 PLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE----- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1060 LVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEE----------------------------------------- 1098
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaallallglggsllsliltiagvlflvl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1099 ------MTLMVNVPKPGHKRTDSTHSSNESEYTFSSEIAETEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVM 1172
Cdd:COG4717 284 gllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1173 QDELDRKEEQVLRSKAKEEERPQIRGAELEYEslKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQL 1252
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEDEEELRAALEQAE--EYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEEL 441
|
410 420
....*....|....*....|.
gi 1542868643 1253 TSVSEELDVRKEEVLILRSQL 1273
Cdd:COG4717 442 EELEEELEELREELAELEAEL 462
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
929-1203 |
1.50e-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: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 929 IMQLQRKVDEQNKDYKCLMEKLTNLEGI--YNSETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTQSEK 1006
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQAAKLQGSDLDrtVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEK 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1007 KSIEEHADRYKQETEQLVSNLKEENTLLKQEKEVLNHRI-VEQAKEMTETMEKKLV----EETKQLELDLNDERLRYQNL 1081
Cdd:TIGR00606 874 LQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSpLETFLEKDQQEKEELIsskeTSNKKAQDKVNDIKEKVKNI 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1082 LNEFSRLEERYDDLKEEM---------TLMVNVPKPGHKRTDSTHSSNESEYTF-SSEIAET---EDIPSRTEEPSEKKV 1148
Cdd:TIGR00606 954 HGYMKDIENKIQDGKDDYlkqketelnTVNAQLEECEKHQEKINEDMRLMRQDIdTQKIQERwlqDNLTLRKRENELKEV 1033
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1542868643 1149 PLDMSLFLKL--QKRVTELEQEKQVMQDELD--------------RKEEQVLRSKAKEEErPQIRGAELEY 1203
Cdd:TIGR00606 1034 EEELKQHLKEmgQMQVLQMKQEHQKLEENIDlikrnhvlalgrqkGYEKEIKHFKKELRE-PQFRDAEEKY 1103
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
960-1098 |
1.70e-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: 44.15 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 960 ETEKLRSDLERL-----QLSEEEAKIATGRVLSLQEEIAKLRKDLEQTQsekKSIEEHADRYKQETEQLvSNLKEENTLL 1034
Cdd:pfam08614 22 ENAKLQSEPESVlpstsSSKLSKASPQSASIQSLEQLLAQLREELAELY---RSRGELAQRLVDLNEEL-QELEKKLRED 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1542868643 1035 KQEKEVLNHRiVEQAKEMTETMEKKLVEETKQLElDLNDErlrYQNLLNEFSRLEERYDDLKEE 1098
Cdd:pfam08614 98 ERRLAALEAE-RAQLEEKLKDREEELREKRKLNQ-DLQDE---LVALQLQLNMAEEKLRKLEKE 156
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
923-1129 |
2.33e-04 |
|
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: 46.21 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 923 IGMENKIMqlqrKVDEQNKdYKCLMEKLTNLEGIYnSETEKLRSDLERLQlseeEAKIATGRVLSLQEEIAKLRKDLEQT 1002
Cdd:pfam05911 624 SSMEDEIK----KHDCIDK-VTLSENKVAQVDNGC-SEIDNLSSDPEIPS----DGPLVSGSNDLKTEENKRLKEEFEQL 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1003 QSEKKSIEEHADRYK----------QETEQLVSNLKEENTLLKQEKEVLNHRIVEQAkEMTETMEKKLVEetkqLELDLN 1072
Cdd:pfam05911 694 KSEKENLEVELASCTenlestksqlQESEQLIAELRSELASLKESNSLAETQLKCMA-ESYEDLETRLTE----LEAELN 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1542868643 1073 DERLRYQNLLNEFS-------RLEERYDDLKEEMTLMVNVPKPGHKRTDS-THSSNESEYTFSSE 1129
Cdd:pfam05911 769 ELRQKFEALEVELEeekncheELEAKCLELQEQLERNEKKESSNCDADQEdKKLQQEKEITAASE 833
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
925-1273 |
2.43e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.32 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 925 MENKIMQLQRKVDEQNKDYKCLMEKLTNLEGiynsETEKLRSDLERLQLSEEE----AKIATGRVLSLQEEIAKLRKDLE 1000
Cdd:pfam01576 775 LELDLKELEAQIDAANKGREEAVKQLKKLQA----QMKDLQRELEEARASRDEilaqSKESEKKLKNLEAELLQLQEDLA 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1001 QTQSEKKSIEEHADRYKQEteqlVSNLKEENTLLKQEKEVLNHRIVEQAKEMTE---TME------KKLVEETKQLELDL 1071
Cdd:pfam01576 851 ASERARRQAQQERDELADE----IASGASGKSALQDEKRRLEARIAQLEEELEEeqsNTEllndrlRKSTLQVEQLTTEL 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1072 NDERLRYQNLLNEFSRLEERYDDLKEEMTLMVNVPKPGHKRTDSthssneseyTFSSEIAETE---DIPSRTEEPSEKKV 1148
Cdd:pfam01576 927 AAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIA---------ALEAKIAQLEeqlEQESRERQAANKLV 997
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1149 pldmslflklqkRVTELEQEKQVMQDELDRKEeqvlrskaKEEERPQIRGAELEYESLKRQELESENkklknelnelrka 1228
Cdd:pfam01576 998 ------------RRTEKKLKEVLLQVEDERRH--------ADQYKDQAEKGNSRMKQLKRQLEEAEE------------- 1044
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1542868643 1229 lseksapEVTAPGApAYRVLMEQLTSVSEELDVRKEEVLILRSQL 1273
Cdd:pfam01576 1045 -------EASRANA-ARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
901-1484 |
4.06e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 901 AKRELKKLKIEARSVERYKklhIGMENKIMQLQRKVDEQNKdykclMEKLTNLEGIYNSETEKLRSDLERLQLS---EEE 977
Cdd:PTZ00121 1092 ATEEAFGKAEEAKKTETGK---AEEARKAEEAKKKAEDARK-----AEEARKAEDARKAEEARKAEDAKRVEIArkaEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 978 AKIATGRVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEVLNHRIVEQAKEMTEtmE 1057
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAE--E 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1058 KKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVNVPKPGHKRTDSTHSSNESEYTFSSEIAETEDIP 1137
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAK 1321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1138 SRTEEPSEKKVPLDMSLFLKlQKRVTELEQEKQVMQDELDRKEEQVLRSKAK-EEERPQIRGAELEYESLKR-QELESEN 1215
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEA-KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKkEEAKKKADAAKKKAEEKKKaDEAKKKA 1400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1216 KKLKNELNELRKALSEKSAPEVTAPGAPAYRVlMEQLTSVSEEL-----------DVRKEEVLILRSQLVSQKEAIQPKD 1284
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKK-ADEAKKKAEEAkkadeakkkaeEAKKAEEAKKKAEEAKKADEAKKKA 1479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1285 D--------KNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETNRLLESQLQSQKRSHEN--------EAEALRG--EIQS 1346
Cdd:PTZ00121 1480 EeakkadeaKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEakkaeekkKADELKKaeELKK 1559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1347 LKEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNENLYFEE---LYADDPKKYQSYRISlykrmidlMEQLEKQDKt 1423
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEekkMKAEEAKKAEEAKIK--------AEELKKAEE- 1630
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1542868643 1424 VRKLKKQLkvfaKKIGELEVGQMENISPGQiIDEPIRPVNIPRK-EKDFQGMLEYKKEDEQK 1484
Cdd:PTZ00121 1631 EKKKVEQL----KKKEAEEKKKAEELKKAE-EENKIKAAEEAKKaEEDKKKAEEAKKAEEDE 1687
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
960-1238 |
5.45e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 960 ETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVSnLKEENTLLKQEKE 1039
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE-LRERAAELEAEAE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1040 VLNHRIVEQAKEMTETMEKKLVEETKQLELDLNDERL-RYQNLLNEFSRLEERYDDLKEemtlmvnvpkpghKRTDSTHS 1118
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLeRIRTLLAAIADAEDEIERLRE-------------KREALAEL 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1119 SNESEytfsseiaetEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQvlrskaKEEERPQIRG 1198
Cdd:PRK02224 622 NDERR----------ERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREE------RDDLQAEIGA 685
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1542868643 1199 AELEYESLKrqELESENKKLKNELNELRKALSEKSAPEVT 1238
Cdd:PRK02224 686 VENELEELE--ELRERREALENRVEALEALYDEAEELESM 723
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
968-1350 |
5.56e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 44.63 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 968 LERLQLSEEEAKiatgrvlSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEVLnhrivE 1047
Cdd:pfam05701 34 VERRKLVELELE-------KVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQDS-----E 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1048 QAKEMTETMEKKLVEETK-----QLELdlndERLRYQNLLNEFSRLEERYDDLKEEMTLMVNVPKPGHKRT-DSTHSSNE 1121
Cdd:pfam05701 102 LAKLRVEEMEQGIADEASvaakaQLEV----AKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAeEAVSASKE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1122 SEYTFssEIAETEDIPSRTE---------EPSEKKVPLDMSL---FLKLQKrvtELEQekqvMQDELDRKEEQVLRSKAK 1189
Cdd:pfam05701 178 IEKTV--EELTIELIATKESlesahaahlEAEEHRIGAALAReqdKLNWEK---ELKQ----AEEELQRLNQQLLSAKDL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1190 EeerpqirgAELEYESLKRQELESE-NKKLKNELNELRKALSEKSAPEVTAPGApayrvlmeqLTSVSEEL-DVR----- 1262
Cdd:pfam05701 249 K--------SKLETASALLLDLKAElAAYMESKLKEEADGEGNEKKTSTSIQAA---------LASAKKELeEVKaniek 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1263 -KEEVLI-------LRSQLVSQKEAIQPKDDKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETN-RLLESQLQSQKRSH 1333
Cdd:pfam05701 312 aKDEVNClrvaaasLRSELEKEKAELASLRQREGMASIAVSSLEAELNRTKSEIALVQAKEKEAReKMVELPKQLQQAAQ 391
|
410 420
....*....|....*....|..
gi 1542868643 1334 ENE-----AEALRGEIQSLKEE 1350
Cdd:pfam05701 392 EAEeakslAQAAREELRKAKEE 413
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
962-1099 |
5.95e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 962 EKLRSDL-ERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQlVSNLKE------ENTLL 1034
Cdd:COG1579 23 EHRLKELpAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-VRNNKEyealqkEIESL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1542868643 1035 KQEKEVLNHRI------VEQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEM 1099
Cdd:COG1579 102 KRRISDLEDEIlelmerIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
902-1231 |
6.58e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 902 KRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGIYNSETEKLRSDLERLQLSEEEAkia 981
Cdd:PRK01156 345 KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDI--- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 982 TGRVLSLQEEIAKLRKDLEQTQSEKKSI--------------EEHADRYKQETEQLVSNLKEENTLLKQEKEVLNHRIVE 1047
Cdd:PRK01156 422 SSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVD 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1048 QaKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEE---RYDDLKEEMTLM---------------------V 1103
Cdd:PRK01156 502 L-KKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDkhdKYEEIKNRYKSLkledldskrtswlnalavislI 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1104 NVPKPGHKRTDSTHSSNESEYTFSSEIAETEDIPSRTE-------------EPSEKKVPLDMSLFLKLQKRVTELEQEKQ 1170
Cdd:PRK01156 581 DIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDksireieneannlNNKYNEIQENKILIEKLRGKIDNYKKQIA 660
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1542868643 1171 VMQDELDRKEEQVLRSKAKEEERPQIRGAeLEYESLKRQELESENKKLKNELNELRKALSE 1231
Cdd:PRK01156 661 EIDSIIPDLKEITSRINDIEDNLKKSRKA-LDDAKANRARLESTIEILRTRINELSDRIND 720
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
907-1076 |
6.77e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 44.63 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 907 KLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNK-------DYKCLMEKLTNLEgiynSETEKLRSDLERLQLSEEEAK 979
Cdd:pfam05701 273 KLKEEADGEGNEKKTSTSIQAALASAKKELEEVKAniekakdEVNCLRVAAASLR----SELEKEKAELASLRQREGMAS 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 980 IAtgrVLSLQEEIAKLRKDLEQTQS-EKKSIEEHADRYK------QETEQLVSNLKEENTLLKQEKEVlnhriVEQAKEM 1052
Cdd:pfam05701 349 IA---VSSLEAELNRTKSEIALVQAkEKEAREKMVELPKqlqqaaQEAEEAKSLAQAAREELRKAKEE-----AEQAKAA 420
|
170 180
....*....|....*....|....
gi 1542868643 1053 TETMEKKLVEETKQLELDLNDERL 1076
Cdd:pfam05701 421 ASTVESRLEAVLKEIEAAKASEKL 444
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
998-1496 |
7.24e-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: 44.29 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 998 DLEQTQSEKksiEEHADRYkQETEQLVSNLKEENTLLKQEKEVLNHRI--VEQAKEMTETMEKK----------LVEETK 1065
Cdd:pfam05622 1 DLSEAQEEK---DELAQRC-HELDQQVSLLQEEKNSLQQENKKLQERLdqLESGDDSGTPGGKKylllqkqleqLQEENF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1066 QLELDLNDERLRYQNLLNEFSRLEERYDDLkeemtlmvnvpkpghkrtdstHSSNESEYTFSSEI---AETEDIPSRTEE 1142
Cdd:pfam05622 77 RLETARDDYRIKCEELEKEVLELQHRNEEL---------------------TSLAEEAQALKDEMdilRESSDKVKKLEA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1143 PSE--KKVPLDMSlflKLQKRVTELEQEKQV-MQDELDRKEE----QVLRSKAkEEERPQIRG--AELEYESLKRQELES 1213
Cdd:pfam05622 136 TVEtyKKKLEDLG---DLRRQVKLLEERNAEyMQRTLQLEEElkkaNALRGQL-ETYKRQVQElhGKLSEESKKADKLEF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1214 ENKKLKNELNELRKalsEKsapevtapgapayrvlmEQLTSvseELDVRKEEVLILRSQLVSQKEAIQPkddKNTMTDST 1293
Cdd:pfam05622 212 EYKKLEEKLEALQK---EK-----------------ERLII---ERDTLRETNEELRCAQLQQAELSQA---DALLSPSS 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1294 ILLEDVQKMKDKGEIAQAYIGLKETNRLLESQlqsQKRSHENEAEALrgeiQSLKEENNRQQQLLAQNLQLPPEARIEas 1373
Cdd:pfam05622 266 DPGDNLAAEIMPAEIREKLIRLQHENKMLRLG---QEGSYRERLTEL----QQLLEDANRRKNELETQNRLANQRILE-- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1374 LQHEITRLTnENLYFEELYADDPkkyqsyrISLYKRMIDLMEQLEKQDKTVRKLKKQLKvfakkigELEVGQMENisPGQ 1453
Cdd:pfam05622 337 LQQQVEELQ-KALQEQGSKAEDS-------SLLKQKLEEHLEKLHEAQSELQKKKEQIE-------ELEPKQDSN--LAQ 399
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1542868643 1454 IIDEpiRPVNIPRKEKDFQGMLE-YKKEDEQklVKNLILELKPR 1496
Cdd:pfam05622 400 KIDE--LQEALRKKDEDMKAMEErYKKYVEK--AKSVIKTLDPK 439
|
|
| IQCD |
cd23767 |
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
809-835 |
7.73e-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: 38.68 E-value: 7.73e-04
10 20
....*....|....*....|....*..
gi 1542868643 809 AKFLRRTKAATIIQKYWRMYVARRRYK 835
Cdd:cd23767 3 EELQRMNRAATLIQALWRGYKVRKELK 29
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
925-1480 |
7.84e-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: 44.65 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 925 MENKIMQLQRKVD--EQNKD-YKCLMEKLTNLEGIYNSE------TEKLRSDLERLQlseEEAKIATGRVLSLQEEIAKL 995
Cdd:TIGR00606 589 TRDRLAKLNKELAslEQNKNhINNELESKEEQLSSYEDKlfdvcgSQDEESDLERLK---EEIEKSSKQRAMLAGATAVY 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 996 RKDLEQTQSEKKSIEEHADR---YKQETEQLVSNLKEENTLLKQEKEVLNHRIVEQAKEMTETMEKKLVE--ETKQLELD 1070
Cdd:TIGR00606 666 SQFITQLTDENQSCCPVCQRvfqTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRqsIIDLKEKE 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1071 LNDERLRYQNLLNEFSRLEeryDDLKEEMTLMVNV-PKPGHKRTDSTHSSNESEYTfsseiAETEDIPSRTEEPSEKKVP 1149
Cdd:TIGR00606 746 IPELRNKLQKVNRDIQRLK---NDIEEQETLLGTImPEEESAKVCLTDVTIMERFQ-----MELKDVERKIAQQAAKLQG 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1150 LDmslflkLQKRVTELEQEKQVMQDELDRKEEQV-LRSKAKEEERPQIrgaeleyeslkrQELESENKKLKNELNELRKA 1228
Cdd:TIGR00606 818 SD------LDRTVQQVNQEKQEKQHELDTVVSKIeLNRKLIQDQQEQI------------QHLKSKTNELKSEKLQIGTN 879
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1229 LSEKSAPEVTApgapayRVLMEQLTSVSEELDVRKEEVL----ILRSQLVSQKEAIQPKDDKNTMTDstillEDVQKMKD 1304
Cdd:TIGR00606 880 LQRRQQFEEQL------VELSTEVQSLIREIKDAKEQDSpletFLEKDQQEKEELISSKETSNKKAQ-----DKVNDIKE 948
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1305 KgeIAQAYIGLKETNRLLESQLQSQKRSHENEaeaLRGEIQSLKEENNRQQQLLAQNLQLppeaRIEASLQHEITRLTNE 1384
Cdd:TIGR00606 949 K--VKNIHGYMKDIENKIQDGKDDYLKQKETE---LNTVNAQLEECEKHQEKINEDMRLM----RQDIDTQKIQERWLQD 1019
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1385 NLyfeelyaddpkkyqsyrislykrmidlmeQLEKQDKTVRKLKKQLKVFAKKIGELEVGQMENisPGQIIDEPIRpvNI 1464
Cdd:TIGR00606 1020 NL-----------------------------TLRKRENELKEVEEELKQHLKEMGQMQVLQMKQ--EHQKLEENID--LI 1066
|
570
....*....|....*..
gi 1542868643 1465 PRKE-KDFQGMLEYKKE 1480
Cdd:TIGR00606 1067 KRNHvLALGRQKGYEKE 1083
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
959-1098 |
8.08e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 959 SETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEK 1038
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1542868643 1039 EVLNHRIVEQAKEMTEtmEKKLVEETKQLELDLndERLRYQNL--LNEFSRLEERYDDLKEE 1098
Cdd:COG1196 746 ELLEEEALEELPEPPD--LEELERELERLEREI--EALGPVNLlaIEEYEELEERYDFLSEQ 803
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
925-1095 |
8.63e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 925 MENKIMQLQRKVDEQNKDYKCLMEKLTNLEgiynSETEKLRSDLERLQlseeeAKIATGR----VLSLQEEIAKLRKDLE 1000
Cdd:COG1579 36 LEDELAALEARLEAAKTELEDLEKEIKRLE----LEIEEVEARIKKYE-----EQLGNVRnnkeYEALQKEIESLKRRIS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1001 QTQSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEVLNHRIVEQAKEmtetmEKKLVEETKQLELDLNDErlryqn 1080
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE-----LEELEAEREELAAKIPPE------ 175
|
170
....*....|....*
gi 1542868643 1081 LLNEFSRLEERYDDL 1095
Cdd:COG1579 176 LLALYERIRKRKNGL 190
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
960-1350 |
8.77e-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: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 960 ETEKLRSDLERLQLSEEEAKIATGR-VLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVSNLKEEntllkqek 1038
Cdd:pfam01576 493 QLEDERNSLQEQLEEEEEAKRNVERqLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEK-------- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1039 evlnhrivEQAKEMTETMEKKLVEETKQLELDLNDERlryqNLLNEFSRLEERYDDLKEEmtlmvnvpkpghkrtdsths 1118
Cdd:pfam01576 565 --------AAAYDKLEKTKNRLQQELDDLLVDLDHQR----QLVSNLEKKQKKFDQMLAE-------------------- 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1119 snesEYTFSSEIAETEDipsRTEEPSEKKVPLDMSLFLKL---QKRVTELEQEKQVMQDELdrkeEQVLRSK------AK 1189
Cdd:pfam01576 613 ----EKAISARYAEERD---RAEAEAREKETRALSLARALeeaLEAKEELERTNKQLRAEM----EDLVSSKddvgknVH 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1190 EEERPQiRGAELEYESLKRQ--ELE-----SENKKLKNELN-ELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEEL-D 1260
Cdd:pfam01576 682 ELERSK-RALEQQVEEMKTQleELEdelqaTEDAKLRLEVNmQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELeD 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1261 VRKEevlilRSQLVSQKeaiqpKDDKNTMTDSTILLEDVQKMKDKG--EIAQAYIGLKETNRLLESQLQS------QKRS 1332
Cdd:pfam01576 761 ERKQ-----RAQAVAAK-----KKLELDLKELEAQIDAANKGREEAvkQLKKLQAQMKDLQRELEEARASrdeilaQSKE 830
|
410
....*....|....*...
gi 1542868643 1333 HENEAEALRGEIQSLKEE 1350
Cdd:pfam01576 831 SEKKLKNLEAELLQLQED 848
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1157-1350 |
9.37e-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: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1157 KLQKRVTELEQEKQVMQDELDRKEEQVlrSKAKEEerpqIRGAELEYESLKRQ--ELESENKKLKNELNELRKALSEK-S 1233
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAEL--EELNEE----YNELQAELEALQAEidKLQAEIAEAEAEIEERREELGERaR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1234 APEVTAPGAPAYRVLMEQlTSVSEELD----VRKeevlILRSQ---LVSQKEAIQPKDDKNTMTDSTilLEDVQKMKDKG 1306
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGS-ESFSDFLDrlsaLSK----IADADadlLEELKADKAELEAKKAELEAK--LAELEALKAEL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1542868643 1307 EIAQAYI-GLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEE 1350
Cdd:COG3883 167 EAAKAELeAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
925-1072 |
9.49e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.47 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 925 MENKIMQLQRKVDEQNKDYKCLMEKLTNLEGIYNSETEK---LRSDLERL-QLSEEEAKIATGRVLSLQEEIAKLrkdLE 1000
Cdd:smart00787 142 LEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRkdaLEEELRQLkQLEDELEDCDPTELDRAKEKLKKL---LQ 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1542868643 1001 QTQSEKKSIEEhadrYKQETEQLVSNLKEENTLLKQEKEVLNH--RIVEQAKEMTETMEKKLVEETKQLELDLN 1072
Cdd:smart00787 219 EIMIKVKKLEE----LEEELQELESKIEDLTNKKSELNTEIAEaeKKLEQCRGFTFKEIEKLKEQLKLLQSLTG 288
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
971-1104 |
1.04e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 971 LQLSEEEAK-IATGRVLSLQEEIAKLRKDLEQTQSEKKS-IEEHADRYKQETEQLVSNL----KEENTLLKQEKEvLNHR 1044
Cdd:PRK12704 44 LEEAKKEAEaIKKEALLEAKEEIHKLRNEFEKELRERRNeLQKLEKRLLQKEENLDRKLelleKREEELEKKEKE-LEQK 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1542868643 1045 IvEQAKEMTETMEKKLVEETKQLEldlnderlRYQNLLNEFSR---LEERYDDLKEEMTLMVN 1104
Cdd:PRK12704 123 Q-QELEKKEEELEELIEEQLQELE--------RISGLTAEEAKeilLEKVEEEARHEAAVLIK 176
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1039-1275 |
1.37e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1039 EVLNHRIVEQAKEMTETMeKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMtlmvnvpkpghKRTDSTHS 1118
Cdd:pfam07888 30 ELLQNRLEECLQERAELL-QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEEL-----------RQSREKHE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1119 SNESEYT----FSSEIAETEDIPSRTEEPSEKKVpldmslfLKLQKRVTELEQEKQVMQDELDRKEEQVLRS----KAKE 1190
Cdd:pfam07888 98 ELEEKYKelsaSSEELSEEKDALLAQRAAHEARI-------RELEEDIKTLTQRVLERETELERMKERAKKAgaqrKEEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1191 EERPQIRgAELEYESLKRQELESENKKLKNELNE-------LRKALSEKSAPEVTAPGAPA-YRVLMEQLTSVSEELDVR 1262
Cdd:pfam07888 171 AERKQLQ-AKLQQTEEELRSLSKEFQELRNSLAQrdtqvlqLQDTITTLTQKLTTAHRKEAeNEALLEELRSLQERLNAS 249
|
250
....*....|...
gi 1542868643 1263 KEEVLILRSQLVS 1275
Cdd:pfam07888 250 ERKVEGLGEELSS 262
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
906-1081 |
1.45e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 906 KKLKIEARSVERYKKlHIGMEN--------KIMQLQRKVDEQNKdykclmekltnlegiynsETEKLRSDLERLQLSEEE 977
Cdd:PRK00409 495 KRLGLPENIIEEAKK-LIGEDKeklneliaSLEELERELEQKAE------------------EAEALLKEAEKLKEELEE 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 978 AKIatgrvlSLQEEIAKLRKDLEqtQSEKKSIEEHadryKQETEQLVSNL----KEENTLLKQEKEVLNHRIVEQAKEMT 1053
Cdd:PRK00409 556 KKE------KLQEEEDKLLEEAE--KEAQQAIKEA----KKEADEIIKELrqlqKGGYASVKAHELIEARKRLNKANEKK 623
|
170 180
....*....|....*....|....*...
gi 1542868643 1054 EtmEKKLVEETKQLELDLNDeRLRYQNL 1081
Cdd:PRK00409 624 E--KKKKKQKEKQEELKVGD-EVKYLSL 648
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1158-1348 |
1.50e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1158 LQKRVTELEQEKQVMQDELDRKEEQvlrskaKEEERPQIRGAELEYESLKRQELESenkkLKNELNELRKALSEKSApev 1237
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEAR------LDALREELDELEAQIRGNGGDRLEQ----LEREIERLERELEERER--- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1238 tapgapAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQpkddkntmtdstilledvqkmkdkgeiaqayiGLKE 1317
Cdd:COG4913 360 ------RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE--------------------------------EELE 401
|
170 180 190
....*....|....*....|....*....|.
gi 1542868643 1318 TNRLLESQLQSQKRSHENEAEALRGEIQSLK 1348
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
902-1042 |
1.72e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.38 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 902 KRELKKLKIEARSVERYKKLHIGMENkimqLQRK---------VDEQNKDYKCLMEKLTNLEGIYNSET----------- 961
Cdd:PRK05771 113 ENEIKELEQEIERLEPWGNFDLDLSL----LLGFkyvsvfvgtVPEDKLEELKLESDVENVEYISTDKGyvyvvvvvlke 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 962 --EKLRSDLERLQLSEEEakIATGRvlSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKE 1039
Cdd:PRK05771 189 lsDEVEEELKKLGFERLE--LEEEG--TPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAE 264
|
...
gi 1542868643 1040 VLN 1042
Cdd:PRK05771 265 ALS 267
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
943-1085 |
1.81e-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: 42.56 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 943 YKCLMEKLTNLEGIYNSETEKLRSDLERLQL------SEEEAKIATGRVLSLQE-EIAKLRKDLEQTQSEKKSIEEHADR 1015
Cdd:cd16269 144 YQLYLEDREKLVEKYRQVPRKGVKAEEVLQEflqskeAEAEAILQADQALTEKEkEIEAERAKAEAAEQERKLLEEQQRE 223
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1016 YKQETEQLVSNLKEENTLLKQEKEVlnhRIVEQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEF 1085
Cdd:cd16269 224 LEQKLEDQERSYEEHLRQLKEKMEE---ERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSL 290
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
904-1069 |
1.82e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.49 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 904 ELKKL--KIEARSVERYKKlHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGIYN---SETEKLRSDLERLQLSEEEa 978
Cdd:pfam15905 160 ELMKLrnKLEAKMKEVMAK-QEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIeekSETEKLLEYITELSCVSEQ- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 979 kiatgrVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEvlnhRIVEQAKEMTETMEK 1058
Cdd:pfam15905 238 ------VEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKE----ELLREYEEKEQTLNA 307
|
170
....*....|.
gi 1542868643 1059 KLVEETKQLEL 1069
Cdd:pfam15905 308 ELEELKEKLTL 318
|
|
| Paralemmin |
pfam03285 |
Paralemmin; |
1160-1282 |
1.94e-03 |
|
Paralemmin;
Pssm-ID: 460875 Cd Length: 301 Bit Score: 42.42 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1160 KRVTELEQEKQvmQDELDRKEEQVLRSKAKEE----ERPQIRGAElEYESLKRQELESENKK---------LKNELNELR 1226
Cdd:pfam03285 5 KRQTEIENKRR--QLEDDRRQLQHLKSKALRErwllEGPPSSASE-EDEARRRQEEEDEQKKklleeiirrLEEEIELLE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1542868643 1227 KALSEKSAPEvtapgapayrVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQP 1282
Cdd:pfam03285 82 EESSISAKKE----------NLAEKLLEITVEKDKVTGETRVLSSTTLLPDDVQPQ 127
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
900-1239 |
1.97e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 900 MAKRELKKLKIEARSVERYKKlhiGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGIYNSETEKLRSDLERLQLSEEEAK 979
Cdd:COG4372 35 KALFELDKLQEELEQLREELE---QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 980 IATGRVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEVLNHRIVEQAKEMTETMEKK 1059
Cdd:COG4372 112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1060 LVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVNVPKPGHKRTDSTHSSNESEYTFSSEIAETEDIPSR 1139
Cdd:COG4372 192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1140 TEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVmQDELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQELESENkkLK 1219
Cdd:COG4372 272 DTEEEELEIAALELEALEEAALELKLLALLLN-LAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL--LV 348
|
330 340
....*....|....*....|
gi 1542868643 1220 NELNELRKALSEKSAPEVTA 1239
Cdd:COG4372 349 GLLDNDVLELLSKGAEAGVA 368
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
765-786 |
2.01e-03 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 37.31 E-value: 2.01e-03
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
960-1052 |
2.11e-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: 42.44 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 960 ETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKE 1039
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
90
....*....|...
gi 1542868643 1040 VLNHRIVEQAKEM 1052
Cdd:COG4942 231 RLEAEAAAAAERT 243
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
986-1226 |
2.13e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.92 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 986 LSLQEEIAKLRKDLEQTQSEKKSIEehadryKQETEQLVSNLKEE-NTLLKQ-EKEVLNHRIVEQAKEMTETMEKKLVEE 1063
Cdd:pfam06160 233 LNVDKEIQQLEEQLEENLALLENLE------LDEAEEALEEIEERiDQLYDLlEKEVDAKKYVEKNLPEIEDYLEHAEEQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1064 TKQLELDL----------NDERLRYQNLLNEFSRLEERYDDLKEEMTlmvnvpkpghkrtdsthssnESEYTFSSEIAET 1133
Cdd:pfam06160 307 NKELKEELervqqsytlnENELERVRGLEKQLEELEKRYDEIVERLE--------------------EKEVAYSELQEEL 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1134 EDIPSRTEEPSEKKVpldmslflKLQKRVTELEQEKQVMQDELDRKEEQVLRSKaKEEERPQIRGAELEYESLKRqELES 1213
Cdd:pfam06160 367 EEILEQLEEIEEEQE--------EFKESLQSLRKDELEAREKLDEFKLELREIK-RLVEKSNLPGLPESYLDYFF-DVSD 436
|
250
....*....|...
gi 1542868643 1214 ENKKLKNELNELR 1226
Cdd:pfam06160 437 EIEDLADELNEVP 449
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
932-1096 |
2.62e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 932 LQRKVDEQNKDYKCLMEKLTNLEgiynSETEKLRSDLERLQlsEEEAKIATGRVLSLQEEIAKLRKDLEQtqsekksIEE 1011
Cdd:COG4913 293 LEAELEELRAELARLEAELERLE----ARLDALREELDELE--AQIRGNGGDRLEQLEREIERLERELEE-------RER 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1012 HADRYKQETEQLvsNLKEENTllkqEKEVLNHRivEQAKEMTETMEkklvEETKQLELDLNDERLRYQNLLNEFSRLEER 1091
Cdd:COG4913 360 RRARLEALLAAL--GLPLPAS----AEEFAALR--AEAAALLEALE----EELEALEEALAEAEAALRDLRRELRELEAE 427
|
....*
gi 1542868643 1092 YDDLK 1096
Cdd:COG4913 428 IASLE 432
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
1036-1353 |
2.77e-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: 41.93 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1036 QEKEVLNHRIV--EQAKEMTETME-----KKLVEETkqlELDLNDERLRYQNLLNEFSRLEERYDDLKEEMtlmvnvpkp 1108
Cdd:pfam04849 43 QIRETLNYFLLcsDRVSQMTKTYNdieavTRLLEEK---ERDLELAARIGQSLLKQNSVLTERNEALEEQL--------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1109 GHKRTDSTHSSNE--------SEYTFSSEIAETEDIPSRTEEPSEKKVPLDMSLFLK-LQKRVTELEQEKQVmqdeldrk 1179
Cdd:pfam04849 111 GSAREEILQLRHElskkddllQIYSNDAEESETESSCSTPLRRNESFSSLHGCVQLDaLQEKLRGLEEENLK-------- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1180 eeqvLRSKAKeeerpQIRGAELEYEsLKRQELESEnkkLKNELNELRKALSEksapevtapgapayrvLMEQLTSVSEEL 1259
Cdd:pfam04849 183 ----LRSEAS-----HLKTETDTYE-EKEQQLMSD---CVEQLSEANQQMAE----------------LSEELARKMEEN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1260 DVRKEEVLILRSQLVSQKEAIQpkddkntmtdstilledvQKMKDKGEIAQAYIGLKETNRLLESQLQSQKRSHENEAEA 1339
Cdd:pfam04849 234 LRQQEEITSLLAQIVDLQHKCK------------------ELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGM 295
|
330
....*....|....
gi 1542868643 1340 LRGEIQSLKEENNR 1353
Cdd:pfam04849 296 LHEAQEELKELRKK 309
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
969-1098 |
2.82e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 969 ERLQLSE---EEAK-IATGRVLSLQEEIAKL---RKDLEQTQSEKKSIEEHADRYKQETEQLVSNLKE--ENTLLKQEKE 1039
Cdd:PRK00409 495 KRLGLPEniiEEAKkLIGEDKEKLNELIASLeelERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEeeDKLLEEAEKE 574
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1542868643 1040 VlnHRIVEQAKEMTETMEKKLVEETKQLELDLNDerlryQNLLNEFSRLEERYDDLKEE 1098
Cdd:PRK00409 575 A--QQAIKEAKKEADEIIKELRQLQKGGYASVKA-----HELIEARKRLNKANEKKEKK 626
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
987-1103 |
3.02e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 41.05 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 987 SLQEEIAKLRKDleqtqsekksiEEHADRYKQETEQLVSNLKEENTLLKQEKEVLNHRIVEQAKEMTETMEKKlvEETKQ 1066
Cdd:pfam13851 30 SLKEEIAELKKK-----------EERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLK--ARLKV 96
|
90 100 110
....*....|....*....|....*....|....*..
gi 1542868643 1067 LELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMV 1103
Cdd:pfam13851 97 LEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAI 133
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
983-1226 |
3.04e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.52 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 983 GRVLSLQEEIAKLRKDLEQTQSEkksieehadrykqETEQLVSNLKEE-NTLLKQ-EKEVLNHRIVEQAKEMTETMEKKL 1060
Cdd:PRK04778 256 KEIQDLKEQIDENLALLEELDLD-------------EAEEKNEEIQERiDQLYDIlEREVKARKYVEKNSDTLPDFLEHA 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1061 VEETKQLELDL----------NDERLRYQNLLNEFSRLEERYDDLKEEMTlmvnvpkpghkrtdsthssnESEYTFSSEI 1130
Cdd:PRK04778 323 KEQNKELKEEIdrvkqsytlnESELESVRQLEKQLESLEKQYDEITERIA--------------------EQEIAYSELQ 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1131 AETEDIPSRTEEPSEKKVpldmslflKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEER-----PQirgaelEYES 1205
Cdd:PRK04778 383 EELEEILKQLEEIEKEQE--------KLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKSnlpglPE------DYLE 448
|
250 260
....*....|....*....|.
gi 1542868643 1206 LKrQELESENKKLKNELNELR 1226
Cdd:PRK04778 449 MF-FEVSDEIEALAEELEEKP 468
|
|
| CBD_MYO6-like |
cd21759 |
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ... |
767-794 |
3.16e-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: 3.16e-03
10 20
....*....|....*....|....*...
gi 1542868643 767 RAACIRIQKTIRGWLLRKKYlRMRKAAI 794
Cdd:cd21759 45 REALIKIQKTVRGYLARKKH-RPRIKGL 71
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
925-1018 |
3.27e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 925 MENKIMQLQRKVDE---QNKDykcLMEKLTNLEgiynSETEKLRSDLERLQlSEEEAKIATGRVLS-LQEEIAKLRKDLE 1000
Cdd:COG2433 411 EEEEIRRLEEQVERleaEVEE---LEAELEEKD----ERIERLERELSEAR-SEERREIRKDREISrLDREIERLERELE 482
|
90
....*....|....*...
gi 1542868643 1001 QTQSEKKSIEEHADRYKQ 1018
Cdd:COG2433 483 EERERIEELKRKLERLKE 500
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
927-1453 |
3.49e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 927 NKIMQLQRKVDEQNKDYKCLMEKLTNLEGIYNSETEKLrsdlerlqlseEEAKIATGRVLSLQEEIAKLRKDLEQTQSEK 1006
Cdd:PRK01156 197 LELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDY-----------NNLKSALNELSSLEDMKNRYESEIKTAESDL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1007 KSIEEHADRYKQETEQLvsnLKEENTLLKQEKEVLNHRI-----VEQAKEMTETMEKKL------VEETKQLELDLND-- 1073
Cdd:PRK01156 266 SMELEKNNYYKELEERH---MKIINDPVYKNRNYINDYFkykndIENKKQILSNIDAEInkyhaiIKKLSVLQKDYNDyi 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1074 -ERLRYQNLLNEFSRLEERYDDLKEEMTLMVNVPKP-GHKRTDSTHSSNESEYTFSSEIAETEDIPSRTEEPSEKkvpld 1151
Cdd:PRK01156 343 kKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKiEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVK----- 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1152 mslFLKLQKRVTELEQEKQVMQDELDRKEE--QVLRSKAK---------EEERPQIRgaelEYESLKRQELESENKKLKN 1220
Cdd:PRK01156 418 ---LQDISSKVSSLNQRIRALRENLDELSRnmEMLNGQSVcpvcgttlgEEKSNHII----NHYNEKKSRLEEKIREIEI 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1221 ELnelrKALSEKsapevtapgapayrvlMEQLTSVSEELDVRKEEVLILRSQLVSQKEAiQPKDDKNtmtdstilleDVQ 1300
Cdd:PRK01156 491 EV----KDIDEK----------------IVDLKKRKEYLESEEINKSINEYNKIESARA-DLEDIKI----------KIN 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1301 KMKDKGEIAQAyigLKETNRLLESQLQSQKRSHENEAEALRGEIQSlkeENNRQQQLLAQNLQLPPEARIeaslqHEItr 1380
Cdd:PRK01156 540 ELKDKHDKYEE---IKNRYKSLKLEDLDSKRTSWLNALAVISLIDI---ETNRSRSNEIKKQLNDLESRL-----QEI-- 606
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1542868643 1381 ltnenlyfEELYADDpkkyQSYRISLYKRMIDLMEQLEKQDKTVRKLKKQLKVFAKKIGEL--EVGQMENISPGQ 1453
Cdd:PRK01156 607 --------EIGFPDD----KSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYkkQIAEIDSIIPDL 669
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
900-1242 |
4.26e-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: 41.87 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 900 MAKRELKKLKIEArSVERYKKLHIGMENKIMQLQRKVDEqnkdYKCLMEKLTNLEgiynseTEKLRSDLERLQLSEEEAK 979
Cdd:COG5185 217 SESTLLEKAKEII-NIEEALKGFQDPESELEDLAQTSDK----LEKLVEQNTDLR------LEKLGENAESSKRLNENAN 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 980 IATGRVLSLQEEIAklrkDLEQTQSEKKSIEEhadrykqETEQLVSNLKEENtllkqekevlnhriVEQAKEMTETMEKK 1059
Cdd:COG5185 286 NLIKQFENTKEKIA----EYTKSIDIKKATES-------LEEQLAAAEAEQE--------------LEESKRETETGIQN 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1060 LVEEtkqLELDLNDERLRYQNLLNEFSRL--EERYDDLKEEM-----TLMVNVPKPGHKRTDSTHSSNESEYTFSSEI-- 1130
Cdd:COG5185 341 LTAE---IEQGQESLTENLEAIKEEIENIvgEVELSKSSEELdsfkdTIESTKESLDEIPQNQRGYAQEILATLEDTLka 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1131 ---------AETEDIPSRTEEPSEKKVPLDMSlflkLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKE--EERPQIRGA 1199
Cdd:COG5185 418 adrqieelqRQIEQATSSNEEVSKLLNELISE----LNKVMREADEESQSRLEEAYDEINRSVRSKKEDlnEELTQIESR 493
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1542868643 1200 ELEYeslkRQELESENKKLKNELNELRKALSEKSAPEVTAPGA 1242
Cdd:COG5185 494 VSTL----KATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRA 532
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
788-810 |
4.63e-03 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 36.15 E-value: 4.63e-03
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
962-1098 |
4.97e-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: 41.53 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 962 EKLRSDLER--------LQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQlvsnlkeentL 1033
Cdd:pfam05262 184 EALREDNEKgvnfrrdmTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQ----------K 253
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1542868643 1034 LKQEKEVLNHRIVEQAKEMTETMEKKLVE-ETKQLELDLNDERLRYQNllnefsrlEERYDDLKEE 1098
Cdd:pfam05262 254 QQEAKNLPKPADTSSPKEDKQVAENQKREiEKAQIEIKKNDEEALKAK--------DHKAFDLKQE 311
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1208-1461 |
5.09e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1208 RQELESENKKLKNELNELRKALSE-KSAPEVTAPGAPAyRVLMEQLTSVSEELDVRKEEVLILRSQL--VSQKEAIQPKD 1284
Cdd:COG3206 177 LEFLEEQLPELRKELEEAEAALEEfRQKNGLVDLSEEA-KLLLQQLSELESQLAEARAELAEAEARLaaLRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1285 DKNTMTDSTI--LLEDVQKMKdkGEIAQAYIGLKETN---RLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQqqlla 1359
Cdd:COG3206 256 LPELLQSPVIqqLRAQLAELE--AELAELSARYTPNHpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAR----- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1360 qnlqlppeariEASLQHEITRLTNEnlyfeelYADDPKKYQSYRislykrmidlmeQLEKQdktVRKLKKQLKVFAKKIG 1439
Cdd:COG3206 329 -----------EASLQAQLAQLEAR-------LAELPELEAELR------------RLERE---VEVARELYESLLQRLE 375
|
250 260
....*....|....*....|..
gi 1542868643 1440 ELEVGQMENISPGQIIDEPIRP 1461
Cdd:COG3206 376 EARLAEALTVGNVRVIDPAVVP 397
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1158-1387 |
5.68e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1158 LQKRVTELEQEKQVMQDELDRKEEQVLRSKAKE-----EERPQIRGAELEYESLKRQELESENKKLKNELNELRKALSEK 1232
Cdd:COG3206 173 ARKALEFLEEQLPELRKELEEAEAALEEFRQKNglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1233 SAPEVTAPGAPAYRVLMEQLTSVSEELDVrkeevliLRSQLVSQkeaiQPkddkntmtdstilleDVQKMKDKgeiaqay 1312
Cdd:COG3206 253 PDALPELLQSPVIQQLRAQLAELEAELAE-------LSARYTPN----HP---------------DVIALRAQ------- 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1542868643 1313 igLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNlqlpPEARIE-ASLQHEITrlTNENLY 1387
Cdd:COG3206 300 --IAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL----PELEAElRRLEREVE--VARELY 367
|
|
| CBD_MYO6-like |
cd21759 |
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ... |
810-835 |
6.56e-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: 39.03 E-value: 6.56e-03
10 20
....*....|....*....|....*.
gi 1542868643 810 KFLRRTKAATIIQKYWRMYVARRRYK 835
Cdd:cd21759 40 KILYRREALIKIQKTVRGYLARKKHR 65
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
928-1177 |
6.64e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.40 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 928 KIMQLQRKVDEQNKDYKCLMEKLtnlegiynSETEKLRSDLE--------RLQLSEEEAKIATGRVLSLQEEIAKLRKDL 999
Cdd:pfam00261 2 KMQQIKEELDEAEERLKEAMKKL--------EEAEKRAEKAEaevaalnrRIQLLEEELERTEERLAEALEKLEEAEKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1000 EQTQSEKKSIEEHAdrykqeteqlvsnLKEENTLLKQEKEvlnhriVEQAKEMTETMEKKLVEETKQL-----ELDLNDE 1074
Cdd:pfam00261 74 DESERGRKVLENRA-------------LKDEEKMEILEAQ------LKEAKEIAEEADRKYEEVARKLvvvegDLERAEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1075 RLRyqnllnefsRLEERYDDLKEEMTLMVNVPK----PGHKRTDSTHSSNESEYTFSSEIAETEDipsRTEEpSEKKVPl 1150
Cdd:pfam00261 135 RAE---------LAESKIVELEEELKVVGNNLKsleaSEEKASEREDKYEEQIRFLTEKLKEAET---RAEF-AERSVQ- 200
|
250 260 270
....*....|....*....|....*....|....
gi 1542868643 1151 dmslflKLQKRVTELEQE-------KQVMQDELD 1177
Cdd:pfam00261 201 ------KLEKEVDRLEDEleaekekYKAISEELD 228
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1177-1503 |
6.69e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1177 DRKEEQVLRSKAKEEERPQIRGAELEYESLKRQELESENKKLKNELNELRKALSEKSapevtapgapayrvlmEQLTSVS 1256
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAR----------------EELEQLE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1257 EELDVRKEEVLILRSQLVSQKEAIQPKDDKNTMTDSTILLEDVQKMKDKGEIAQA---YIGLKETNRLLESQ---LQSQK 1330
Cdd:COG4372 66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELqkeRQDLEQQRKQLEAQiaeLQSEI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1331 RSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNEnlyfEELYADDPKKYQSYRISLYKRM 1410
Cdd:COG4372 146 AEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKE----EELAEAEKLIESLPRELAEELL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1411 IDLMEQLEKQDKTVRKLKKQ--LKVFAKKIGELEVGQMENISPGQIIDEPIRPVNIPRKEKDFQGMLEYKKEDEQKLVKN 1488
Cdd:COG4372 222 EAKDSLEAKLGLALSALLDAleLEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALL 301
|
330
....*....|....*
gi 1542868643 1489 LILELKPRGVAVNLI 1503
Cdd:COG4372 302 LNLAALSLIGALEDA 316
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
12-49 |
7.22e-03 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 36.25 E-value: 7.22e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1542868643 12 RVWIPDPEEVWKSAELLKdyKPGDKVlLLQLEDGKDLE 49
Cdd:pfam02736 5 LVWVPDPKEGFVKGEIKE--EEGDKV-TVETEDGKTVT 39
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
910-1219 |
8.52e-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: 41.19 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 910 IEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKC-LMEKLTNLEGIYNSETEKLRS---DLERLQLSEEEAKIATGRV 985
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACeIRDQITSKEAQLESSREIVKSyenELDPLKNRLKEIEHNLSKI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 986 LSLQEEIA----------KLRKDLEQ--------TQSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEVLNHRIVE 1047
Cdd:TIGR00606 265 MKLDNEIKalksrkkqmeKDNSELELkmekvfqgTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1048 QAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFsrleERYDDLKEEMTLMVNVPKPGHKRTDSTHSSNESEYTFS 1127
Cdd:TIGR00606 345 LLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGF----ERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSK 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1128 SEIAETEdipsrTEEPSEKKVPLDMSLFLK---LQKRVTELEQEKQVMQ------DELDRKEEQVLRSKA---KEEERPQ 1195
Cdd:TIGR00606 421 ERLKQEQ-----ADEIRDEKKGLGRTIELKkeiLEKKQEELKFVIKELQqlegssDRILELDQELRKAERelsKAEKNSL 495
|
330 340
....*....|....*....|....
gi 1542868643 1196 IRGAELEYESLKRQELESENKKLK 1219
Cdd:TIGR00606 496 TETLKKEVKSLQNEKADLDRKLRK 519
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
987-1077 |
8.65e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.09 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 987 SLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQET---EQLVSNLKEENTLLKQEKEVLNHRIVEQAKEMTETMEKKLVEE 1063
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELvalEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEITDQA 225
|
90 100
....*....|....*....|
gi 1542868643 1064 TKQLELD------LNDERLR 1077
Cdd:PRK11448 226 AKRLELSeeetriLIDQQLR 245
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
862-879 |
9.12e-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: 9.12e-03
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
988-1231 |
9.49e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 988 LQEEIAKLRKDLEQTQSEKKSIEEHADRYKQETEQLVSNLKEentllkqekevlnhrIVEQAKEMTETMeKKLVEETKQl 1067
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE---------------LREEAQELREKR-DELNEKVKE- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1068 eldLNDERlryQNLLNEFSRLEERYDDLKEEMtlmvnvpkpghkrtDSTHSSNESEYTFSSEIAETEDipsrteepsekk 1147
Cdd:COG1340 76 ---LKEER---DELNEKLNELREELDELRKEL--------------AELNKAGGSIDKLRKEIERLEW------------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1148 vpldmslflKLQKRVTELEQEKQVMqDELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQ--ELESENKKLKNELNEL 1225
Cdd:COG1340 124 ---------RQQTEVLSPEEEKELV-EKIKELEKELEKAKKALEKNEKLKELRAELKELRKEaeEIHKKIKELAEEAQEL 193
|
....*.
gi 1542868643 1226 RKALSE 1231
Cdd:COG1340 194 HEEMIE 199
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
943-1072 |
9.70e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.05 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 943 YKCLMEKLTNLEGIYNSET-EKLRSDLerLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTQSEKKSIEEHADRYKQ--E 1019
Cdd:cd22656 93 YAEILELIDDLADATDDEElEEAKKTI--KALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDllT 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1542868643 1020 TEQLVSNLKEENTLLKQEKEvLNHRIVEQAKEMTETMEKKLVEETKQLELDLN 1072
Cdd:cd22656 171 DEGGAIARKEIKDLQKELEK-LNEEYAAKLKAKIDELKALIADDEAKLAAALR 222
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
928-1082 |
9.73e-03 |
|
Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.
Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 39.18 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 928 KIMQLQrkVDEQNKDYKCLMEKLTNLEGiYNSETEKLRSDLERLqlseeeakiatgrvLSLQEEIAKLrkdLEQTQSEKK 1007
Cdd:pfam05266 57 KVKKLQ--VDDSRSVFESLMESFAELEK-HGFDVKAPQSRINKL--------------LSLKDRQTKL---LEELKKLEK 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1542868643 1008 SIEEHADRyKQETEQLVSNLkEENTLLKQEKEVLnhriveqAKEMTETMEKKLVE---ETKQLELDLNDERLRYQNLL 1082
Cdd:pfam05266 117 KIAEEESE-KRKLEEEIDEL-EKKILELERQLAL-------AKEKKEAADKEIARlksEAEKLEQEIQDVELEFEATA 185
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
925-1101 |
9.93e-03 |
|
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: 40.77 E-value: 9.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 925 MENKIMQLQRKVDEQNKDYKCLMEKLTNLEGIYNseteKLRSDLERLQlseEEAKIATGRVLSLQEEIAKLR---KDLEQ 1001
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN----KIKQNLEQKQ---KELKSKEKELKKLNEEKKELEekvKDLTK 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542868643 1002 TQSEKKSIEEHADRYKQETEQLVSNLKEE---------NTLLKQEKEVLNHRIvEQAKEMTETMEKKlveeTKQLELDLN 1072
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDElnkddfelkKENLEKEIDEKNKEI-EELKQTQKSLKKK----QEEKQELID 592
|
170 180
....*....|....*....|....*....
gi 1542868643 1073 DERLRYQNLLNEFSRLEERYDDLKEEMTL 1101
Cdd:TIGR04523 593 QKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| |
