|
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: 1317.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd01380 1 PAVLHNLKVRFCQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 163 GESGAGKTVSAKYAMRYFATVSGSAS-EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATVGGSSSgETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 242 YLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISESY 321
Cdd:cd01380 161 YLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 322 QMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQATNARD 401
Cdd:cd01380 241 QMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 402 ALAKHIYAKLFNWIVDHVNQALHSAV--KQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 479
Cdd:cd01380 321 ALAKHIYAQLFDWIVDRINKALASPVkeKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 480 EQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNK-CALFEKPRLSNKAFIIQHFADKVE 558
Cdd:cd01380 401 EEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTAFIVKHFADDVE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 559 YQCEGFLEKNKDTVFEEQIKVLKSSKFkmlpelfqddekavsptsatssgrtpltrtpskptkgrpgqtakeHKKTVGHQ 638
Cdd:cd01380 481 YQVEGFLEKNRDTVSEEHLNVLKASKN---------------------------------------------RKKTVGSQ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 639 FRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKD 718
Cdd:cd01380 516 FRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKE 595
|
650 660 670
....*....|....*....|....*....|....
gi 2015234411 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: 1079.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 72 NDLTALSYLHEPAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMA 151
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRY-KSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 152 RDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEAN---VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGF 228
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNvgrLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 229 DKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPVIEGVDDAKEMAHT 308
Cdd:pfam00063 161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 309 RQACTLLGISESYQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYI 388
Cdd:pfam00063 241 DKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETVS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 389 KPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHS-AVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNM 467
Cdd:pfam00063 321 KPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVkTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 468 HVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKPRL-SN 545
Cdd:pfam00063 401 HMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKpLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHFQKPRLqGE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 546 KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAVSPTSATSSgrtpltrtpskptKGRPG 625
Cdd:pfam00063 480 THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESG-------------KSTPK 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 626 QTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:pfam00063 547 RTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQE 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2015234411 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: 1018.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 64 NPDILVGENDLTALSYLHEPAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVA 143
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRY-LKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 144 EEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEAN-VEEKVLASNPIMESIGNAKTTRNDNSSRFGK 222
Cdd:smart00242 80 DNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGsVEDQILESNPILEAFGNAKTLRNNNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 223 YIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPVIEGVDDA 302
Cdd:smart00242 160 FIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 303 KEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVVFMSRDSD-SCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLA 381
Cdd:smart00242 240 EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDnAASTVKDKEELSNAAELLGVDPEELEKALTKRKIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 382 TATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKL 461
Cdd:smart00242 320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 462 QQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEK 540
Cdd:smart00242 400 QQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKpPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFSKP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 541 PRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkavsptsatssgrtpltrtPSKPT 620
Cdd:smart00242 480 KKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGV-------------------SNAGS 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 621 KGRPgqtakehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSR 700
Cdd:smart00242 541 KKRF--------QTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYR 612
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2015234411 701 WTYQEFFSRYRVLMKQK--DVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFRAGQVAYLEKLR 762
Cdd:smart00242 613 LPFDEFLQRYRVLLPDTwpPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
7-1234 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 965.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 7 YTKFARVWIPDPEEVWKSAELLK-DYKPGDKVLLLHLEDG-------KDLEYRLDpktkelphlrNPDILVGENDLTALS 78
Cdd:COG5022 6 AEVGSGCWIPDEEKGWIWAEIIKeAFNKGKVTEEGKKEDGesvsvkkKVLGNDRI----------KLPKFDGVDDLTELS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 79 YLHEPAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQS 158
Cdd:COG5022 76 YLNEPAVLHNLEKRY-NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 159 IIVSGESGAGKTVSAKYAMRYFATVSGSASE--ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIG 236
Cdd:COG5022 155 IIISGESGAGKTENAKRIMQYLASVTSSSTVeiSSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 237 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLG 316
Cdd:COG5022 235 AKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 317 ISESYQMGIFRILAGILHLGNVVFMSrDSDSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQA 396
Cdd:COG5022 315 IDEEEQDQIFKILAAILHIGNIEFKE-DRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 397 TNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:COG5022 394 LAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEE 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 477 YMKEQIPWTLIDFYDNQPCINLIESK--LGILDLLDEECKMPKGTDDTWAQKLYNT-HLNKCALFEKPRLSNKAFIIQHF 553
Cdd:COG5022 474 YVKEGIEWSFIDYFDNQPCIDLIEKKnpLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNKFVVKHY 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 554 ADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAVSptsatssgrtpltrtpskptKGRPgqtakehkK 633
Cdd:COG5022 554 AGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIES--------------------KGRF--------P 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 634 TVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVL 713
Cdd:COG5022 606 TLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRIL 685
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 714 MKQK------DVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFRAGQVAYLEKLRADKLRAACIRIQKTIRGWLLRKKYL 787
Cdd:COG5022 686 SPSKswtgeyTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYL 765
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 788 RMRKAAITVQRYVRGHQARCYAKFLRRTKAATIIQKYWRMYVARRRYKIMRTAAIVLQSYL-RGYLARNRYHKILREHKA 866
Cdd:COG5022 766 QALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIkREKKLRETEEVEFSLKAE 845
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 867 VIIQKWVRGWLARTYYRRSIHAIIYLQCCFRRMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQ-NKDYKC 945
Cdd:COG5022 846 VLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDlIENLEF 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 946 LMEKLTNLEGTYNSETEKLRSDLERLQLSEeeakiatgrVLSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQLVS 1025
Cdd:COG5022 926 KTELIARLKKLLNNIDLEEGPSIEYVKLPE---------LNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKN 996
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1026 NLKEENTLLKQ------EKEALNHRIVEQAKEMTETMEKKLVEETKQLELDLNDERlryQNLLNEFSRLEERYDDLKeem 1099
Cdd:COG5022 997 FKKELAELSKQygalqeSTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLK---GLLLLENNQLQARYKALK--- 1070
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1100 tlmvnVPKPGHKRTDSTHSSNESEYTFSSEIAETE----DIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQ-----EKQ 1170
Cdd:COG5022 1071 -----LRRENSLLDDKQLYQLESTENLLKTINVKDlevtNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQlvntlEPV 1145
|
1210 1220 1230 1240 1250 1260
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2015234411 1171 VMQDELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQE--LESENKKLKNELNELRKALSEKSS 1234
Cdd:COG5022 1146 FQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSalYDEKSKLSSSEVNDLKNELIALFS 1211
|
|
| 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: 880.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMG-DMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd00124 1 AAILHNLRERY-ARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 162 SGESGAGKTVSAKYAMRYFATVSGSAS------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRII 235
Cdd:cd00124 80 SGESGAGKTETTKLVLKYLAALSGSGSskssssASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 236 GANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANN----FHYTNQGGSPVIEGVDDAKEMAHTRQA 311
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSyyylNDYLNSSGCDRIDGVDDAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 312 CTLLGISESYQMGIFRILAGILHLGNVVFMSRDSD--SCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIK 389
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 390 PISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQH--SFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNM 467
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 468 HVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNK 546
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKpLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAKL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 547 AFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKfkmlpelfqddekavsptsatssgrtpltrtpskptkgrpgq 626
Cdd:cd00124 480 EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS------------------------------------------ 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 627 takehkktvghQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEF 706
Cdd:cd00124 518 -----------QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEF 586
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2015234411 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: 792.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd01377 1 ASVLHNLRERY-YSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 163 GESGAGKTVSAKYAMRYFATVSGSA--------SEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRI 234
Cdd:cd01377 80 GESGAGKTENTKKVIQYLASVAASSkkkkesgkKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 235 IGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTL 314
Cdd:cd01377 160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 315 LGISESYQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPISKL 394
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 395 QATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 474
Cdd:cd01377 320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 475 EEYMKEQIPWTLIDF-YDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR--LSNKAFII 550
Cdd:cd01377 400 EEYKKEGIEWTFIDFgLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKpkKSEAHFIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 551 QHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAVSPTSATSSGRTPLtrtpskptkgrpgqtake 630
Cdd:cd01377 480 KHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGGGKKKKKGGSF------------------ 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 631 hkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRY 710
Cdd:cd01377 542 --RTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRY 619
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 2015234411 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: 768.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd01384 1 PGVLHNLKVRY-ELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 162 SGESGAGKTVSAKYAMRYFATVSGSAS--EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANM 239
Cdd:cd01384 80 SGESGAGKTETTKMLMQYLAYMGGRAVteGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 240 RTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISE 319
Cdd:cd01384 160 RTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 320 SYQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEP---LSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQA 396
Cdd:cd01384 240 EEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSefhLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 397 TNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:cd01384 320 TLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 477 YMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNThLNKCALFEKPRLSNKAFIIQHFAD 555
Cdd:cd01384 400 YTKEEIDWSYIEFVDNQDVLDLIEKKpGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKPKLSRTDFTIDHYAG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekAVSPTSATSSGrtpltrtpSKPTkgrpgqtakehkkTV 635
Cdd:cd01384 479 DVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLF-----PPLPREGTSSS--------SKFS-------------SI 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK 715
Cdd:cd01384 533 GSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAP 612
|
650 660 670
....*....|....*....|....*....|....*..
gi 2015234411 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: 754.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 84 AVLHNLRVRFIDsKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd01381 2 GILRNLLIRYRE-KLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 164 ESGAGKTVSAKYAMRYFATVSGSASEanVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYL 243
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHSW--IEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 244 LEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISESYQM 323
Cdd:cd01381 159 LEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 324 GIFRILAGILHLGNVVFMSRDS---DSCTIpPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQATNAR 400
Cdd:cd01381 239 DIFKLLAAILHLGNIKFEATVVdnlDASEV-RDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 401 DALAKHIYAKLFNWIVDHVNQALHSAVKQHSF---IGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEY 477
Cdd:cd01381 318 DAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 478 MKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPR-LSNKAFIIQHFAD 555
Cdd:cd01381 398 DKEGINWQHIEFVDNQDVLDLIALKpMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNN-KNYLKPKsDLNTSFGINHFAG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkavsPTSATSSGRTPltrtpskptkgrpgqtakehkkTV 635
Cdd:cd01381 477 VVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDI----SMGSETRKKSP----------------------TL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK 715
Cdd:cd01381 531 SSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP 610
|
650 660 670
....*....|....*....|....*....|....*...
gi 2015234411 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: 734.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDmdPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd01383 1 PSVLHNLEYRY-SQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKLLDS--PHVYAVADTAYREMMRDEINQSIIIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 163 GESGAGKTVSAKYAMRYFATVSGSASeaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTY 242
Cdd:cd01383 78 GESGAGKTETAKIAMQYLAALGGGSS--GIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 243 LLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISESYQ 322
Cdd:cd01383 156 LLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKEDQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 323 MGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQATNARDA 402
Cdd:cd01383 236 EHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 403 LAKHIYAKLFNWIVDHVNQALHSAVKQHS-FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQ 481
Cdd:cd01383 316 LAKAIYASLFDWLVEQINKSLEVGKRRTGrSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 482 IPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLyNTHLNKCALFEKPRlsNKAFIIQHFADKVEYQ 560
Cdd:cd01383 396 IDWTKVDFEDNQECLDLIEKKpLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCFKGER--GGAFTIRHYAGEVTYD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 561 CEGFLEKNKDTVFEEQIKVLKSSKFKmLPELF-----QDDEKAVSPTSATSSGRTpltrtpskptkgrpgqtakehKKTV 635
Cdd:cd01383 473 TSGFLEKNRDLLHSDLIQLLSSCSCQ-LPQLFaskmlDASRKALPLTKASGSDSQ---------------------KQSV 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLM- 714
Cdd:cd01383 531 ATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLp 610
|
650 660 670
....*....|....*....|....*....|....*..
gi 2015234411 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: 726.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14883 2 GINTNLKVRY-KKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 164 ESGAGKTVSAKYAMRYFATVSGSASEanVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYL 243
Cdd:cd14883 81 ESGAGKTETTKLILQYLCAVTNNHSW--VEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 244 LEKSRVVFQAEEERNYHIFYQLCASANL-PEFKA-LRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISESY 321
Cdd:cd14883 159 LEQSRITFQAPGERNYHVFYQLLAGAKHsKELKEkLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPEEM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 322 QMGIFRILAGILHLGNVVFMSRDSDSCTIPPKH-EPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQATNAR 400
Cdd:cd14883 239 QEGIFSVLSAILHLGNLTFEDIDGETGALTVEDkEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 401 DALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKE 480
Cdd:cd14883 319 DAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 481 QIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKP--RLSNKAFIIQHFADKV 557
Cdd:cd14883 399 GINWSHIVFTDNQECLDLIEKPpLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPdrRRWKTEFGVKHYAGEV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 558 EYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQ-DDEKAVSPTSATSSGRTPLTRTpskpTKGRPgqtakehkkTVG 636
Cdd:cd14883 478 TYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTyPDLLALTGLSISLGGDTTSRGT----SKGKP---------TVG 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 637 HQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQ 716
Cdd:cd14883 545 DTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPR 624
|
650 660 670
....*....|....*....|....*....|....*..
gi 2015234411 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, ... |
1503-1877 |
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 2015234411 1503 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 1582
Cdd:cd15478 1 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1583 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 1662
Cdd:cd15478 81 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1663 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAVTLNNLLLRKDMCSWSKGMQIR 1742
Cdd:cd15478 161 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1743 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 1822
Cdd:cd15478 241 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2015234411 1823 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 1877
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: 708.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd01378 2 AINENLKKRF-ENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 164 ESGAGKTVSAKYAMRYFATVSGSaSEANVE---EKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMR 240
Cdd:cd01378 81 ESGAGKTEASKRIMQYIAAVSGG-SESEVErvkDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHIT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 241 TYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISES 320
Cdd:cd01378 160 NYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 321 YQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKhEPLSIFCDLMGVAFEEMSHWLCHRKLATATE---TYIKPISKLQAT 397
Cdd:cd01378 240 EQDSIFRILAAILHLGNIQFAEDEEGNAAISDT-SVLDFVAYLLGVDPDQLEKALTHRTIETGGGgrsVYEVPLNVEQAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 398 NARDALAKHIYAKLFNWIVDHVNQALHSAVKQHS-FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:cd01378 319 YARDALAKAIYSRLFDWIVERINKSLAAKSGGKKkVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 477 YMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECK-MPKGTDDTWAQKLyNTHLNKCALFEKP----RLSNKAFII 550
Cdd:cd01378 399 YVREGIEWTPIKYFNNKIICDLIEEKpPGIFAILDDACLtAGDATDQTFLQKL-NQLFSNHPHFECPsghfELRRGEFRI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 551 QHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAVSptsatssgrtpltrtpskptKGRPgqtake 630
Cdd:cd01378 478 KHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDS--------------------KKRP------ 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 631 hkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRY 710
Cdd:cd01378 532 --PTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERY 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 2015234411 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, ... |
1503-1874 |
0e+00 |
|
Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. They interact with several adaptor proteins, in case of Myo5b-CBD, Rab11-family interacting protein 2.
Pssm-ID: 271261 Cd Length: 372 Bit Score: 647.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1503 KEDEQKLVKNLILELKPRGVAVNlIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 1582
Cdd:cd15477 1 KEDEALLIRNLVTDLKPQAVSAT-VPCLPAYILYMCIRHADYINDDQKVHSLLTSTINGIKKVLKKHNDDFEMTSFWLAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1583 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 1662
Cdd:cd15477 80 TCRLLHCLKQYSGDEGFMTQNTAKQNEHCLKNFDLTEYRQVLSDLSIQIYQQLIKIAEGILQPMIVSAMLENESIQGLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1663 VKPTGLRKRTSSIAD-EGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAVTLNNLLLRKDMCSWSKGMQI 1741
Cdd:cd15477 160 VKPMGYRKRSSSMADgDNSYTLEALIRQLNTFHSIMCDQGLDPEIIQQVFKQLFYMINAVTLNNLLLRKDVCSWSTGMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1742 RYNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVS 1821
Cdd:cd15477 240 RYNISQLEEWLRGRNLHQSGAAQTMEPLIQAAQLLQLKKKTSEDAEAICSLCTALSTQQIVKILNLYTPLNEFEERVTVS 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2015234411 1822 FIRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFI 1874
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: 639.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14903 1 AAILYNVKKRFL-RKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 162 SGESGAGKTVSAKYAMRYFATVSGSASEANVEeKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:cd14903 80 SGESGAGKTETTKILMNHLATIAGGLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 242 YLLEKSRVVFQAEEERNYHIFYQLCASANLPEfkALRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISESY 321
Cdd:cd14903 159 YLLEKTRVISHERPERNYHIFYQLLASPDVEE--RLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 322 QMGIFRILAGILHLGNVVFMSRDSD--SCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQATNA 399
Cdd:cd14903 237 QEVLFEVLAGILHLGQLQIQSKPNDdeKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDC 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 400 RDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 479
Cdd:cd14903 317 RDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 480 EQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKAFIIQHFADKVEY 559
Cdd:cd14903 397 EGIRWAHIDFADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSRTQFTIKHYAGPVTY 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 560 QCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqdDEKAVSPTSATSSGRTPltrtpskptkGRPGQTAKEHKKTVGHQF 639
Cdd:cd14903 477 ESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLF--KEKVESPAAASTSLARG----------ARRRRGGALTTTTVGTQF 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 640 RNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQK-D 718
Cdd:cd14903 545 KDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGrN 624
|
650 660 670
....*....|....*....|....*....|....
gi 2015234411 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: 629.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14872 1 AMIVHNLRKRFKNDQ-IYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 163 GESGAGKTVSAKYAMRYFATVSGSASeaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTY 242
Cdd:cd14872 80 GESGAGKTEATKQCLSFFAEVAGSTN--GVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 243 LLEKSRVVFQAEEERNYHIFYQLCASAnlPEFKALRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISESYQ 322
Cdd:cd14872 158 LLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFDDADI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 323 MGIFRILAGILHLGNVVF---MSRDSDSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLAT-ATETYIKPISKLQATN 398
Cdd:cd14872 236 NNVMSLIAAILKLGNIEFasgGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLTPAQATD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 399 ARDALAKHIYAKLFNWIVDHVNQALHSA-VKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEY 477
Cdd:cd14872 316 ACDALAKAAYSRLFDWLVKKINESMRPQkGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEALY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 478 MKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTH-LNKCALFEKPRLSNKAFIIQHFAD 555
Cdd:cd14872 396 QSEGVKFEHIDFIDNQPVLDLIEKKQpGLMLALDDQVKIPKGSDATFMIAANQTHaAKSTFVYAEVRTSRTEFIVKHYAG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkavsptsatssgrtpltrtPSKPTKgrpgqtakehKKTV 635
Cdd:cd14872 476 DVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSE-------------------GDQKTS----------KVTL 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK 715
Cdd:cd14872 527 GGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVK 606
|
650 660 670
....*....|....*....|....*....|....*...
gi 2015234411 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: 626.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 86 LHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGES 165
Cdd:cd01385 4 LENLRARFKHGK-IYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 166 GAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLE 245
Cdd:cd01385 83 GSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 246 KSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISESYQMGI 325
Cdd:cd01385 163 KSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQRQI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 326 FRILAGILHLGNVVFMSRD---SDSCTIPPKhEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQATNARDA 402
Cdd:cd01385 243 FSVLSAVLHLGNIEYKKKAyhrDESVTVGNP-EVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 403 LAKHIYAKLFNWIVDHVNQAL----HSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYM 478
Cdd:cd01385 322 MAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 479 KEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKlYNTHLNKCALFEKPRLSNKAFIIQHFADKV 557
Cdd:cd01385 402 KEGISWHNIEYTDNTGCLQLISKKpTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQVMEPAFIIAHYAGKV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 558 EYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAV-----------------SPTSATSSGRTPLTRTPSKP- 619
Cdd:cd01385 481 KYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVAVfrwavlrafframaafrEAGRRRAQRTAGHSLTLHDRt 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 620 TKGRPGQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPS 699
Cdd:cd01385 561 TKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSV 640
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2015234411 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: 621.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 86 LHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 164
Cdd:cd01382 4 LNNIRVRYSKDK-IYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 165 SGAGKTVSAKYAMRYFATVSGSASeANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 244
Cdd:cd01382 83 SGAGKTESTKYILRYLTESWGSGA-GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 245 EKSRVVFQAEEERNYHIFYQLCASANLPEFKALrLGDANnfhytnqggspviegVDDAKEMAHTRQACTLLGISESYQMG 324
Cdd:cd01382 162 EKSRICVQSKEERNYHIFYRLCAGAPEDLREKL-LKDPL---------------LDDVGDFIRMDKAMKKIGLSDEEKLD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 325 IFRILAGILHLGNVVFMSRDSDS---CTIPPKHEP-LSIFCDLMGVAFEEMSHWLCHRKLATATE----TYIK-PISKLQ 395
Cdd:cd01382 226 IFRVVAAVLHLGNIEFEENGSDSgggCNVKPKSEQsLEYAAELLGLDQDELRVSLTTRVMQTTRGgakgTVIKvPLKVEE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 396 ATNARDALAKHIYAKLFNWIVDHVNQAL---HSAvkqhSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKL 472
Cdd:cd01382 306 ANNARDALAKAIYSKLFDHIVNRINQCIpfeTSS----YFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 473 EQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPRLS------- 544
Cdd:cd01382 382 EQELYEKEGLGVKEVEYVDNQDCIDLIEAKLvGILDLLDEESKLPKPSDQHFTSAVHQKHKNH-FRLSIPRKSklkihrn 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 545 ---NKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkAVSPTSATSSGRTPLtrtpskptk 621
Cdd:cd01382 461 lrdDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESST-NNNKDSKQKAGKLSF--------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 622 grpgqtakehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRW 701
Cdd:cd01382 531 -----------ISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRT 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 2015234411 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, ... |
1504-1870 |
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: 616.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1504 EDEQKLVKNLILELKPRGvAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNT 1583
Cdd:cd15470 1 EDESRLIKNLITDLKPRG-AVGLLPGLPAYILFMCIRHADYVNDEAKVRSLLTATINAIKKVLKKHSEDFEMLSFWLVNT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1584 CRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmivsgmlehetiqgvsgv 1663
Cdd:cd15470 80 CRLLNCLKQYSGEEEFMKHNTPKQNEHCLKNFDLSEYRQVLSDLAIQIYQQLIKRAEEILQP------------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1664 kptglrkrtssiadegtyTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAVTLNNLLLRKDMCSWSKGMQIRY 1743
Cdd:cd15470 142 ------------------TLDSLLQQLNSFHTTLTQHGLDPELIKQVFRQLFYLICASTLNNLLLRKDLCSWSKGMQIRY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1744 NVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFI 1823
Cdd:cd15470 204 NVSQLEEWLRDKGLQDSGARETLEPLIQAAQLLQVKKTTEEDAQSICEMCTKLTTAQIVKILNLYTPVDDFEERVTPSFI 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2015234411 1824 RTIQMRLRDRKDSP--QLLMDAKHIFPVTFPFNPSSLALETIQIPASLG 1870
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: 612.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd01387 2 TVLWNLKTRY-ERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 164 ESGAGKTVSAKYAMRYFATVSGSAsEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMRTYL 243
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRR-NNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAITSQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 244 LEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISESYQM 323
Cdd:cd01387 159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 324 GIFRILAGILHLGNVVFMSRDSDSctippKHEPLSIFCD--------LMGVAFEEMSHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd01387 239 SIFRILASVLHLGNVYFHKRQLRH-----GQEGVSVGSDaeiqwvahLLQISPEGLQKALTFKVTETRRERIFTPLTIDQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQE 475
Cdd:cd01387 314 ALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 476 EYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKL-YNTHLNKcaLFEKPRLSNKAFIIQHF 553
Cdd:cd01387 394 EYIREQIDWTEIAFADNQPVINLISKKpVGILHILDDECNFPQATDHSFLEKChYHHALNE--LYSKPRMPLPEFTIKHY 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 554 ADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekavsptsatssgRTPLTRTPSKPTKGRpGQTAKEHKK 633
Cdd:cd01387 472 AGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSH-------------RAQTDKAPPRLGKGR-FVTMKPRTP 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 634 TVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVL 713
Cdd:cd01387 538 TVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 2015234411 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: 601.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 84 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14873 2 SIMYNLFQRYKRNQ-IYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 163 GESGAGKTVSAKYAMRYFATVS-------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRII 235
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISqqslelsLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 236 GANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLL 315
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 316 GISESYQMGIFRILAGILHLGNVVFMSrdSDSCTIPPKhEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEFIT--AGGAQVSFK-TALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAvKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQE 475
Cdd:cd14873 318 AVDSRDSLAMALYARCFEWVIKKINSRIKGK-EDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 476 EYMKEQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPRLSNKAFIIQHFAD 555
Cdd:cd14873 397 EYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANN-HFYVKPRVAVNNFGVKHYAG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekavsptSATSSGRTpltrtpskptkgrPGQTAKEHKKTV 635
Cdd:cd14873 476 EVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHV-------SSRNNQDT-------------LKCGSKHRRPTV 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK 715
Cdd:cd14873 536 SSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMR 615
|
650 660 670
....*....|....*....|....*....|....*.
gi 2015234411 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: 596.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMAR----DERNQS 158
Cdd:cd14890 2 SLLHTLRLRY-ERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 159 IIVSGESGAGKTVSAKYAMRYFATVS-----------------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFG 221
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITsgfaqgasgegeaaseaIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 222 KYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTnQGGSPVIEGVDD 301
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYL-RGECSSIPSCDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 302 AKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVVF-MSRDSDSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKL 380
Cdd:cd14890 240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFeSENDTTVLEDATTLQSLKLAAELLGVNEDALEKALLTRQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 381 ATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEK 460
Cdd:cd14890 320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 461 LQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL----GILDLLDeECKMPKGTDdtwAQKLYNTHLNkcA 536
Cdd:cd14890 400 LQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVngkpGIFITLD-DCWRFKGEE---ANKKFVSQLH--A 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 537 LFEKPRLSNKA--------------------FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSkfkmlpelfqdde 596
Cdd:cd14890 474 SFGRKSGSGGTrrgssqhphfvhpkfdadkqFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQS------------- 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 597 kavsptsaTSSGRtpltrtpskptkgrpgqtakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKR 676
Cdd:cd14890 541 --------RRSIR----------------------EVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLD 590
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2015234411 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: 589.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAY---SGQNMGD---MDPHIFAVAEEAYKQMARDER- 155
Cdd:cd14901 1 PSILHVLRRRF-AHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehGERRAAGerkLPPHVYAVADKAFRAMLFASRg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 156 ---NQSIIVSGESGAGKTVSAKYAMRYFATVS-------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIE 225
Cdd:cd14901 80 qkcDQSILVSGESGAGKTETTKIIMNYLASVSsatthgqNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 226 IGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPV-IEGVDDAKE 304
Cdd:cd14901 160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDrRDGVDDSVQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 305 MAHTRQACTLLGISESYQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEP-LSIFCDLMGVAFEEMSHWLCHRKLATA 383
Cdd:cd14901 240 YAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLAnVRAACDLLGLDMDVLEKTLCTREIRAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 384 TETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQAL--HSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKL 461
Cdd:cd14901 320 GEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIaySESTGASRFIGIVDIFGFEIFATNSLEQLCINFANEKL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 462 QQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNThLNKCALFEK 540
Cdd:cd14901 400 QQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARpTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHASFSV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 541 PRLSN--KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPelfqddekavsptsatssgrtpltrtpsk 618
Cdd:cd14901 479 SKLQQgkRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS----------------------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 619 ptkgrpgqtakehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFP 698
Cdd:cd14901 530 --------------STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYP 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 2015234411 699 SRWTYQEFFSRYRVLMKQK-------DVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIF 749
Cdd:cd14901 596 VRFPHDAFVHTYSCLAPDGasdtwkvNELAERLMSQLQHSELNIEHLPPFQVGKTKVF 653
|
|
| 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: 566.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 89 LRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGE--DIINAYSGQNMGDMD-PHIFAVAEEAYKQMARD----ERNQSIIV 161
Cdd:cd14892 7 LRRRY-ERDAIYTFTADILISINPYKSIPLLYDvpGFDSQRKEEATASSPpPHVFSIAERAYRAMKGVgkgqGTPQSIVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 162 SGESGAGKTVSAKYAMRYFATVSGSASEA-----------NVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDK 230
Cdd:cd14892 86 SGESGAGKTEASKYIMKYLATASKLAKGAstskgaanaheSIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 231 RYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQ 310
Cdd:cd14892 166 DGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVDGVDDATEFKQLRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 311 ACTLLGISESYQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEP--LSIFCDLMGVAFEEMSHWLCHRKLATATETYI 388
Cdd:cd14892 246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGvnVAKAAGLLGVDAAELMFKLVTQTTSTARGSVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 389 K-PISKLQATNARDALAKHIYAKLFNWIVDHVNqALHSAV-----------KQHSFIGVLDIYGFETFEINSFEQFCINY 456
Cdd:cd14892 326 EiKLTAREAKNALDALCKYLYGELFDWLISRIN-ACHKQQtsgvtggaaspTFSPFIGILDIFGFEIMPTNSFEQLCINF 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 457 ANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMP-KGTDDTWAQKLYNTHLNK 534
Cdd:cd14892 405 TNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKpLGLLPLLEEQMLLKrKTTDKQLLTIYHQTHLDK 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 535 CALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKfkmlpelfqddekavsptsatssgrtpltr 614
Cdd:cd14892 485 HPHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS------------------------------ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 615 tpskptkgrpgqtakehkktvghQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISA 694
Cdd:cd14892 535 -----------------------KFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRR 591
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2015234411 695 AGFPSRWTYQEFFSRYRVLMKQK----------DVLSDRKQTCKNVLEKLivDKDKYQFGKTKIFFR 751
Cdd:cd14892 592 EGFPIRRQFEEFYEKFWPLARNKagvaaspdacDATTARKKCEEIVARAL--ERENFQLGRTKVFLR 656
|
|
| 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: 564.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSgQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14888 1 ASILHSLNLRF-DIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 162 SGESGAGKTVSAKYAMRYFATVsGSASE---ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDK-------- 230
Cdd:cd14888 79 SGESGAGKTESTKYVMKFLACA-GSEDIkkrSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskrmsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 231 -RYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASA-------NLPEFKALRLGDANN----------------FH 286
Cdd:cd14888 158 dRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAreakntgLSYEENDEKLAKGADakpisidmssfephlkFR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 287 YTNQGGSPVIEGVDDAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVVFM-SRDSDSCTI--PPKHEPLSIFCDL 363
Cdd:cd14888 238 YLTKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFEnNEACSEGAVvsASCTDDLEKVASL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 364 MGVAFEEMSHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQAL-HSAVKQHSFIGVLDIYGFE 442
Cdd:cd14888 318 LGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIgYSKDNSLLFCGVLDIFGFE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 443 TFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDD 521
Cdd:cd14888 398 CFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKpLGIFCMLDEECFVPGGKDQ 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 522 TWAQKLYNTHLNKcALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQddekavsp 601
Cdd:cd14888 478 GLCNKLCQKHKGH-KRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFS-------- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 602 tsatssgrtpltrtpSKPTKGRPGQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQL 681
Cdd:cd14888 549 ---------------AYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQL 613
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 682 RACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkqkdvlsdRKQTCKNVLEklivdkdkYQFGKTKIFFR 751
Cdd:cd14888 614 KYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILL--------NGEGKKQLSI--------WAVGKTLCFFK 667
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
83-751 |
0e+00 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 561.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFIDSkLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd01379 1 DTIVSQLQKRYSRD-QIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 163 GESGAGKTVSAKYAMRYFaTVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTY 242
Cdd:cd01379 80 GESGAGKTESANLLVQQL-TVLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 243 LLEKSRVVFQAEEERNYHIFYQLCASanLPEFKAL---RLGDANNFHYTNQGGspviEGVDDAKEMAHTR------QAC- 312
Cdd:cd01379 159 LLEKSRVVHQAIGERNFHIFYYIYAG--LAEDKKLakyKLPENKPPRYLQNDG----LTVQDIVNNSGNRekfeeiEQCf 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 313 TLLGISESYQMGIFRILAGILHLGNVVFMSRDS-----DSCTIpPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETY 387
Cdd:cd01379 233 KVIGFTKEEVDSVYSILAAILHIGDIEFTEVESnhqtdKSSRI-SNPEALNNVAKLLGIEADELQEALTSHSVVTRGETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 388 IKPISKLQATNARDALAKHIYAKLFNWIVDHVNQAL----HSAVKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQ 463
Cdd:cd01379 312 IRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpdrSASDEPLS-IGILDIFGFENFQKNSFEQLCINIANEQIQY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 464 QFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNthlN-KCALFEKP 541
Cdd:cd01379 391 YFNQHIFAWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKpMGLLALLDEESRFPKATDQTLVEKFHN---NiKSKYYWRP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 542 RLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLpelfqddekavsptsatssgrtpltrtpskptk 621
Cdd:cd01379 468 KSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV--------------------------------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 622 grpgqtakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRW 701
Cdd:cd01379 515 ----------RQTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRI 584
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 2015234411 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 |
4.07e-179 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 557.28 E-value: 4.07e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14929 1 ASVLHTLRRRY-DHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 163 GESGAGKTVSAKYAMRYFATVSGSASE----ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGAN 238
Cdd:cd14929 80 GESGAGKTVNTKHIIQYFATIAAMIESkkklGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 239 MRTYLLEKSRVVFQAEEERNYHIFYQLCASANlpEFKALRLGDAN--NFHYTNQGGSPViEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14929 160 IDIYLLEKSRVIFQQPGERNYHIFYQILSGKK--ELRDLLLVSANpsDFHFCSCGAVAV-ESLDDAEELLATEQAMDILG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 317 ISESYQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQA 396
Cdd:cd14929 237 FLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 397 TNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:cd14929 317 TYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 477 YMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKAFIIQ---- 551
Cdd:cd14929 397 YRKEGIDWVSIDFgLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHfelv 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 552 HFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaVSPTSATSSGRtpltrtpskptkgrpgqtaKEH 631
Cdd:cd14929 477 HYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENY---ISTDSAIQFGE-------------------KKR 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 632 KKTVGHQFRNSLH-----LLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEF 706
Cdd:cd14929 535 KKGASFQTVASLHkenlnKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADF 614
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 2015234411 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 |
3.70e-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: 552.35 E-value: 3.70e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14913 1 PAVLYNLKDRY-TSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 163 GESGAGKTVSAKYAMRYFATVSG---------SASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14913 80 GESGAGKTVNTKRVIQYFATIAAtgdlakkkdSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANlPEFKALRLGDAN--NFHYTNQGgSPVIEGVDDAKEMAHTRQA 311
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKK-PELIELLLITTNpyDYPFISQG-EILVASIDDAEELLATDSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 312 CTLLGISESYQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPI 391
Cdd:cd14913 238 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 392 SKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFK 471
Cdd:cd14913 318 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 472 LEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR-LSNKA-- 547
Cdd:cd14913 398 LEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKvVKGRAea 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 548 -FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekavsPTSATSSGrtPLTRTPSKPTKGRPGQ 626
Cdd:cd14913 478 hFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY--------ATFATADA--DSGKKKVAKKKGSSFQ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 627 takehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEF 706
Cdd:cd14913 548 -------TVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDF 620
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2015234411 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 |
7.84e-177 |
|
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: 551.09 E-value: 7.84e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14904 1 PSILFNLKKRFAASK-PYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 162 SGESGAGKTVSAKYAMRYFATVSGSASEANVEeKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:cd14904 80 SGESGAGKTETTKIVMNHLASVAGGRKDKTIA-KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 242 YLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQG-GSPVIEGVDDAKEMAHTRQACTLLGISES 320
Cdd:cd14904 159 YLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSlAQMQIPGLDDAKLFASTQKSLSLIGLDND 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 321 YQMGIFRILAGILHLGNVVFMSRDSDSCTIPpKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQATNAR 400
Cdd:cd14904 239 AQRTLFKILSGVLHLGEVMFDKSDENGSRIS-NGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEENR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 401 DALAKHIYAKLFNWIVDHVNQAL---HSAVKQHsfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEY 477
Cdd:cd14904 318 DALAKAIYSKLFDWMVVKINAAIstdDDRIKGQ--IGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 478 MKEQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHL----NKCALFekPRLSNKAFIIQHF 553
Cdd:cd14904 396 IREGLQWDHIEYQDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQtkkdNESIDF--PKVKRTQFIINHY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 554 ADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkAVSPTSATSSGRtpltrtpskptkgrpgqtAKEHKK 633
Cdd:cd14904 474 AGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE-APSETKEGKSGK------------------GTKAPK 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 634 TVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVL 713
Cdd:cd14904 535 SLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIM 614
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 2015234411 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 |
1.38e-176 |
|
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: 551.10 E-value: 1.38e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14927 2 SVLHNLRRRY-SRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 164 ESGAGKTVSAKYAMRYFATVS-------------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDK 230
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAalgdgpgkkaqflATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 231 RYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLcASANLPEFKALRLGDAN--NFHYTNQGGSPViEGVDDAKEMAHT 308
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQI-LSGKKPELQDMLLVSMNpyDYHFCSQGVTTV-DNMDDGEELMAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 309 RQACTLLGISESYQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYI 388
Cdd:cd14927 239 DHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 389 KPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMH 468
Cdd:cd14927 319 KGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 469 VFKLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKA 547
Cdd:cd14927 399 MFILEQEEYKREGIEWVFIDFgLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 548 -----FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddEKAVSPTSATSsgrtPLTRTPSKPTKG 622
Cdd:cd14927 479 kyeahFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY---ENYVGSDSTED----PKSGVKEKRKKA 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 623 RPGQTAKE-HKKtvghqfrnSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRW 701
Cdd:cd14927 552 ASFQTVSQlHKE--------NLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRI 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 2015234411 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 |
5.09e-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: 546.92 E-value: 5.09e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14920 2 SVLHNLKDRYY-SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 164 ESGAGKTVSAKYAMRYFATVSGS-------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIG 236
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASShkgrkdhNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 237 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPvIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIP-IPGQQDKDNFQETMEAMHIMG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 317 ISESYQMGIFRILAGILHLGNVVFM-SRDSDSCTIpPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14920 240 FSHEEILSMLKVVSSVLQFGNISFKkERNTDQASM-PENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 474
Cdd:cd14920 319 ADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 475 EEYMKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKA-FI 549
Cdd:cd14920 399 EEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAdFC 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 550 IQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAVSPTSATSSGRTpltrtpskpTKGRPGQTAK 629
Cdd:cd14920 479 IIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTET---------AFGSAYKTKK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 630 EHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSR 709
Cdd:cd14920 550 GMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2015234411 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 |
2.91e-170 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 533.84 E-value: 2.91e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 85 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP---------IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDER 155
Cdd:cd14907 3 LLINLKKRYQQDK-IFTYVGPTLIVMNPYKQIDnlfseevmqMYKEQIIQNGEYFDIKKEPPHIYAIAALAFKQLFENNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 156 NQSIIVSGESGAGKTVSAKYAMRYFATVSG------------------SASEANVEEKVLASNPIMESIGNAKTTRNDNS 217
Cdd:cd14907 82 KQAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevltltssiratSKSTKSIEQKILSCNPILEAFGNAKTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 218 SRFGKYIEIGFDKRYR-IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDAN---NFHYTNQGGS 293
Cdd:cd14907 162 SRFGKYVSILVDKKKRkILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLsgdRYDYLKKSNC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 294 PVIEGVDDAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVVFMSR--DSDSCTIPPKHEPLSIFCDLMGVAFEEM 371
Cdd:cd14907 242 YEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDStlDDNSPCCVKNKETLQIIAKLLGIDEEEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 372 SHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQAL--HSAVKQHSF------IGVLDIYGFET 443
Cdd:cd14907 322 KEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpKDEKDQQLFqnkylsIGLLDIFGFEV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 444 FEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTL--IDFYDNQPCINLIES-KLGILDLLDEECKMPKGTD 520
Cdd:cd14907 402 FQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSYTDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 521 DTWAQKLYNTHLNKCALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKavs 600
Cdd:cd14907 482 EKLLNKIKKQHKNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGEDG--- 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 601 ptsatssgrtpltrtpSKPTKGRPGQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQ 680
Cdd:cd14907 559 ----------------SQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQ 622
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2015234411 681 LRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkqkdvlsdrkqtcKNVLeklivdkdkyqFGKTKIFFR 751
Cdd:cd14907 623 IRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLK-------------KNVL-----------FGKTKIFMK 669
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
83-751 |
8.61e-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: 532.49 E-value: 8.61e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14909 1 ASVLHNLRQRYY-AKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 163 GESGAGKTVSAKYAMRYFATVSGS-------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRII 235
Cdd:cd14909 80 GESGAGKTENTKKVIAYFATVGASkktdeaaKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 236 GANMRTYLLEKSRVVFQAEEERNYHIFYQLcASANLPEFKALRL--GDANNFHYTNQGGSpVIEGVDDAKEMAHTRQACT 313
Cdd:cd14909 160 GADIETYLLEKARVISQQSLERSYHIFYQI-MSGSVPGVKEMCLlsDNIYDYYIVSQGKV-TVPNVDDGEEFSLTDQAFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 314 LLGISESYQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPISK 393
Cdd:cd14909 238 ILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 394 LQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLE 473
Cdd:cd14909 318 QQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 474 QEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKA----- 547
Cdd:cd14909 398 QEEYKREGIDWAFIDFgMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGqqaah 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 548 FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAVSPTSATSSGRtpltrtpskptkGRPGQT 627
Cdd:cd14909 478 FAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGR------------GKKGGG 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 628 AkehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFF 707
Cdd:cd14909 546 F----ATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFK 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2015234411 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, ... |
1504-1871 |
2.94e-169 |
|
Cargo binding domain of myosin 5C; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. The MyoV-CBDs directly interact with several adaptor proteins.MyoVb and myoVc areprimarily expressed in epithelial cells, and have been implicated as motors involved in recycling endosomes.
Pssm-ID: 271260 [Multi-domain] Cd Length: 332 Bit Score: 517.41 E-value: 2.94e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1504 EDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNT 1583
Cdd:cd15476 1 EDEAKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRHADYLNDANKLKSLMNAIITGVKQVIKEHQEDFEMLSFWLSNT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1584 CRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmivsgmlehetiqgvsgv 1663
Cdd:cd15476 81 YHFLNCLKQYSGEEEFMKHNTPRQNKNCLKNFDLSEHRQILSDLAIRIYHQFISVMENNLQP------------------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1664 kptglrkrtssiadegtyTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAVTLNNLLLRKDMCSWSKGMQIRY 1743
Cdd:cd15476 143 ------------------TISSILQQLSYFYSTMCQHGMDPELIKQAVKQLFFLIGAVTLNSIFLRKDMCSCRKGMQIRC 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1744 NVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFI 1823
Cdd:cd15476 205 NISYLEEWLKEKNLQNSNAKETLEPLSQAAWLLQVNKTTDDDAKEICERCTELSAVQIVKILNSYTPIDDFEKRVTPSFV 284
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2015234411 1824 RTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGL 1871
Cdd:cd15476 285 RKVQSLLQNREGSSQLMLDTKYRFQVTFPFCPSPQALEMLQVPSSLKL 332
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
83-751 |
8.61e-169 |
|
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: 530.25 E-value: 8.61e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAY------SGQNM---GDMDPHIFAVAEEAYKQMARD 153
Cdd:cd14908 1 PAILHSLSRRF-FRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYrqegllRSQGIespQALGPHVFAIADRSYRQMMSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 154 ER-NQSIIVSGESGAGKTVSAKYAMRYFATV----------SGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGK 222
Cdd:cd14908 80 IRaSQSILISGESGAGKTESTKIVMLYLTTLgngeegapneGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 223 YIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGD--------ANNFHYTNQGGSP 294
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDgitgglqlPNEFHYTGQGGAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 295 VIEGVDDAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVVFMSRDSDSCTIPPK---HEPLSIFCDLMGVAFEEM 371
Cdd:cd14908 240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEegnEKCLARVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 372 SHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ--HSFIGVLDIYGFETFEINSF 449
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKdiRSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 450 EQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIES-KLGILDLLDEECKMP-KGTDDTWAQKL 527
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAkKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 528 YNTHLNKC--ALFEKPRLSNKA-------FIIQHFADKVEYQCE-GFLEKNKDtvfeeqiKVLKSSKfkmlpELFQDdek 597
Cdd:cd14908 480 YETYLPEKnqTHSENTRFEATSiqktkliFAVRHFAGQVQYTVEtTFCEKNKD-------EIPLTAD-----SLFES--- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 598 avsptsatssgrtpltrtpskptkgrpgqtakehkktvGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRA 677
Cdd:cd14908 545 --------------------------------------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRV 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 678 VQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK--QKDVLS------DRKQTCKNVLEKLIVD------------ 737
Cdd:cd14908 587 TEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPliPEVVLSwsmerlDPQKLCVKKMCKDLVKgvlspamvsmkn 666
|
730
....*....|....*.
gi 2015234411 738 --KDKYQFGKTKIFFR 751
Cdd:cd14908 667 ipEDTMQLGKSKVFMR 682
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
84-751 |
1.26e-168 |
|
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: 529.55 E-value: 1.26e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14911 2 SVLHNIKDRYY-SGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 164 ESGAGKTVSAKYAMRYFATVSGSASEAN----------------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIG 227
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASKPKGSgavphpavnpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 228 FDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPViEGVDDAKEMAH 307
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPV-PGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 308 TRQACTLLGISESYQMGIFRILAGILHLGNVVF-MSRDSDSCTIPPKHEPLSIfCDLMGVAFEEMSHWLCHRKLATATET 386
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFrQERNNDQATLPDNTVAQKI-AHLLGLSVTDMTRAFLTPRIKVGRDF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 387 YIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQF 465
Cdd:cd14911 319 VTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 466 NMHVFKLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKPRLS 544
Cdd:cd14911 399 NHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFMKTDFR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 545 NKA-FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAVSPTSATSSgrtplTRTPSKPTKGR 623
Cdd:cd14911 478 GVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTD-----TQFGARTRKGM 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 624 pgqtakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTY 703
Cdd:cd14911 553 --------FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPF 624
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 2015234411 704 QEFFSRYRVLMKQ--KDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14911 625 QEFRQRYELLTPNviPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
83-751 |
9.12e-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: 513.50 E-value: 9.12e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14917 1 PAVLYNLKERY-ASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 163 GESGAGKTVSAKYAMRYFATVSG---------SASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14917 80 GESGAGKTVNTKRVIQYFAVIAAigdrskkdqTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANlPEFKALRLGDANNFHYTN-QGGSPVIEGVDDAKEMAHTRQAC 312
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKK-PELLDMLLITNNPYDYAFiSQGETTVASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 313 TLLGISESYQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPIS 392
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 393 KLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKL 472
Cdd:cd14917 319 VQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 473 EQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR-LSNKA--- 547
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRnIKGKPeah 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 548 FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekavsptsaTSSGRTPLTRTPSKPTKGRPGQt 627
Cdd:cd14917 479 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN----------YAGADAPIEKGKGKAKKGSSFQ- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 628 akehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFF 707
Cdd:cd14917 548 ------TVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFR 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2015234411 708 SRYRVLMKQ---KDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14917 622 QRYRILNPAaipEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
85-751 |
1.70e-161 |
|
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: 509.83 E-value: 1.70e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 85 VLHNLRVRFIDSkLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQM----ARDERNQSII 160
Cdd:cd14889 3 LLEVLKVRFMQS-NIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMlgrlARGPKNQCIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 161 VSGESGAGKTVSAKYAMRYFATVSGSASEanVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMR 240
Cdd:cd14889 82 ISGESGAGKTESTKLLLRQIMELCRGNSQ--LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 241 TYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISES 320
Cdd:cd14889 159 EYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYDEVCNAMDMVGFTEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 321 YQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHE-PLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQATNA 399
Cdd:cd14889 239 EEVDMFTILAGILSLGNITFEMDDDEALKVENDSNgWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAEDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 400 RDALAKHIYAKLFNWIVDHVNQALHSAVK---QHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:cd14889 319 RDSIAKVAYGRVFGWIVSKINQLLAPKDDssvELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLMEQKE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 477 YMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLyNTHLNKCALFEKPRLSNKAFIIQHFAD 555
Cdd:cd14889 399 YKKEGIDWKEITYKDNKPILDLFLNKpIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYGKSRSKSPKFTVNHYAG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekavsptSATSSGRTPLTRTPSKPTKGRPGQTAKEhKKTV 635
Cdd:cd14889 478 KVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLF----------TATRSRTGTLMPRAKLPQAGSDNFNSTR-KQSV 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK 715
Cdd:cd14889 547 GAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILLC 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 2015234411 716 QKDvLSDRKQTCKNVLEKliVDKDKYQFGKTKIFFR 751
Cdd:cd14889 627 EPA-LPGTKQSCLRILKA--TKLVGWKCGKTRLFFK 659
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
84-751 |
3.40e-160 |
|
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: 506.10 E-value: 3.40e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 84 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14934 2 SVLDNLRQRYTNMR-IYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 164 ESGAGKTVSAKYAMRYFATVSGSASEA-----NVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGAN 238
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSsdgkgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 239 MRTYLLEKSRVVFQAEEERNYHIFYQLCASANlPEF--KALRLGDANNFHYTNQGGSpVIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14934 161 IESYLLEKSRVISQQAAERGYHIFYQILSNKK-PELieSLLLVPNPKEYHWVSQGVT-VVDNMDDGEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 317 ISESYQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQA 396
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 397 TNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:cd14934 319 NNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 477 YMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKP-----RLSNKAFII 550
Cdd:cd14934 399 YKREGIEWVFIDFgLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPkggkgKGPEAHFEL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 551 QHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFkMLPELFQDDEKAVSPTSATSSGRTPLtrtpskptkgrpgqtake 630
Cdd:cd14934 479 VHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSL-GLLALLFKEEEAPAGSKKQKRGSSFM------------------ 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 631 hkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRY 710
Cdd:cd14934 540 ---TVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRY 616
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2015234411 711 RVLmkQKDVLS----DRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14934 617 QVL--NPNVIPqgfvDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
83-751 |
3.84e-160 |
|
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: 506.52 E-value: 3.84e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14916 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 163 GESGAGKTVSAKYAMRYFATVSG----------SASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd14916 80 GESGAGKTVNTKRVIQYFASIAAigdrskkenpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANlPEFKALRLGDANNFHYTN-QGGSPVIEGVDDAKEMAHTRQA 311
Cdd:cd14916 160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKK-PELLDMLLVTNNPYDYAFvSQGEVSVASIDDSEELLATDSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 312 CTLLGISESYQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPI 391
Cdd:cd14916 239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 392 SKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFK 471
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 472 LEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR----LSNK 546
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRnvkgKQEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 547 AFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAvsptSATSSGrtpltrtpskptKGRPGQ 626
Cdd:cd14916 479 HFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASA----DTGDSG------------KGKGGK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 627 TAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEF 706
Cdd:cd14916 543 KKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2015234411 707 FSRYRVL----MKQKDVLSDRKQTCKnVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14916 623 RQRYRILnpaaIPEGQFIDSRKGAEK-LLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
84-751 |
9.02e-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: 503.02 E-value: 9.02e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14932 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 164 ESGAGKTVSAKYAMRYFATVSGSA-----------SEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQgGSPVIEGVDDAKEMAHTRQAC 312
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSN-GNVTIPGQQDKELFAETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 313 TLLGISESYQMGIFRILAGILHLGNVVF-MSRDSDSCTIPPKHEPLSIfCDLMGVAFEEMSHWLCHRKLATATETYIKPI 391
Cdd:cd14932 240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFkKERNSDQASMPDDTAAQKV-CHLLGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 392 SKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14932 319 TQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKP-RLSN 545
Cdd:cd14932 399 ILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQGNN-PKFQKPkKLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 546 KA-FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAVSPTSATSsgrtpLTRTPSKPTKGRP 624
Cdd:cd14932 478 DAdFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAG-----MGESLHGAFKTRK 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 625 GQTakehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQ 704
Cdd:cd14932 553 GMF-----RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2015234411 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 |
1.32e-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: 502.34 E-value: 1.32e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14912 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 163 GESGAGKTVSAKYAMRYFATVSGSAS-----------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR 231
Cdd:cd14912 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 232 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANlPEFKALRLGDANNFHYT-NQGGSPVIEGVDDAKEMAHTRQ 310
Cdd:cd14912 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKK-PELIEMLLITTNPYDYPfVSQGEISVASIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 311 ACTLLGISESYQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKP 390
Cdd:cd14912 239 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 391 ISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14912 319 QTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRL----SN 545
Cdd:cd14912 399 VLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVvkgkAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 546 KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAVSPTSATSSgrtpltrtpskpTKGrpG 625
Cdd:cd14912 479 AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGA------------KKG--G 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 626 QTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14912 545 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2015234411 706 FFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14912 625 FKQRYKVLNASaipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
83-751 |
2.18e-158 |
|
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: 500.73 E-value: 2.18e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRF-IDSKLIYTYCGIVLVAINPYEQLPiygEDIINAYSGQNMGDMDPHIFAVAEEAYKQM---ARDERNQS 158
Cdd:cd14891 1 AGILHNLEERSkLDNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMclgSGRMQNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 159 IIVSGESGAGKTVSAKYAMRYFATVS-----------------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFG 221
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAvggkkasgqdieqsskkRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 222 KYIEIGFDKR-YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPVIEGVD 300
Cdd:cd14891 158 KFMKLQFTKDkFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 301 DAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVVFMSRDSDSCTI----PPKHEPLSIFCDLMGVAFEEMSHWLC 376
Cdd:cd14891 238 DAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAeiasESDKEALATAAELLGVDEEALEKVIT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 377 HRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEI-NSFEQFCIN 455
Cdd:cd14891 318 QREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFETkNDFEQLLIN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 456 YANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTHL-N 533
Cdd:cd14891 398 YANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPnGILPLLDNEARNPNPSDAKLNETLHKTHKrH 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 534 KCALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKfkmlpelfqddekavsptsatssgrtplt 613
Cdd:cd14891 478 PCFPRPHPKDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASSA----------------------------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 614 rtpskptkgrpgqtakehkktvghQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRIS 693
Cdd:cd14891 529 ------------------------KFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVL 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2015234411 694 AAGFPSRWTYQEFFSRYRVLM----KQKDVLSDRKQTcKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14891 585 KVGLPTRVTYAELVDVYKPVLppsvTRLFAENDRTLT-QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
83-751 |
2.36e-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: 501.52 E-value: 2.36e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14923 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 163 GESGAGKTVSAKYAMRYFATVS----------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd14923 80 GESGAGKTVNTKRVIQYFATIAvtgdkkkeqqPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANlPEFKALRLGDAN--NFHYTNQGgSPVIEGVDDAKEMAHTRQ 310
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKK-PELIDLLLISTNpfDFPFVSQG-EVTVASIDDSEELLATDN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 311 ACTLLGISESYQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKP 390
Cdd:cd14923 238 AIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 391 ISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14923 318 QNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR-LSNKA- 547
Cdd:cd14923 398 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKpAKGKAe 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 548 --FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekavSPTSATSSGRTPLTRTPSKpTKGRPG 625
Cdd:cd14923 478 ahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLF-------SNYAGAEAGDSGGSKKGGK-KKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 626 QtakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14923 550 Q-------TVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYAD 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2015234411 706 FFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14923 623 FKQRYRILNASaipEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
84-751 |
1.08e-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: 499.93 E-value: 1.08e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14921 2 SVLHNLRERYF-SGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 164 ESGAGKTVSAKYAMRYFATVSGS-------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIG 236
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASShkgkkdtSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 237 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPvIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVP-IPAAQDDEMFQETLEAMSIMG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 317 ISESYQMGIFRILAGILHLGNVVF-MSRDSDSCTIPPKHEPLSIfCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14921 240 FSEEEQLSILKVVSSVLQLGNIVFkKERNTDQASMPDNTAAQKV-CHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 474
Cdd:cd14921 319 ADFAIEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 475 EEYMKEQIPWTLIDF-YDNQPCINLIE---SKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPR-LSNKA-F 548
Cdd:cd14921 399 EEYQREGIEWNFIDFgLDLQPCIELIErpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNH-PKFQKPKqLKDKTeF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 549 IIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAVSPTSATSSGRTPLtrtPSKptkgrpGQTA 628
Cdd:cd14921 478 SIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSL---PSA------SKTK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 629 KEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 708
Cdd:cd14921 549 KGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2015234411 709 RYRVLMKQK--DVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14921 629 RYEILAANAipKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
85-751 |
1.29e-157 |
|
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: 498.06 E-value: 1.29e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 85 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDM-DPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14897 3 IVQTLKSRYNKDK-FYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVRSQrPPHLFWIADQAYRRLLETGRNQCILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 164 ESGAGKTVSAKYAMRYFATVSGSASEaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYL 243
Cdd:cd14897 82 ESGAGKTESTKYMIKHLMKLSPSDDS-DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 244 LEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNfHYTNQGGSPVIEGVDDAKEMAHTRQACT-------LLG 316
Cdd:cd14897 161 LEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDC-HRILRDDNRNRPVFNDSEELEYYRQMFHdltnimkLIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 317 ISESYQMGIFRILAGILHLGNVVFMS-RDSDSCTIPPKHePLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14897 240 FSEEDISVIFTILAAILHLTNIVFIPdEDTDGVTVADEY-PLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQH-----SFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14897 319 ANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQimtrgPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 471 KLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLyNTHLNKCALFEKPRLSNKAFI 549
Cdd:cd14897 399 PRERSEYEIEGIEWRDIEYHDNDDVLELFFKKpLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESPRYVASPGNRVAFG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 550 IQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekavspTSatssgrtpltrtpskptkgrpgqtak 629
Cdd:cd14897 478 IRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF---------TS-------------------------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 630 ehkktvghQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSR 709
Cdd:cd14897 523 --------YFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKR 594
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 2015234411 710 YRVLM-KQKDVLSDRKQTCKNVLEKLivDKDKYQFGKTKIFFR 751
Cdd:cd14897 595 YKEICdFSNKVRSDDLGKCQKILKTA--GIKGYQFGKTKVFLK 635
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
83-751 |
6.41e-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: 497.72 E-value: 6.41e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14918 1 PGVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 163 GESGAGKTVSAKYAMRYFATVSGSAS---------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14918 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANlPEFKALRLGDANNFHYT-NQGGSPVIEGVDDAKEMAHTRQAC 312
Cdd:cd14918 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKK-PDLIEMLLITTNPYDYAfVSQGEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 313 TLLGISESYQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPIS 392
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 393 KLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKL 472
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 473 EQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRL----SNKA 547
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVvkgkAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 548 FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAVSPTSATSSGRtpltrtpskpTKGRPGQt 627
Cdd:cd14918 479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAK----------KKGSSFQ- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 628 akehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFF 707
Cdd:cd14918 548 ------TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFK 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2015234411 708 SRYRVLMKQ---KDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14918 622 QRYKVLNASaipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
83-751 |
1.52e-155 |
|
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: 493.86 E-value: 1.52e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14910 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 163 GESGAGKTVSAKYAMRYFATVSGSAS-----------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR 231
Cdd:cd14910 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 232 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANlPEFKALRLGDANNFHYT-NQGGSPVIEGVDDAKEMAHTRQ 310
Cdd:cd14910 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKK-PDLIEMLLITTNPYDYAfVSQGEITVPSIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 311 ACTLLGISESYQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKP 390
Cdd:cd14910 239 AIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 391 ISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14910 319 QTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKA-- 547
Cdd:cd14910 399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKve 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 548 --FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekavsptsatsSGRTPLTRTPSKPTKGrpG 625
Cdd:cd14910 479 ahFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLF--------------SGAAAAEAEEGGGKKG--G 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 626 QTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14910 543 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2015234411 706 FFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14910 623 FKQRYKVLNASaipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
83-751 |
3.57e-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: 3.57e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14915 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 163 GESGAGKTVSAKYAMRYFATVSGSAS-----------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR 231
Cdd:cd14915 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeaasgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 232 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANlPEFKALRLGDAN--NFHYTNQGgSPVIEGVDDAKEMAHTR 309
Cdd:cd14915 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKK-PELIEMLLITTNpyDFAFVSQG-EITVPSIDDQEELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 310 QACTLLGISESYQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIK 389
Cdd:cd14915 238 SAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 390 PISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHV 469
Cdd:cd14915 318 GQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 470 FKLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSN-KA 547
Cdd:cd14915 398 FVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKgKA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 548 ---FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAVSPTSATSSGrtpltrtpskptkgrp 624
Cdd:cd14915 478 eahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGGGKKG---------------- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 625 GQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQ 704
Cdd:cd14915 542 GKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYA 621
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 2015234411 705 EFFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14915 622 DFKQRYKVLNASaipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
85-749 |
3.03e-154 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 489.75 E-value: 3.03e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 85 VLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAY-SGQNMGDMDPHIFAVAEEAYK--QMARDERNQSII 160
Cdd:cd14880 3 VLRCLQARYT-ADTFYTNAGCTLVALNPFKPVPqLYSPELMREYhAAPQPQKLKPHIFTVGEQTYRnvKSLIEPVNQSIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 161 VSGESGAGKTVSAKYAMRYFATVSGSAS--EAN-----VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14880 82 VSGESGAGKTWTSRCLMKFYAVVAASPTswESHkiaerIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTnqggsPVIEGVDDAKEMAHTRQACT 313
Cdd:cd14880 162 MTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWL-----PNPERNLEEDCFEVTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 314 LLGISESYQMGIFRILAGILHLGNVVFMSRDSDSCTIPPK---HEPLSIFCDLMGVAFEEMSHWLCHRKLATATE--TYI 388
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMddtKESVRTSALLLKLPEDHLLETLQIRTIRAGKQqqVFK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 389 KPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNM 467
Cdd:cd14880 317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 468 HVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIE-SKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNK 546
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKLSRE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 547 -AFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAVSPTSATSSGRTPLTrtpskptkgrpg 625
Cdd:cd14880 477 pSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQSRAPVL------------ 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 626 qtakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14880 545 --------TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQN 616
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2015234411 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 |
1.73e-153 |
|
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: 488.45 E-value: 1.73e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14919 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 164 ESGAGKTVSAKYAMRYFATVSGS----ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANM 239
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASShkskKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 240 RTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQgGSPVIEGVDDAKEMAHTRQACTLLGISE 319
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSN-GHVTIPGQQDKDMFQETMEAMRIMGIPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 320 SYQMGIFRILAGILHLGNVVF-MSRDSDSCTIPPKHEPLSIfCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQATN 398
Cdd:cd14919 240 EEQMGLLRVISGVLQLGNIVFkKERNTDQASMPDNTAAQKV-SHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 399 ARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEY 477
Cdd:cd14919 319 AIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 478 MKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYN---THLNkcalFEKPR-LSNKA-F 548
Cdd:cd14919 399 QREGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQeqgTHPK----FQKPKqLKDKAdF 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 549 IIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAVSPTSATSSGRTPLtrtpskptkgrPG--Q 626
Cdd:cd14919 475 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETAL-----------PGafK 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 627 TAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEF 706
Cdd:cd14919 544 TRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEF 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2015234411 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 |
4.71e-152 |
|
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: 485.61 E-value: 4.71e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGediINAYSGQNMGDMD--PHIFAVAEEAYKQMAR------- 152
Cdd:cd14895 1 PAFVDYLAQRYGVDQ-VYCRSGAVLIAVNPFKHIPgLYD---LHKYREEMPGWTAlpPHVFSIAEGAYRSLRRrlhepga 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 153 DERNQSIIVSGESGAGKTVSAKYAMRYFA--------TVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYI 224
Cdd:cd14895 77 SKKNQTILVSGESGAGKTETTKFIMNYLAesskhttaTSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 225 EIGF-----DKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGD--ANNFHYTNQGGSPVI- 296
Cdd:cd14895 157 RMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELlsAQEFQYISGGQCYQRn 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 297 EGVDDAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVVFMS-------RDSDSCTIPPK-----------HEPLS 358
Cdd:cd14895 237 DGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVAssedegeEDNGAASAPCRlasaspssltvQQHLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 359 IFCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQAlhSAVKQHS------- 431
Cdd:cd14895 317 IVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSA--SPQRQFAlnpnkaa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 432 ------FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LG 504
Cdd:cd14895 395 nkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRpSG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 505 ILDLLDEECKMPKGTDDTWAQKLYNThLNKCALFEKPRL--SNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKS 582
Cdd:cd14895 475 IFSLLDEECVVPKGSDAGFARKLYQR-LQEHSNFSASRTdqADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGK 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 583 SKFKMLPELFqdDEKAVSPTSATSSGRTPLTRTPSKPTkgrpgqtakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIK 662
Cdd:cd14895 554 TSDAHLRELF--EFFKASESAELSLGQPKLRRRSSVLS-----------SVGIGSQFKQQLASLLDVVQQTQTHYIRCIK 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 663 PNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLSdrkQTCKNVLEKLIVdkDKYQ 742
Cdd:cd14895 621 PNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASD---ATASALIETLKV--DHAE 695
|
....*....
gi 2015234411 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 |
2.84e-150 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 481.31 E-value: 2.84e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAY--------SGQNMGDMDPHIFAVAEEAYKQMARD 153
Cdd:cd14902 1 AALLQALSERF-EHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFGGLLKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 154 ER-NQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEANVE--------EKVLASNPIMESIGNAKTTRNDNSSRFGKYI 224
Cdd:cd14902 80 ERrNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEgsdaveigKRILQTNPILESFGNAQTIRNDNSSRFGKFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 225 EIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGS----PVIEGVD 300
Cdd:cd14902 160 KIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGPsfarKRAVADK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 301 DAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVVFM---SRDSDSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCH 377
Cdd:cd14902 240 YAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTaenGQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 378 RKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIV-------DHVNQALHSAVKQHSF--IGVLDIYGFETFEINS 448
Cdd:cd14902 320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVrrlsdeiNYFDSAVSISDEDEELatIGILDIFGFESLNRNG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 449 FEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKL 527
Cdd:cd14902 400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSnGLFSLLDQECLMPKGSNQALSTKF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 528 YNTHLNKcalfekprlsnKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQdDEKAVSPTSATSS 607
Cdd:cd14902 480 YRYHGGL-----------GQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGA-DENRDSPGADNGA 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 608 G---RTPLTRTPSkptkgrpgqtakehkktVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRAC 684
Cdd:cd14902 548 AgrrRYSMLRAPS-----------------VSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSV 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 685 GVLETIRISAAGFPSRWTYQEF---FSRYRVLMKQKD----------------------VLSDRKQTCKNVLEKLIVDKD 739
Cdd:cd14902 611 GVLEAVRIARHGYSVRLAHASFielFSGFKCFLSTRDraakmnnhdlaqalvtvlmdrvLLEDGVEREEKNPGALTAVTG 690
|
730 740
....*....|....*....|....*.
gi 2015234411 740 KY--------------QFGKTKIFFR 751
Cdd:cd14902 691 DGsgtafendcrrkdvQVGRTLVFCK 716
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
84-751 |
1.14e-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: 478.05 E-value: 1.14e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14930 2 SVLHNLRERYY-SGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 164 ESGAGKTVSAKYAMRYFATVSGSAS-------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIG 236
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKgrkepgvPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 237 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGgsPVIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG--PSSSPGQERELFQETLESLRVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 317 ISESYQMGIFRILAGILHLGNVVF-MSRDSDSCTIpPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14930 239 FSHEEITSMLRMVSAVLQFGNIVLkRERNTDQATM-PDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 474
Cdd:cd14930 318 ADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 475 EEYMKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKPR-LSNKA-F 548
Cdd:cd14930 398 EEYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRhLRDQAdF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 549 IIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAVSPTSATSSGrtpltrtpSKPTKGRPgqtA 628
Cdd:cd14930 477 SVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLG--------DGPPGGRP---R 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 629 KEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 708
Cdd:cd14930 546 RGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2015234411 709 RYRVLMKQK--DVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14930 626 RYEILTPNAipKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
84-751 |
3.14e-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: 476.87 E-value: 3.14e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd15896 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 164 ESGAGKTVSAKYAMRYFATVSGS-----------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQgGSPVIEGVDDAKEMAHTRQAC 312
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSN-GNVTIPGQQDKDLFTETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 313 TLLGISESYQMGIFRILAGILHLGNVVF-MSRDSDSCTIPPKHEPLSIfCDLMGVAFEEMSHWLCHRKLATATETYIKPI 391
Cdd:cd15896 240 RIMGIPEDEQIGMLKVVASVLQLGNMSFkKERHTDQASMPDNTAAQKV-CHLMGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 392 SKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd15896 319 TQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIE---SKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNK 546
Cdd:cd15896 399 ILEQEEYQREGIEWSFIDFgLDLQPCIDLIEkpaSPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 547 A-FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAVSPTSATSSGRTPltrtpskptkgRPG 625
Cdd:cd15896 479 AdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSEMP-----------GAF 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 626 QTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd15896 548 KTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2015234411 706 FFSRYRVLMKQK--DVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd15896 628 FRQRYEILTPNAipKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
85-725 |
1.65e-146 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 467.48 E-value: 1.65e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 85 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAY---------SGQNMGD--MDPHIFAVAEEAYKQMAR 152
Cdd:cd14900 3 ILSALETRFYAQK-IYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssSTRNKGSdpMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 153 ----DERNQSIIVSGESGAGKTVSAKYAMRYFA---------TVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSR 219
Cdd:cd14900 82 glngVMSDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaaSVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 220 FGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAsanlpefkalrlgdannfhytnqGGSPVIEGV 299
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAI-----------------------GASEAARKR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 300 DDAKEMAhtrQACTLLGISESYQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHE--PLSIF-----CDLMGVAFEEMS 372
Cdd:cd14900 219 DMYRRVM---DAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDlaPSSIWsrdaaATLLSVDATKLE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 373 HWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALH--SAVKQHS---FIGVLDIYGFETFEIN 447
Cdd:cd14900 296 KALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKmdDSSKSHGglhFIGILDIFGFEVFPKN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 448 SFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQK 526
Cdd:cd14900 376 SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRpTGILSLIDEECVMPKGSDTTLASK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 527 LYnTHLNKCALFEKPRLSNKA--FIIQHFADKVEYQCEGFLEKNKDTVFEEQIkvlksskfkmlpELFQDdekavsptsa 604
Cdd:cd14900 456 LY-RACGSHPRFSASRIQRARglFTIVHYAGHVEYSTDGFLEKNKDVLHQEAV------------DLFVY---------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 605 tssgrtpltrtpskptkgrpgqtakehkktvGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRAC 684
Cdd:cd14900 513 -------------------------------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCN 561
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2015234411 685 GVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLSDRKQ 725
Cdd:cd14900 562 GVMEAVRVARAGFPIRLLHDEFVARYFSLARAKNRLLAKKQ 602
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
83-751 |
5.12e-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: 455.78 E-value: 5.12e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14896 1 SSVLLCLKKRF-HLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 163 GESGAGKTVSAKYAMRYFATVSGSASEANVE--EKVLasnPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMR 240
Cdd:cd14896 80 GHSGSGKTEAAKKIVQFLSSLYQDQTEDRLRqpEDVL---PILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 241 TYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISES 320
Cdd:cd14896 156 HYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 321 YQMGIFRILAGILHLGNVVFMSRDSDSctippkHEPLSIFCD--------LMGVAFEEMSHWLCHRKLATATETYIKPIS 392
Cdd:cd14896 236 ELTAIWAVLAAILQLGNICFSSSERES------QEVAAVSSWaeihtaarLLQVPPERLEGAVTHRVTETPYGRVSRPLP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 393 KLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSF--IGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14896 310 VEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 471 KLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPRLSNKAFI 549
Cdd:cd14896 390 AQEEEECQRELLPWVPIPQPPRESCLDLLVDQPhSLLSILDDQTWLSQATDHTFLQKCHYHHGDH-PSYAKPQLPLPVFT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 550 IQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQddekavsptsatssgrtpltrtpskptKGRPGQTAK 629
Cdd:cd14896 469 VRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQ---------------------------EAEPQYGLG 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 630 EHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSR 709
Cdd:cd14896 522 QGKPTLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLAR 601
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2015234411 710 YRVLMKQK-DVLSDRKQtCKNVLEKLI-VDKDKYQFGKTKIFFR 751
Cdd:cd14896 602 FGALGSERqEALSDRER-CGAILSQVLgAESPLYHLGATKVLLK 644
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
53-803 |
1.64e-140 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 457.95 E-value: 1.64e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 53 DPKTKE-----LPHLRNPDILVGEN---DLTALSYLHEPAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDII 124
Cdd:PTZ00014 72 DPPTNStfevkPEHAFNANSQIDPMtygDIGLLPHTNIPCVLDFLKHRYL-KNQIYTTADPLLVAINPFKDLGNTTNDWI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 125 NAY-SGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIM 203
Cdd:PTZ00014 151 RRYrDAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLKIQNAIMAANPVL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 204 ESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANlPEFKA-LRLGDA 282
Cdd:PTZ00014 231 EAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGAN-DEMKEkYKLKSL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 283 NNFHYTNQgGSPVIEGVDDAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVVFMSRDSD-----SCTIPPKHEPL 357
Cdd:PTZ00014 310 EEYKYINP-KCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGgltdaAAISDESLEVF 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 358 SIFCDLMGVAFEEMSHWLchrklaTATETYI------KPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHS 431
Cdd:PTZ00014 389 NEACELLFLDYESLKKEL------TVKVTYAgnqkieGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 432 FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLD 510
Cdd:PTZ00014 463 FIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGkSVLSILE 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 511 EECKMPKGTDD----TWAQKLYNthlNKCALFEKpRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFK 586
Cdd:PTZ00014 543 DQCLAPGGTDEkfvsSCNTNLKN---NPKYKPAK-VDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNP 618
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 587 MLPELFQDDEkavsptsatssgrtpLTRtpskptkgrpGQTAKehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDF 666
Cdd:PTZ00014 619 LVRDLFEGVE---------------VEK----------GKLAK--GQLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNEN 671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 667 KFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRV--LMKQKDVLSDRKQTCKNVLEKLIVDKDKYQFG 744
Cdd:PTZ00014 672 KKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYldLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIG 751
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2015234411 745 KTKIFFRAGQVAYLEKLRADKLRA--ACIRIqktIRGWLLRKKYLR-MRKAAITVQR---YVRGH 803
Cdd:PTZ00014 752 KTMVFLKKDAAKELTQIQREKLAAwePLVSV---LEALILKIKKKRkVRKNIKSLVRiqaHLRRH 813
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
85-749 |
2.29e-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: 448.27 E-value: 2.29e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 85 VLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQN-MGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14906 3 ILNNLGKRYK-SDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINqNKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 163 GESGAGKTVSAKYAMRYFATVSGSASEAN---------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR-Y 232
Cdd:cd14906 82 GESGSGKTEASKTILQYLINTSSSNQQQNnnnnnnnnsIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 233 RIIGANMRTYLLEKSRVVFQAEEER-NYHIFYQLCASANLPEFKALRL-GDANNFHYTN-------------QGGSPVIE 297
Cdd:cd14906 162 KIDGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLnNDPSKYRYLDarddvissfksqsSNKNSNHN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 298 GVDDAKE-MAHTRQACTLLGISESYQMGIFRILAGILHLGNVVFmSRDSDSCTI----PPKHEPLSIFCDLMGVAFEEMS 372
Cdd:cd14906 242 NKTESIEsFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEF-EEDSDFSKYayqkDKVTASLESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 373 HWLCHRKLATATE--TYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQ-----------ALHSAVKQHSFIGVLDIY 439
Cdd:cd14906 321 QALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRkfnqntqsndlAGGSNKKNNLFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 440 GFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKG 518
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKsDGILSLLDDECIMPKG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 519 TDDTWAQKlYNTHLNKCALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKA 598
Cdd:cd14906 481 SEQSLLEK-YNKQYHNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQITS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 599 VSPTSATSSGRTpltrtpskptkgrpgqtakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAV 678
Cdd:cd14906 560 TTNTTKKQTQSN-----------------------TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVL 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 679 QQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLSDRKQTCKNVLEKLIV---------------------- 736
Cdd:cd14906 617 SQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIqsklktmgisnnkkknnsnsns 696
|
730
....*....|....*..
gi 2015234411 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 |
2.51e-135 |
|
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: 437.50 E-value: 2.51e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSG-QNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14876 1 PCVLDFLKHRYLKNQ-IYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 162 SGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:cd14876 80 SGESGAGKTEATKQIMRYFASAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 242 YLLEKSRVVFQAEEERNYHIFYQLCASANlPEFKA-LRLGDANNFHYTNqGGSPVIEGVDDAKEMAHTRQACTLLGISES 320
Cdd:cd14876 160 FLLEKSRIVTQDDNERSYHIFYQLLKGAD-SEMKSkYHLLGLKEYKFLN-PKCLDVPGIDDVADFEEVLESLKSMGLTEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 321 YQMGIFRILAGILHLGNVVFMSRD----SDSCTIPPkhEPLSIF---CDLMGVAFEEMSHWLChRKLATATETYIK-PIS 392
Cdd:cd14876 238 QIDTVFSIVSGVLLLGNVKITGKTeqgvDDAAAISN--ESLEVFkeaCSLLFLDPEALKRELT-VKVTKAGGQEIEgRWT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 393 KLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKL 472
Cdd:cd14876 315 KDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFER 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 473 EQEEYMKEQIPWTLIDFYDNQPCIN-LIESKLGILDLLDEECKMPKGTDD----TWAQKLYNthlNKCALFEKpRLSNKA 547
Cdd:cd14876 395 ESKLYKDEGIPTAELEYTSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEkfvsACVSKLKS---NGKFKPAK-VDSNIN 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 548 FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekavsptsatssgrTPLTRtpskptkgrpGQT 627
Cdd:cd14876 471 FIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEG---------------VVVEK----------GKI 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 628 AKehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFF 707
Cdd:cd14876 526 AK--GSLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFL 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2015234411 708 SRYRVL-MKQKDVLSDRKQT-CKNVLEKLIVDKDKYQFGKTKIF 749
Cdd:cd14876 604 YQFKFLdLGIANDKSLDPKVaALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
84-736 |
1.91e-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: 423.35 E-value: 1.91e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYS---GQNMGDM-------DPHIFAVAEEAYKQMAR 152
Cdd:cd14899 2 SILNALRLRY-ERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhNSQFGDRvtstdprEPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 153 DERNQSIIVSGESGAGKTVSAKYAMRYFATVSG----------------SASEANVEEKVLASNPIMESIGNAKTTRNDN 216
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGtgnnnltnsesisppaSPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 217 SSRFGKYIEIGF-DKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQL------CASANLPEFKALRlGDANNFHYTN 289
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELlsadnnCVSKEQKQVLALS-GGPQSFRLLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 290 QG-GSPVIEGVDDAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVVFM--------------SRDSDSCTIPPKH 354
Cdd:cd14899 240 QSlCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEqiphkgddtvfadeARVMSSTTGAFDH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 355 epLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVK------ 428
Cdd:cd14899 320 --FTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASapwgad 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 429 ---------QHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLI 499
Cdd:cd14899 398 esdvddeedATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 500 ESK-LGILDLLDEECKMPKGTDDTWAQKLY--------NTHLNKCALFEKprlsNKAFIIQHFADKVEYQCEGFLEKNKD 570
Cdd:cd14899 478 EHRpIGIFSLTDQECVFPQGTDRALVAKYYlefekknsHPHFRSAPLIQR----TTQFVVAHYAGCVTYTIDGFLAKNKD 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 571 TVFEEQIKVLKSSKFKMLPELfqddekAVSPTSATSSGRTPLTRTPSKPTKGRPGQTAkehKKTVGHQFRNSLHLLMETL 650
Cdd:cd14899 554 SFCESAAQLLAGSSNPLIQAL------AAGSNDEDANGDSELDGFGGRTRRRAKSAIA---AVSVGTQFKIQLNELLSTV 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 651 NATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYR----VLMKQKDVLSDRKQT 726
Cdd:cd14899 625 RATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYRrvllSLYKWGDNDFERQMR 704
|
730
....*....|
gi 2015234411 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 |
2.88e-123 |
|
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: 403.88 E-value: 2.88e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 85 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMG-----DMDPHIFAVAEEAYKQMARDERNQS 158
Cdd:cd14886 3 VIDILRDRFAKDK-IYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 159 IIVSGESGAGKTVSAKYAMRYFAtVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGAN 238
Cdd:cd14886 82 CIVSGESGAGKTETAKQLMNFFA-YGHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 239 MRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLgIS 318
Cdd:cd14886 161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKL-FS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 319 ESYQMGIFRILAGILHLGNVVFMSRDS---DSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14886 240 KNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQE 475
Cdd:cd14886 320 AEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEIQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 476 EYMKEQIPWTLIDFYDNQPCINLIES-KLGILDLLDEECKMPKGTDDTWAQKLyNTHLNKcALFEKPRLSNKAFIIQHFA 554
Cdd:cd14886 400 EYEIEGIDHSMITFTDNSNVLAVFDKpNLSIFSFLEEQCLIQTGSSEKFTSSC-KSKIKN-NSFIPGKGSQCNFTIVHTA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 555 DKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekavsptsatssgrtpltrtpskptkgRPGQTAKEHKKT 634
Cdd:cd14886 478 ATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSD----------------------------IPNEDGNMKGKF 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 635 VGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLM 714
Cdd:cd14886 530 LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILI 609
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2015234411 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 |
1.11e-121 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 399.57 E-value: 1.11e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 85 VLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAY-SGQNMGDMDPHIFAVAEEAYKQM-ARDERNQSIIVS 162
Cdd:cd14875 3 LLHCIKERFEKLHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 163 GESGAGKTVSAKYAMRYFATVS----GSASEANVEEKVLA----SNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRI 234
Cdd:cd14875 83 GESGSGKTENAKMLIAYLGQLSymhsSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPTSGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 235 -IGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKAL-RLGDANNFHYTNQGGSPVIEGVD-----DAKEMAH 307
Cdd:cd14875 163 mVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTFVRRGVDgktldDAHEFQN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 308 TRQACTLLGISESYQMGIFRILAGILHLGNVVFMSRDSDSCTIPpKHEPLSIFCDLMGVAFEEMSHwlChrkLATATETY 387
Cdd:cd14875 243 VRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIA-DETPFLTACRLLQLDPAKLRE--C---FLVKSKTS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 388 IKPI--SKLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHS--FIGVLDIYGFETFEINSFEQFCINYANEKLQQ 463
Cdd:cd14875 317 LVTIlaNKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCSGckYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 464 QFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR 542
Cdd:cd14875 397 HYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKrTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPYFVLPK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 543 --LSNKaFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekavsptsatssgrtpltrtpskpt 620
Cdd:cd14875 477 stIPNQ-FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTE------------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 621 kgrpgQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSR 700
Cdd:cd14875 531 -----KGLARRKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVR 605
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 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 |
1.89e-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: 376.16 E-value: 1.89e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 84 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQlpIYGEDIINAYSgQNMGDMDPHIFAVAEEAYKQMARdERNQSIIVSG 163
Cdd:cd14898 2 ATLEILEKRYASGK-IYTKSGLVFLALNPYET--IYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 164 ESGAGKTVSAKYAMRYFatVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRyrIIGANMRTYL 243
Cdd:cd14898 77 ESGSGKTENAKLVIKYL--VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFDGK--ITGAKFETYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 244 LEKSRVVFQAEEERNYHIFYQLCASanlpefKALRLgdANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISeSYQm 323
Cdd:cd14898 153 LEKSRVTHHEKGERNFHIFYQFCAS------KRLNI--KNDFIDTSSTAGNKESIVQLSEKYKMTCSAMKSLGIA-NFK- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 324 GIFRILAGILHLGNVVFmsrDSDSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATEtYIKPISKL-QATNARDA 402
Cdd:cd14898 223 SIEDCLLGILYLGSIQF---VNDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGE-TIEVFNTLkQARTIRNS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 403 LAKHIYAKLFNWIVDHVNQALhSAVKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQI 482
Cdd:cd14898 299 MARLLYSNVFNYITASINNCL-EGSGERS-ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEGI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 483 PWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKL--YNTHlnkcalFEKPRLSNKaFIIQHFADKVEYQ 560
Cdd:cd14898 377 EWPDVEFFDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIkkYLNG------FINTKARDK-IKVSHYAGDVEYD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 561 CEGFLEKNKDtvfEEQIKVLKSskfkmlpelfqddekavsptsatssgrtpltrtpskptkgrPGQTAKEHKKTVGHQFR 640
Cdd:cd14898 450 LRDFLDKNRE---KGQLLIFKN-----------------------------------------LLINDEGSKEDLVKYFK 485
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2015234411 641 NSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVL 713
Cdd:cd14898 486 DSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRIL 558
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
84-750 |
1.99e-108 |
|
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: 361.10 E-value: 1.99e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 84 AVLHNLRVRFIdSKLIYTYCGI-VLVAINPYEQLPI--------YGEDIINAYSGQNMGDMdPHIFAVAEEAYKQMARDE 154
Cdd:cd14879 5 AITSHLASRFR-SDLPYTRLGSsALVAVNPYKYLSSnsdaslgeYGSEYYDTTSGSKEPLP-PHAYDLAARAYLRMRRRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 155 RNQSIIVSGESGAGKTVSAKYAMRYFATVSGSAS-EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14879 83 EDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKkGTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYT---NQGGSPVIEGVDDAKEMAHTRQ 310
Cdd:cd14879 163 LIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasyGCHPLPLGPGSDDAEGFQELKT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 311 ACTLLGISESYQMGIFRILAGILHLGNVVFM---SRDSDSCTIPPKHEpLSIFCDLMGVAFEEMSHWL------CHRKLA 381
Cdd:cd14879 243 ALKTLGFKRKHVAQICQLLAAILHLGNLEFTydhEGGEESAVVKNTDV-LDIVAAFLGVSPEDLETSLtyktklVRKELC 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 382 TateTYIKPIsklQATNARDALAKHIYAKLFNWIVDHVNQALhSAVKQ--HSFIGVLDIYGFETF---EINSFEQFCINY 456
Cdd:cd14879 322 T---VFLDPE---GAAAQRDELARTLYSLLFAWVVETINQKL-CAPEDdfATFISLLDFPGFQNRsstGGNSLDQFCVNF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 457 ANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECK-MPKGTDDTWAQKLYNTHLNK 534
Cdd:cd14879 395 ANERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKpGGLLGILDDQTRrMPKKTDEQMLEALRKRFGNH 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 535 CALFEKPRLSNK----AFIIQHFADKVEYQCEGFLEKNKDTVfeeqikvlkSSKFkmlpelfqddekaVSptsatssgrt 610
Cdd:cd14879 475 SSFIAVGNFATRsgsaSFTVNHYAGEVTYSVEGFLERNGDVL---------SPDF-------------VN---------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 611 pLTRtpskptkgrpGQTakehkktvghQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETI 690
Cdd:cd14879 523 -LLR----------GAT----------QLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELA 581
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 691 RISAAGFPSRWTYQEFFSRYrvlmKQKDVLSDRKQTCKNVLEKLIVDKDKYQFGKTKIFF 750
Cdd:cd14879 582 ARLRVEYVVSLEHAEFCERY----KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
84-751 |
1.54e-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: 327.16 E-value: 1.54e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 84 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAY---SGQNMGDMDPHIFAVAEEAYKQMARDERNQSII 160
Cdd:cd14878 2 SLLYEIQKRFGNNQ-IYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 161 VSGESGAGKTVSAKYAMRYFATVSGSaSEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGF-DKRYRIIGANM 239
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASS-SRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 240 RTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQG---GSPVIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14878 160 YTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmreDVSTAERSLNREKLAVLKQALNVVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 317 ISESYQMGIFRILAGILHLGNVVFMS-RDSDSCTIpPKHEPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14878 240 FSSLEVENLFVILSAILHLGDIRFTAlTEADSAFV-SDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 396 ATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSF----IGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFK 471
Cdd:cd14878 319 AEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 472 LEQEEYMKEQIPW----------TLIDFYDNQPcinlieskLGILDLLDEECKMPKGTDDTWAQKLY----NTHLNKCAL 537
Cdd:cd14878 399 QEQTECVQEGVTMetayspgnqtGVLDFFFQKP--------SGFLSLLDEESQMIWSVEPNLPKKLQslleSSNTNAVYS 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 538 FEK-------PRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQddekavsptsatssgrt 610
Cdd:cd14878 471 PMKdgngnvaLKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ----------------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 611 pltrtpSKPTkgrpgqtakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETI 690
Cdd:cd14878 534 ------SKLV-------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMV 594
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2015234411 691 RISAAGFPSRWTYQEFFSRYRVLMKQkdVLSDRKQT-----CKNVLEKliVDKDKYQFGKTKIFFR 751
Cdd:cd14878 595 KIFRYGYPVRLSFSDFLSRYKPLADT--LLGEKKKQsaeerCRLVLQQ--CKLQGWQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
85-751 |
1.89e-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: 320.42 E-value: 1.89e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 85 VLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYgediINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 164
Cdd:cd14937 3 VLNMLALRY-KKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 165 SGAGKTVSAKYAMRYFatVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 244
Cdd:cd14937 78 SGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 245 EKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGgSPVIEGVDDAKEMAHTRQACTLLGISEsYQMG 324
Cdd:cd14937 156 ENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNK-NVVIPEIDDAKDFGNLMISFDKMNMHD-MKDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 325 IFRILAGILHLGNVVFMSRDS---DSCTIPPKH--EPLSIFCDLMGVAFEEMSHWLCHRKLATATETYIKPISKLQATNA 399
Cdd:cd14937 234 LFLTLSGLLLLGNVEYQEIEKggkTNCSELDKNnlELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 400 RDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 479
Cdd:cd14937 314 CKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYKA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 480 EQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTwaqkLYNTHLNKCALFEK----PRLSNKAFIIQHFAD 555
Cdd:cd14937 394 EDILIESVKYTTNESIIDLLRGKTSIISILEDSCLGPVKNDES----IVSVYTNKFSKHEKyastKKDINKNFVIKHTVS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkavsptSATSSGRtpltrtpskptkgrpgqtakehKKTV 635
Cdd:cd14937 470 DVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE------VSESLGR----------------------KNLI 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAgFPSRWTYQEFFSRYRVL-- 713
Cdd:cd14937 522 TFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNISFF-FQYKYTFDVFLSYFEYLdy 600
|
650 660 670
....*....|....*....|....*....|....*...
gi 2015234411 714 MKQKDVLSDRKQTCKNVLEKlIVDKDKYQFGKTKIFFR 751
Cdd:cd14937 601 STSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
85-751 |
1.15e-93 |
|
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: 320.03 E-value: 1.15e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 85 VLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 164
Cdd:cd01386 3 VLHTLRQRY-GANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 165 SGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 244
Cdd:cd01386 82 SGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 245 EKSRVVFQAEEERNYHIFYQLCASANLPEFKALRL---GDANNFhytnqGGSPVIEGVD---DAKEMAHTRQACTLLGIS 318
Cdd:cd01386 162 ERSRVARRPEGESNFNVFYYLLAGADAALRTELHLnqlAESNSF-----GIVPLQKPEDkqkAAAAFSKLQAAMKTLGIS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 319 ESYQMGIFRILAGILHLGNvvfmsrdSDSCTIPP-------KHEPLSIFCDLMGVAFEEMSHWLCHRKL------ATATE 385
Cdd:cd01386 237 EEEQRAIWSILAAIYHLGA-------AGATKAASagrkqfaRPEWAQRAAYLLGCTLEELSSAIFKHHLsggpqqSTTSS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 386 TYIKPIS------KLQATNARDALAKHIYAKLFNWIVDHVNQALHSAVKQHSFIGVLDIYGFETFE------INSFEQFC 453
Cdd:cd01386 310 GQESPARsssggpKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAhsgsqrGATFEDLC 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 454 INYANEKLQQQFNMHVFKLEQEEYMKEQIPwtlIDFYDNQPC----INLI---------------ESKLGILDLLDEECK 514
Cdd:cd01386 390 HNYAQERLQLLFHERTFVAPLERYKQENVE---VDFDLPELSpgalVALIdqapqqalvrsdlrdEDRRGLLWLLDEEAL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 515 MPKGTDDTWAQKLYnTHLNKCALFEKPRLSNKA-----FIIQHF--ADKVEYQCEGFLEKNKDTVFEEQikvlksskfkm 587
Cdd:cd01386 467 YPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSegplqFVLGHLlgTNPVEYDVSGWLKAAKENPSAQN----------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 588 LPELFQDDEKavsptsatssgrtpltrtpskptkgrpgQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPN--- 664
Cdd:cd01386 535 ATQLLQESQK----------------------------ETAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQhna 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 665 ---DFKFPFTFDEKRAVQ------QLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK-------QKDVLSDRKQTCK 728
Cdd:cd01386 587 gkdERSTSSPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPpltkklgLNSEVADERKAVE 666
|
730 740
....*....|....*....|...
gi 2015234411 729 NVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd01386 667 ELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
83-751 |
3.80e-93 |
|
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: 319.67 E-value: 3.80e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFI-------DSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDER 155
Cdd:cd14887 1 PNLLENLYQRYNkayinkeNRNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 156 NQSIIVSGESGAGKTVSAKYAMRYFATVS---GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSdrrHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYtnqggspviegvddakEMAHTRQAC 312
Cdd:cd14887 161 KLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPEST----------------DLRRITAAM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 313 TLLGISESYQMGIFRILAGILHLGNVVFMSRDSDSCTIPPKHEPLSIFCDLMGVAFEEMSHWLCHR---KLATATETYIK 389
Cdd:cd14887 225 KTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSVSVGCEETAADRSHSSEVKCLSsglKVTEASRKHLK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 390 PISKL--------------------------------QATNARDALAKHIYAKLFNWIVDHVNQALHSAVK--------- 428
Cdd:cd14887 305 TVARLlglppgvegeemlrlalvsrsvretrsffdldGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsded 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 429 -----QHSFIGVLDIYGFETFE---INSFEQFCINYANEKLqqqfnmHVFKLEQ-----------EEYMKEQI------- 482
Cdd:cd14887 385 tpsttGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERL------HCFLLEQlilnehmlytqEGVFQNQDcsafpfs 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 483 ----------PWTLIDF-----------YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKP 541
Cdd:cd14887 459 fplastltssPSSTSPFsptpsfrsssaFATSPSLPSSLSSLSSSLSSSPPVWEGRDNSDLFYEKLNKNIINSAKYKNIT 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 542 R---LSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEqikvlksskfkmLPELFqddekavsptsatSSGRTPLTRTPSK 618
Cdd:cd14887 539 PalsRENLEFTVSHFACDVTYDARDFCRANREATSDE------------LERLF-------------LACSTYTRLVGSK 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 619 PTKGRpgQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFP 698
Cdd:cd14887 594 KNSGV--RAISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFP 671
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 2015234411 699 SRWTYQEFFSRY--RVLMKQKDVLSDrKQTCKNVLEKLIVDKDKYQFGKTKIFFR 751
Cdd:cd14887 672 CRLPYVELWRRYetKLPMALREALTP-KMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
84-750 |
4.90e-92 |
|
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: 313.20 E-value: 4.90e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 84 AVLHNLRVRFIDSKLiYTYCGIVLVAINPYEqlpiygeDIINAY---SGQNMGDMdPHIFAVAEEAYKQMARDERNQSII 160
Cdd:cd14881 2 AVMKCLQARFYAKEF-FTNVGPILLSVNPYR-------DVGNPLtltSTRSSPLA-PQLLKVVQEAVRQQSETGYPQAII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 161 VSGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKryriiGANMR 240
Cdd:cd14881 73 LSGTSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-----GALYR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 241 T----YLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLG--DANNFHYTNQgGSPVIEGVDDAKEMAHTRQACTL 314
Cdd:cd14881 148 TkihcYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgySPANLRYLSH-GDTRQNEAEDAARFQAWKACLGI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 315 LGISESyqmGIFRILAGILHLGNVVFMsrDSDSCTIPPKHE-PLSIFCDLMGVAFEEMshwlcHRKLATATET----YIK 389
Cdd:cd14881 227 LGIPFL---DVVRVLAAVLLLGNVQFI--DGGGLEVDVKGEtELKSVAALLGVSGAAL-----FRGLTTRTHNargqLVK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 390 PISKLQATNA-RDALAKHIYAKLFNWIVDHVN--QALHSAVKQHS---FIGVLDIYGFETFEINSFEQFCINYANEKLQQ 463
Cdd:cd14881 297 SVCDANMSNMtRDALAKALYCRTVATIVRRANslKRLGSTLGTHAtdgFIGILDMFGFEDPKPSQLEHLCINLCAETMQH 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 464 QFNMHVFKLEQEEYMKEQIPWTL-IDFYDNQPCINLIES-KLGILDLLDEECKmPKGTDDTWAQKLYNTHLNKCALFEKP 541
Cdd:cd14881 377 FYNTHIFKSSIESCRDEGIQCEVeVDYVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 542 RLSNKAFIIQHFADKVEYQCEGFLEKNKDTVfeeqikvlksskfkmlpelfQDDEKAVSPTSATSSGRtpLTRTpskptk 621
Cdd:cd14881 456 PQDDRMFGIRHFAGRVVYDASDFLDTNRDVV--------------------PDDLVAVFYKQNCNFGF--ATHT------ 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 622 grpgqtakehkktvgHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRW 701
Cdd:cd14881 508 ---------------QDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRM 572
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 702 TYQEFFSRYRVL--MKQKDVLSDRKQTCKNVLEKLIVDKDK---------YQFGKTKIFF 750
Cdd:cd14881 573 RFKAFNARYRLLapFRLLRRVEEKALEDCALILQFLEAQPPsklssvstsWALGKRHIFL 632
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
97-751 |
2.20e-91 |
|
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: 312.80 E-value: 2.20e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 97 KLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSgQNMGdMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKY 175
Cdd:cd14905 14 EIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN-QRRG-LPPHLFALAAKAISDMQDFRRDQLIFIGGESGSGKSENTKI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 176 AMRYFATVSGSASEAnVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEE 255
Cdd:cd14905 92 IIQYLLTTDLSRSKY-LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQNKG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 256 ERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPVIEGVDDAKEMAHTRQACTLLGISESYQMGIFRILAGILHL 335
Cdd:cd14905 171 ERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFIIIL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 336 GNVVFMSRDSDSctiPPKHEPLsifcdlmgvaFEEMSHWLCHRklATATETYI---KPISKLQATNARDALAKHIYAKLF 412
Cdd:cd14905 251 GNVTFFQKNGKT---EVKDRTL----------IESLSHNITFD--STKLENILisdRSMPVNEAVENRDSLARSLYSALF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 413 NWIVDHVNQALHSAVKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPW-TLIDFYD 491
Cdd:cd14905 316 HWIIDFLNSKLKPTQYSHT-LGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWmTPISFKD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 492 NQPCINLIESklgILDLLDEECKMPKGTDDTWAQKLYNtHLNKCALF-EKPrlsNKaFIIQHFADKVEYQCEGFLEKNKD 570
Cdd:cd14905 395 NEESVEMMEK---IINLLDQESKNINSSDQIFLEKLQN-FLSRHHLFgKKP---NK-FGIEHYFGQFYYDVRGFIIKNRD 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 571 TVFEEQIKVLKSSKFKML-------------PELFQD-DEKAVSPTSATSSGRTPLT---------RTPSKPTKGRPGQT 627
Cdd:cd14905 467 EILQRTNVLHKNSITKYLfsrdgvfninatvAELNQMfDAKNTAKKSPLSIVKVLLScgsnnpnnvNNPNNNSGGGGGGG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 628 AKEHKKTVGHQFRNSLHLLMETLNATTP--HYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14905 547 NSGGGSGSGGSTYTTYSSTNKAINNSNCdfHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKI 626
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 2015234411 706 FFSRYRVLMKQkdvlsdrKQTCKNVLEKLI---VDKDK-----YQFGKTKIFFR 751
Cdd:cd14905 627 FFDRFSFFFQN-------QRNFQNLFEKLKendINIDSilpppIQVGNTKIFLR 673
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
83-750 |
3.58e-88 |
|
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: 303.75 E-value: 3.58e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYS-------GQNMGDMDPHIFAVAEEAYKQMARDE 154
Cdd:cd14884 1 PNVLQNLKNRYLKNK-IYTFHASLLLALNPYKPLKeLYDQDVMNVYLhkksnsaASAAPFPKAHIYDIANMAYKNMRGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 155 RNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR--- 231
Cdd:cd14884 80 KRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVent 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 232 ------YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQL---CASANLPEFKALR----------------LGDANNFH 286
Cdd:cd14884 160 qknmfnGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVlrgLSDEDLARRNLVRncgvygllnpdeshqkRSVKGTLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 287 YTNQGGSPVIEGVD-DAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNvvfmsrDSDSCTippkheplsifCDLMG 365
Cdd:cd14884 240 LGSDSLDPSEEEKAkDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGN------RAYKAA-----------AECLQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 366 VAFEEMSHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQAL------------HSAVKQHSFI 433
Cdd:cd14884 303 IEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdesdneDIYSINEAII 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 434 GVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESklgILDLLDEEC 513
Cdd:cd14884 383 SILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAK---IFRRLDDIT 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 514 KMP----KGTDDTWAQKLYNTHlNKCALFEK-------PRL---SNKA-------FIIQHFADKVEYQCEGFLEKNKDTV 572
Cdd:cd14884 460 KLKnqgqKKTDDHFFRYLLNNE-RQQQLEGKvsygfvlNHDadgTAKKqnikkniFFIRHYAGLVTYRINNWIDKNSDKI 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 573 fEEQIKVLKSskfkmlpelfqddekavsptsaTSSGRTpLTRTPSKPTKGrpgqtakeHKKTVGHQFRNSLHLLMETLNA 652
Cdd:cd14884 539 -ETSIETLIS----------------------CSSNRF-LREANNGGNKG--------NFLSVSKKYIKELDNLFTQLQS 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 653 TTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkQKDVLSDRKQTCKNVLE 732
Cdd:cd14884 587 TDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKETAAALKEQI-AKELEKCNSNTDIEYQR 665
|
730
....*....|....*...
gi 2015234411 733 KLIVDKDKYQFGKTKIFF 750
Cdd:cd14884 666 RLAALDVQFIPDGRLYAF 683
|
|
| Myo5-like_CBD |
cd14945 |
Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied ... |
1504-1827 |
1.07e-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: 282.37 E-value: 1.07e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1504 EDEQKLVKNLILELKPRGVAVNLipgLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNT 1583
Cdd:cd14945 1 SEEDSLLRGIVTDFEPSSGDHKL---TPAYILYLCIRHAASNGLTGQSTSLLNKVLKTIQQVVQQHNDDMQLLAFWLSNA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1584 CRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmivsgmlehetiqgvsgv 1663
Cdd:cd14945 78 SELLYFLKQDSKLYGAAGEAPQKEEEQKLTVSDLNELKQDLEAVSIKIYQQALKYLNKNLQP------------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1664 kptglrkrtssiadegtyTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAVTLNNLLLRKDMCSWSKGMQIRY 1743
Cdd:cd14945 140 ------------------KIRDIVKFLNSFLDLLKSFHVHPEIRSQVFTQLFSFINARLFNQLITKKDALSWSRGMQIRA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1744 NVSQLEEWLRDKNLmNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFI 1823
Cdd:cd14945 202 NISRLEEWCEGRGL-EHLAVDFLSKLIQAVQLLQLKKYTQEDIEILCELCPSLNPAQLQAILTQYQPANYGESPVPKEIL 280
|
....
gi 2015234411 1824 RTIQ 1827
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 |
1.72e-82 |
|
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: 285.23 E-value: 1.72e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYsgqnmgdmdpHIFAVAEEAYKQMARDERN-QSIIVS 162
Cdd:cd14874 2 GIAQNLHERF-KKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 163 GESGAGKTVSAKYAMRYFATVSGSASEAnveEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMR-T 241
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTT---KHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLNLKyT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 242 YLLEKSRVVFQAEEERNYHIFYQLCASANlPEFKA-LRLGDANNFHYTNQGGSpvIEGV-DDAKEMAHTRQACTLLGISE 319
Cdd:cd14874 147 VPLEVPRVISQKPGERNFNVFYEVYHGLN-DEMKAkFGIKGLQKFFYINQGNS--TENIqSDVNHFKHLEDALHVLGFSD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 320 SYQMGIFRILAGILHLGNVVFMSR-----DSDSCTIPPKHEpLSIFCDLMGVAFEEMSHWLchrklaTATETYIKPISKL 394
Cdd:cd14874 224 DHCISIYKIISTILHIGNIYFRTKrnpnvEQDVVEIGNMSE-VKWVAFLLEVDFDQLVNFL------LPKSEDGTTIDLN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 395 QATNARDALAKHIYAKLFNWIVD----HVNQALHSAVkqhsfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14874 297 AALDNRDSFAMLIYEELFKWVLNriglHLKCPLHTGV-----ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 471 KLEQEEYMKEQIPwtlIDF-----YDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCAlFEKPRLS 544
Cdd:cd14874 372 HDQLVDYAKDGIS---VDYkvpnsIENGKTVELLFKKpYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS-YGKARNK 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 545 NK-AFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQddekavSPTSATSsgrtpltrtpskptkgr 623
Cdd:cd14874 448 ERlEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE------SYSSNTS----------------- 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 624 pgqtakEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTY 703
Cdd:cd14874 505 ------DMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISK 578
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 2015234411 704 QEFFSRYRVLMKqKDV--LSDRKQTCKNVLEKLIVD-KDKYQFGKTKIFFR 751
Cdd:cd14874 579 TTFARQYRCLLP-GDIamCQNEKEIIQDILQGQGVKyENDFKIGTEYVFLR 628
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
86-750 |
2.30e-73 |
|
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: 261.83 E-value: 2.30e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 86 LHNLRVRF-IDSklIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQN----------MGDMDPHIFAVAEEAYKQMARDE 154
Cdd:cd14893 4 LYTLRARYrMEQ--VYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSReqtplyekdtVNDAPPHVFALAQNALRCMQDAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 155 RNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEAN-----------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKY 223
Cdd:cd14893 82 EDQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPdsegasgvlhpIGQQILHAFTILEAFGNAATRQNRNSSRFAKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 224 IEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANL-PEFK-ALRLGD-ANNFHYTNQGGSPVIEGVD 300
Cdd:cd14893 162 ISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdPTLRdSLEMNKcVNEFVMLKQADPLATNFAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 301 DAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVVFMS----------------RDSDSCTIppkHEPLSIF--CD 362
Cdd:cd14893 242 DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPdpeggksvggansttvSDAQSCAL---KDPAQILlaAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 363 LMGVAFEEMSHWLCHRKL----ATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQAL---------HSAVKQ 429
Cdd:cd14893 319 LLEVEPVVLDNYFRTRQFfskdGNKTVSSLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdryekSNIVIN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 430 HSFIGVLDIYGFETFE--INSFEQFCINYANEKLQQQF-------NMHVFKLEQEEYMKEQIPWTLIDF-YDNQPCINLI 499
Cdd:cd14893 399 SQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvqntlaiNFSFLEDESQQVENRLTVNSNVDItSEQEKCLQLF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 500 ESK-LGILDLLDEECKMPKGTDDTWAQKLYN--------THLNKCALFEKPRLSNKA-----FIIQHFADKVEYQCEGFL 565
Cdd:cd14893 479 EDKpFGIFDLLTENCKVRLPNDEDFVNKLFSgneavgglSRPNMGADTTNEYLAPSKdwrllFIVQHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 566 EKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAVSPTSATSSGrtplTRTPSKPTKGRPGQTAKEHKKTVGH----QFRN 641
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAAKQT----EERGSTSSKFRKSASSARESKNITDsaatDVYN 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 642 SLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYrvlmkqKDVLS 721
Cdd:cd14893 635 QADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY------KNVCG 708
|
730 740 750
....*....|....*....|....*....|...
gi 2015234411 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 |
3.17e-63 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 229.24 E-value: 3.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 85 VLHNLRVRfIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 164
Cdd:cd14882 3 ILEELRHR-YLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 165 SGAGKTVSAKYAMRYFATVSGSASeaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 244
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNR--GATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 245 EKSRVVFQAEEERNYHIFY----QLCASANLPEFKalrLGDANNFHY----TNQGGSPVIEGVDD----AKEMAHTRQAC 312
Cdd:cd14882 160 EKLRVSTTDGNQSNFHIFYyfydFIEAQNRLKEYN---LKAGRNYRYlripPEVPPSKLKYRRDDpegnVERYKEFEEIL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 313 TLLGISESYQMGIFRILAGILHLGNVVFmsRDSDSCTIPPKHEPLSIFCDLMGVAfEEMSHW----LCHRKLATATEtyi 388
Cdd:cd14882 237 KDLDFNEEQLETVRKVLAAILNLGEIRF--RQNGGYAELENTEIASRVAELLRLD-EKKFMWaltnYCLIKGGSAER--- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 389 KPISKLQATNARDALAKHIYAKLFNWIVDHVNQALH--SAV--KQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQ 464
Cdd:cd14882 311 RKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSfpRAVfgDKYS-ISIHDMFGFECFHRNRLEQLMVNTLNEQMQYH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 465 FNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCI-NLIESKLGILDLLDEECKMPKGtddtwAQKLYNTHLNKCALFEKPrL 543
Cdd:cd14882 390 YNQRIFISEMLEMEEEDIPTINLRFYDNKTAVdQLMTKPDGLFYIIDDASRSCQD-----QNYIMDRIKEKHSQFVKK-H 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 544 SNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekavsptsaTSSgrtpltrtpskptkgr 623
Cdd:cd14882 464 SAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMF------------TNS---------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 624 pgQTAKehKKTVGHQFRNSLHLLMETL----NATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPS 699
Cdd:cd14882 516 --QVRN--MRTLAATFRATSLELLKMLsigaNSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSY 591
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 2015234411 700 RWTYQEFFSRYRVLMKQKDVLSD-RKQTCKNVLEKLIVdkDKYQFGKTKIFFR 751
Cdd:cd14882 592 RIPFQEFLRRYQFLAFDFDETVEmTKDNCRLLLIRLKM--EGWAIGKTKVFLK 642
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
106-229 |
7.78e-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: 7.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 106 VLVAINPYEQLPIYGED-IINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVS 184
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2015234411 185 GSASEAN--------------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFD 229
Cdd:cd01363 81 FNGINKGetegwvylteitvtLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLD 139
|
|
| DIL |
pfam01843 |
DIL domain; The DIL domain has no known function. |
1709-1812 |
6.72e-42 |
|
DIL domain; The DIL domain has no known function.
Pssm-ID: 460359 [Multi-domain] Cd Length: 103 Bit Score: 149.28 E-value: 6.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1709 QVVKQMFYIVGAVTLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLmNSGAKETLEPLIQAAQLLQVKKKTDDDAEA 1788
Cdd:pfam01843 1 QLFSQLFYFINAELFNRLLLRKKYCSWSKGMQIRYNLSRLEEWARSNGL-ESEARDHLAPLIQAAQLLQLRKSTLEDLDS 79
|
90 100
....*....|....*....|....
gi 2015234411 1789 ICSMCNALTTAQIVKVLNLYTPVN 1812
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 |
2.94e-38 |
|
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: 154.99 E-value: 2.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 83 PAVLHNLRVRFIDSKLiYTYCGIVLVAINPYEQLPIYGEDIINAYSGQN-MGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14938 1 PSVLYHLKERFKNNKF-YTKMGPLLIFINPKINNNINNEETIEKYKCIDcIEDLSLNEYHVVHNALKNLNELKRNQSIII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 162 SGESGAGKTVSAKYAMRYFA-TVSGSASEA---------------------NVEEKVLASNPIMESIGNAKTTRNDNSSR 219
Cdd:cd14938 80 SGESGSGKSEIAKNIINFIAyQVKGSRRLPtnlndqeednihneentdyqfNMSEMLKHVNVVMEAFGNAKTVKNNNSSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 220 FGKYIEIGFDKRyRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASANLPEFKALRLGDANNFHYTNQGGSPVIEGV 299
Cdd:cd14938 160 FSKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 300 DDAKEMAHTRQACTLLGISESYQMgIFRILAGILHLGNV----------VFMSRDSDSCTIppkhEPLSIFCDL-----M 364
Cdd:cd14938 239 YSGKILELLKSLNYIFDDDKEIDF-IFSVLSALLLLGNTeivkafrkksLLMGKNQCGQNI----NYETILSELensedI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 365 GVAFEEMSHWLCHRKLATATETYIKPIS---------------KLQATNARDALAKHIYAKLFNWIVDHVNQ---ALHSA 426
Cdd:cd14938 314 GLDENVKNLLLACKLLSFDIETFVKYFTtnyifndsilikvhnETKIQKKLENFIKTCYEELFNWIIYKINEkctQLQNI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 427 VKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTL-IDFYDNQPCIN-LIESKLG 504
Cdd:cd14938 394 NINTNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNlLVGPTEG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 505 ILDLLDEECKMPKGTDDTwaqKLYNTHLNKCA-----LFEKPRLSN-KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIK 578
Cdd:cd14938 474 SLFSLLENVSTKTIFDKS---NLHSSIIRKFSrnskyIKKDDITGNkKTFVITHSCGDIIYNAENFVEKNIDILTNRFID 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 579 VLKSSKFKMLpelfqddEKAVSPTSATSSG------RTPLTRTPSKPTKgRPGQTAKEHKKTVghqFRNSLHLLMETLNA 652
Cdd:cd14938 551 MVKQSENEYM-------RQFCMFYNYDNSGniveekRRYSIQSALKLFK-RRYDTKNQMAVSL---LRNNLTELEKLQET 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 653 TTPHYVRCIKPNDFK-FPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkqkdvlSDRKQTCKNVL 731
Cdd:cd14938 620 TFCHFIVCMKPNESKrELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKN------EDLKEKVEALI 693
|
730
....*....|....*...
gi 2015234411 732 EKLIVDKDKYQFGKTKIF 749
Cdd:cd14938 694 KSYQISNYEWMIGNNMIF 711
|
|
| Myo5p-like_CBD_DIL_ANK |
cd15473 |
cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ... |
1530-1859 |
2.57e-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: 126.52 E-value: 2.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1530 LPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNTCRFLHCLKQysgEEGFmkhntsrqne 1609
Cdd:cd15473 32 VPANLLFLCARYAHYHCSPELLEDLLLGALDRIEDVVEANPWDMTLLAFWLSNVTLLLHYLKK---DAGL---------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1610 hcltNFDLAEYRQVLSDLAIQIYQQLVRVLEnilqpmivsgmlehetiqgvsgvkptglrKRTSSIADEGTYTLDSIlrq 1689
Cdd:cd15473 99 ----VEATPEFQQELAELINEIFVLIIRDAE-----------------------------RRIDKLLDASPRNITSL--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1690 LNSFHSVMCQHGMDPELIKQVVKQMFYIVGAVTLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLM-------NSGA 1762
Cdd:cd15473 143 LSSTLYVLELYDVHPAIIIQALSQLFYWLGCELFNRILTNKKYLCRSKAMQIRMNLSALEDWARSNNLQpekgespPRIA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1763 KETLEPLIQAAQLLQVKKKTDDDAEAICSM--CNALTTAQIVKVLNLYTP-VNefEERVSVSFIRTIQMRLRDRKDSpql 1839
Cdd:cd15473 223 RSHLAPVIQLLQWLQCLSSLDDFESLIATIqqLDALNPLQLLRAVKDYRYeVN--EGRMPEECVKYLAQLQKDWLDS--- 297
|
330 340
....*....|....*....|
gi 2015234411 1840 lmdaKHIFPVTFPFNPSSLA 1859
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 |
1.63e-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: 128.32 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 196 VLASNPIMESIGNAKTTRNDNSSRFGKY--IEIGFDK---RYRIIGANMRTYLLEKSRVVFQA------EEERNYHIFYQ 264
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLhpwEFQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 265 LCASANLPEF-----KALRLG--DANNFHYTNQGGSPVIEGVD-------DAKEMAHTRQACTLLGISESYQMGIFRILA 330
Cdd:cd14894 329 MVAGVNAFPFmrllaKELHLDgiDCSALTYLGRSDHKLAGFVSkedtwkkDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 331 GILHLGNVVFMSRDSDSCTIPPK----HEPLSIFCDLMGVAFEEMSHWLCHRK--LATATETYIKPISKLQATNARDALA 404
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSStgalNAPQKVVELLELGSVEKLERMLMTKSvsLQSTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 405 KHIYAKLFNWIVDHVNQALH-----------------SAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQqfnm 467
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEATKmsalstdgnkhqmdsnaSAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYA---- 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 468 hvfKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKLGILDLLdEECKMPKGTDDTWAQ------KLYNTHL---NKCALF 538
Cdd:cd14894 565 ---REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASL-EELTILHQSENMNAQqeekrnKLFVRNIydrNSSRLP 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 539 EKPRLSNKA------------FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekavsptsATS 606
Cdd:cd14894 641 EPPRVLSNAkrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNE---------SSQ 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 607 SGRTPLTrtpSKPTKGRPGQTAKEHKKTVGhQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGV 686
Cdd:cd14894 712 LGWSPNT---NRSMLGSAESRLSGTKSFVG-QFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRL 787
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2015234411 687 ---LETIRISAAGFPS-RWTYQEFFSRYRVLMKQKDVLSDRKQTCKNVLEKL 734
Cdd:cd14894 788 irqMEICRNSSSSYSAiDISKSTLLTRYGSLLREPYILDDVAGDNSNLMNWL 839
|
|
| Myo5p-like_CBD_fungal |
cd15474 |
cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin ... |
1509-1853 |
3.54e-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: 120.99 E-value: 3.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1509 LVKNLILELKPRGVAVN----LIPGLPAYILFMCVRHADYLNDDQKVRSL--LTSTINSIKKVLKKRgDDFETVSFWLSN 1582
Cdd:cd15474 11 LKSVEVLELKDISDEVSgdnlLFLGHVNFLIYSQMWKSLLELLTQSERFLshVLSYIASIVDSLPKK-ETIPDGAFWLAN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1583 TCRFLHCL--KQYSGEEGFMKHNTSRQNEHCLTNFDlaEYRQVLSdlaiQIYQQLVRVLENILQPMIVSGMLEHETIQGV 1660
Cdd:cd15474 90 LHELRSFVvyLLSLIEHSSSDEFSKESEEYWNTLFD--KTLKHLS----NIYSTWIDKLNKHLSPKIEGAVLVLLTSLDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1661 SGvkptgLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAVTLNNLLLRKDMCSWSKGMQ 1740
Cdd:cd15474 164 SE-----LIDLNKEFFNKPKKKMADLITFLNEVYDLLQSFSVQPELLNAIVSSTLQYINVEAFNSLITKRSALSWKRGSQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1741 IRYNVSQLEEWLRDKNLmnSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNeFEERVSV 1820
Cdd:cd15474 239 ISYNVSRLKEWCHQHGL--SDANLQLEPLIQASKLLQLRKDDENDFKIILSVCYALNPAQIQKLLDKYQPAN-YEAPVPK 315
|
330 340 350
....*....|....*....|....*....|....
gi 2015234411 1821 SFIRTI-QMRLRDRKDSPQLLMDAKHIFPVTFPF 1853
Cdd:cd15474 316 EFLNALeKLIKKENLSLPGRKNNSKMEIPESSNF 349
|
|
| fMyo2p_CBD |
cd15480 |
cargo binding domain of fungal myosin 2; Yeast myosin V travels along actin cables, actin ... |
1682-1877 |
5.96e-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: 120.76 E-value: 5.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1682 TLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAVTLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNlMNSG 1761
Cdd:cd15480 167 TMDDILNFFNKVYKSMKSYYIEESVIRQVVTELLKLIGVTAFNDLLMRRNFLSWKRGLQINYNITRLEEWCKSHD-IPEG 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1762 AkETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTpVNEFEERVSVSFIRTIQMRLR--DRKDSPQL 1839
Cdd:cd15480 246 T-LQLEHLMQATKLLQLKKATLEDIEIIYDVCWILTPAQIQKLISQYY-VADYENPISPEILKAVAARVKpeDKSDHLLL 323
|
170 180 190
....*....|....*....|....*....|....*...
gi 2015234411 1840 LMDAKHIFPVTFPFNPSSLALETIqIPASLGLGFISRV 1877
Cdd:cd15480 324 IPLVEEVGPFEDPFPREIAGLEAY-IPAWLNLPHIRRL 360
|
|
| Myo5p-like_CBD_afadin |
cd15471 |
cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and ... |
1531-1810 |
1.41e-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: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1531 PAYILFMCVRH---ADYLNDD------QKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNTCRFLHCLKQysgeegfmk 1601
Cdd:cd15471 25 PAYTLYLAARYrlsTHYRPELtpteraHKLTAFLNKIASLIQQVIQEQRNIAGALAFWMANASELLNFLKQ--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1602 hntsrqnEHCLTNFDLaEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSGVKPTglrkrtssiadegTY 1681
Cdd:cd15471 96 -------DRDLSAFSV-QAQDVLAEAVQSAFSYLVRCLQEELERSLPAFLDSLVSLDDEPAIGDV-------------LH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1682 TLDSILRQLNsfhsvmcQHGMDPELIKQVVKQMFYIVGAVTLNNLLLRKD--MCSWSKGMQIRYNVSQLEEWLrDKNLMN 1759
Cdd:cd15471 155 TLSSAMRLLR-------RCRVNAALTIQLFSQLFHFINAWLFNSLVSNPDsgLCTRYWGKRLRQRLAHVEAWA-ERQGLE 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2015234411 1760 SGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTP 1810
Cdd:cd15471 227 LAADCHLDRIVQAANLLTAPKYSAEDVANLSSTCFKLNSLQLRALLSHYQP 277
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
902-1281 |
2.50e-15 |
|
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: 82.41 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 902 KRELKKLKIEARSVERYKKLHigmeNKIMQLQRKVdeQNKDYKCLMEKLTNLEGTYNSETEKLRSDLERLQLSEEEAKIA 981
Cdd:TIGR02168 199 ERQLKSLERQAEKAERYKELK----AELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 982 TGRVLSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQekealnhriVEQAKEMTETMEKKLV 1061
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE---------LESKLDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1062 EETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmvnvpkpghKRTDSTHSSNESEYTFSSEI----AETEDIP 1137
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLE----------TLRSKVAQLELQIASLNNEIerleARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1138 SRTEEPSEKKVPLDMSL----FLKLQKRVTELEQEKQVMQDELDRKEEQvlrskaKEEERPQIRGAELEYESLKRQELES 1213
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLeeaeLKELQAELEELEEELEELQEELERLEEA------LEELREELEEAEQALDAAERELAQL 487
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2015234411 1214 ENKK--LKNELNELRKALSEKSSPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLV------SQKEAIQ 1281
Cdd:TIGR02168 488 QARLdsLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVvvenlnAAKKAIA 563
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
901-1467 |
1.65e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.34 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 901 AKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGtynsETEKLRSDLERL--------Q 972
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELRE----ELEKLEKEVKELeelkeeieE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 973 LSEEEAKIaTGRVLSLQEEIAKLR----------KDLEQTRSEKKSIEEHADRY------KQETEQLVSNLKEENTLLKQ 1036
Cdd:PRK03918 243 LEKELESL-EGSKRKLEEKIRELEerieelkkeiEELEEKVKELKELKEKAEEYiklsefYEEYLDELREIEKRLSRLEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1037 EKEALNHRIVEqakemTETMEKKLVEETKQLEldlnderlryqNLLNEFSRLEERYDDLKEEMTLMVNVPKpghkrtdst 1116
Cdd:PRK03918 322 EINGIEERIKE-----LEEKEERLEELKKKLK-----------ELEKRLEELEERHELYEEAKAKKEELER--------- 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1117 HSSNESEYTFSSEIAETEDIPSRTEEPSEKkvpldmslFLKLQKRVTELEQEKQVMQDELDRKEEQ-----VLRSKAKEE 1191
Cdd:PRK03918 377 LKKRLTGLTPEKLEKELEELEKAKEEIEEE--------ISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1192 ERPQIRG---AELEYESLKRQELESENKKLKNELNELRKALSEKssPEVTapgapAYRVLMEQLTSVSEELDVR------ 1262
Cdd:PRK03918 449 HRKELLEeytAELKRIEKELKEIEEKERKLRKELRELEKVLKKE--SELI-----KLKELAEQLKELEEKLKKYnleele 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1263 ---------KEEVLILRSQLVSQKEAIQPKNTMTDSTILLEdvqKMKDKGEIAQAYIgLKETNRSSAMDCHELNED-GEL 1332
Cdd:PRK03918 522 kkaeeyeklKEKLIKLKGEIKSLKKELEKLEELKKKLAELE---KKLDELEEELAEL-LKELEELGFESVEELEERlKEL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1333 LLVYE---GLKQANRLLESQLQSQKRShENEAEALRGEIQSLkeennrqqqllaqnlqlppEARIEaSLQHEITRLtnEN 1409
Cdd:PRK03918 598 EPFYNeylELKDAEKELEREEKELKKL-EEELDKAFEELAET-------------------EKRLE-ELRKELEEL--EK 654
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2015234411 1410 LYFEELYADDPKKYQSYRiSLYKRMIDLMEQLEKQ----DKTVRKLKKQLKVFAKKIGELEV 1467
Cdd:PRK03918 655 KYSEEEYEELREEYLELS-RELAGLRAELEELEKRreeiKKTLEKLKEELEEREKAKKELEK 715
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
902-1281 |
7.64e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 77.42 E-value: 7.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 902 KRELKKLKIEARSVERYKKLHI---------------GMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGTYNSETEKLRs 966
Cdd:TIGR02169 197 RQQLERLRREREKAERYQALLKekreyegyellkekeALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 967 dlerlQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTRSekkSIEEHADRYKQETEQLVsNLKEENTLLKQEKEALNHRIV 1046
Cdd:TIGR02169 276 -----ELNKKIKDLGEEEQLRVKEKIGELEAEIASLER---SIAEKERELEDAEERLA-KLEAEIDKLLAEIEELEREIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1047 EQAKEMTETME--KKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMtlmvnvpkpghkrtdsthssNESEY 1124
Cdd:TIGR02169 347 EERKRRDKLTEeyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI--------------------NELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1125 TFSSEIAETEDIPSRTEEpsekkvpLDMSLFLKLQKrVTELEQEKQVMQDELDRKEEQVLRSKA-KEEERPQIRGAELEY 1203
Cdd:TIGR02169 407 ELDRLQEELQRLSEELAD-------LNAAIAGIEAK-INELEEEKEDKALEIKKQEWKLEQLAAdLSKYEQELYDLKEEY 478
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2015234411 1204 eslkrQELESENKKLKNELNELrKALSEKSSPEVtapgaPAYRvlmeqltSVSEELDVRKEEVLILRSQLVSQKEAIQ 1281
Cdd:TIGR02169 479 -----DRVEKELSKLQRELAEA-EAQARASEERV-----RGGR-------AVEEVLKASIQGVHGTVAQLGSVGERYA 538
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
957-1231 |
1.29e-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: 76.63 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 957 YNSETEKLRSDLERLQLSEEEAKIATGRVLS----LQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQL---VSNLKE 1029
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKeleeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLeerIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1030 ENTLLKQEKEALNHRIVEQAKEMTETMEK--KLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMtlmvnvpk 1107
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEieELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL-------- 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1108 pghkrtdsthssNESEYTFSSEIAETEDIPSRTEEPSEKkvpldmslFLKLQKRVTELEQEKQVMQDELDRKEEQvlrsK 1187
Cdd:TIGR02168 827 ------------ESLERRIAATERRLEDLEEQIEELSED--------IESLAAEIEELEELIEELESELEALLNE----R 882
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2015234411 1188 AKEEERPQIRGAELEYESLKRQELESENKKLKNELNELRKALSE 1231
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
898-1460 |
1.35e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.26 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 898 RMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGTYnSETEKLRSDLE--RLQLSE 975
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV-KELEELKEEIEelEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 976 EEAKIAT--GRVLSLQEEIAKLRK---DLEQTRSEKKSIEEHADRY------KQETEQLVSNLKEENTLLKQEKEALNHR 1044
Cdd:PRK03918 250 LEGSKRKleEKIRELEERIEELKKeieELEEKVKELKELKEKAEEYiklsefYEEYLDELREIEKRLSRLEEEINGIEER 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1045 IVEqakemTETMEKKLVEETKQLEldlnderlryqNLLNEFSRLEERYDDLKEEMTLMVNVPKpghkrtdstHSSNESEY 1124
Cdd:PRK03918 330 IKE-----LEEKEERLEELKKKLK-----------ELEKRLEELEERHELYEEAKAKKEELER---------LKKRLTGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1125 TFSSEIAETEDIPSRTEEPSEKkvpldmslFLKLQKRVTELEQEKQVMQDELDRKEEQ-----VLRSKAKEEERPQIRG- 1198
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEE--------ISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEe 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1199 --AELEYESLKRQELESENKKLKNELNELRKALSEKssPEVTApgapaYRVLMEQLTSVSEELDVR-------------- 1262
Cdd:PRK03918 457 ytAELKRIEKELKEIEEKERKLRKELRELEKVLKKE--SELIK-----LKELAEQLKELEEKLKKYnleelekkaeeyek 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1263 -KEEVLILRSQLVSQKEAIQPKNTMTDSTILLEdvqKMKDKGEIAQAYIgLKETNRSSAMDCHELNED-GELLLVYE--- 1337
Cdd:PRK03918 530 lKEKLIKLKGEIKSLKKELEKLEELKKKLAELE---KKLDELEEELAEL-LKELEELGFESVEELEERlKELEPFYNeyl 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1338 GLKQANRLLESQLQSQKRShENEAEALRGEIQSLKEENNRQqqllaqnlqlppEARIEASL----QHEITRLTNENLYFE 1413
Cdd:PRK03918 606 ELKDAEKELEREEKELKKL-EEELDKAFEELAETEKRLEEL------------RKELEELEkkysEEEYEELREEYLELS 672
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1414 ELYA---DDPKKYQSYRISLYKRMIDLMEQLEKQDKTVRKLKKQLKVFAK 1460
Cdd:PRK03918 673 RELAglrAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALER 722
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
902-1280 |
1.66e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.13 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 902 KRELKKLKIEARSVERYKKLHIGMEnkimqlQRKVDEQNKDYKCLMEKLTNLEGTYNSETEKLRSDLERLQLSEEEAKIA 981
Cdd:COG1196 199 ERQLEPLERQAEKAERYRELKEELK------ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 982 TGRVLSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKEentlLKQEKEALNHRIVEQAKEMTETMEKKLV 1061
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE----LEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1062 EETK--QLELDLNDERLRYQNLLNEFSRLEERYDDLKEEmtlmvnvpkpghkrtdstHSSNESEytfSSEIAETEDIPSR 1139
Cdd:COG1196 349 AEEEleEAEAELAEAEEALLEAEAELAEAEEELEELAEE------------------LLEALRA---AAELAAQLEELEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1140 TEEpsekkvpldmslflKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEErpqiRGAELEYESLKRQELESENKKLK 1219
Cdd:COG1196 408 AEE--------------ALLERLERLEEELEELEEALAELEEEEEEEEEALEE----AAEEEAELEEEEEALLELLAELL 469
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2015234411 1220 NELNELRKALSEKSSPEVTApgAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAI 1280
Cdd:COG1196 470 EEAALLEAALAELLEELAEA--AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
942-1466 |
7.89e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 7.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 942 DYKCLMEKLTNLEGTYNSETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKqETE 1021
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-ELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1022 QLVSNLKEENTLLKQEKEALNHRIVEqakemTETMEKKLVEETKQLEldlndERLRYqnlLNEFSRLEERYDDLKEEMTL 1101
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRE-----LEERIEELKKEIEELE-----EKVKE---LKELKEKAEEYIKLSEFYEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1102 MVNVPKPGHKRTDSTHSSNESeytFSSEIAETEDIPSRTEEPSEKKVpldmslflKLQKRVTELEQEKQVMQDELDRKEE 1181
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEING---IEERIKELEEKEERLEELKKKLK--------ELEKRLEELEERHELYEEAKAKKEE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1182 -QVLRSKAKEEERPQIRgAELEYESLKRQELESENKK-------LKNELNELRKALSEKSSPEVTAP--GAPA----YRV 1247
Cdd:PRK03918 374 lERLKKRLTGLTPEKLE-KELEELEKAKEEIEEEISKitarigeLKKEIKELKKAIEELKKAKGKCPvcGRELteehRKE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1248 LMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQpkntmtdstILLEDVQKMKDKGEIAQAYIGLKEtnRSSAMDCHELN 1327
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELE---------KVLKKESELIKLKELAEQLKELEE--KLKKYNLEELE 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1328 EDGELllvYEGLKQANRLLESQLQSQKRS------HENEAEALRGEIQSLKEEnnrqqqllaqnlqlppeariEASLQHE 1401
Cdd:PRK03918 522 KKAEE---YEKLKEKLIKLKGEIKSLKKElekleeLKKKLAELEKKLDELEEE--------------------LAELLKE 578
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2015234411 1402 ITRLTNENLYFEELYADDPKKYQSYRISLYKRMIDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1466
Cdd:PRK03918 579 LEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
927-1461 |
9.71e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 70.14 E-value: 9.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 927 NKIMQLQRKVDEQNKDYKCLMEKLTNLegtyNSETEKLRSDLER----LQLSEEEAKIATGRVLSLQEEIAKLRKDLEQT 1002
Cdd:pfam05483 268 DKANQLEEKTKLQDENLKELIEKKDHL----TKELEDIKMSLQRsmstQKALEEDLQIATKTICQLTEEKEAQMEELNKA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1003 RSEKKSIeehADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVEQAKEMTETMEKKLVEETKQLELD------LNDERL 1076
Cdd:pfam05483 344 KAAHSFV---VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEelkkilAEDEKL 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1077 RYQNllNEFSRLEERYDDLKEEMTLMVNV-PKPGHKRTDSTHSSNESEYTFSSEIaetEDIPSRTEEPSEKKVPLDM-SL 1154
Cdd:pfam05483 421 LDEK--KQFEKIAEELKGKEQELIFLLQArEKEIHDLEIQLTAIKTSEEHYLKEV---EDLKTELEKEKLKNIELTAhCD 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1155 FLKLQKRvtELEQEKQVMQDELDRKEEQVLRSKaKEEER--PQIRGAElEYESLKRQELESENKKLKNELNELRKALSEK 1232
Cdd:pfam05483 496 KLLLENK--ELTQEASDMTLELKKHQEDIINCK-KQEERmlKQIENLE-EKEMNLRDELESVREEFIQKGDEVKCKLDKS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1233 SspevtapgapayrvlmEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKNTMTDStiLLEDVQKMKDKGeiaqayigl 1312
Cdd:pfam05483 572 E----------------ENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE--LHQENKALKKKG--------- 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1313 keTNRSSAMDCHELNEDgELLLVYEGLKQANRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLlaqnlqlppEA 1392
Cdd:pfam05483 625 --SAENKQLNAYEIKVN-KLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKL---------QK 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1393 RIEASLQHEITRLT-----NENLY---FEE------LYADDPKKYQSYRISLYKRMIDLMEQL---EKQDKTVRKLKKQL 1455
Cdd:pfam05483 693 EIDKRCQHKIAEMValmekHKHQYdkiIEErdselgLYKNKEQEQSSAKAALEIELSNIKAELlslKKQLEIEKEEKEKL 772
|
....*.
gi 2015234411 1456 KVFAKK 1461
Cdd:pfam05483 773 KMEAKE 778
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
902-1209 |
3.30e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.94 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 902 KRELKKLKIEARS-VERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLE----------GTYNSETEKLRSDLER 970
Cdd:TIGR02169 697 LRRIENRLDELSQeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEqeienvkselKELEARIEELEEDLHK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 971 LQLSEE--EAKIATGRVLSLQEEIAKLRK----------DLEQTRSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEK 1038
Cdd:TIGR02169 777 LEEALNdlEARLSHSRIPEIQAELSKLEEevsriearlrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1039 EALNHRiveqaKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEmtlmVNVPKPGHKRTDSTHS 1118
Cdd:TIGR02169 857 ENLNGK-----KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ----IEKKRKRLSELKAKLE 927
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1119 sneseyTFSSEIAETEDIPSRTEEPSEKKVPLDmslflKLQKRVTELEQEKQVMQ-------DELDRKEEQVLRSKAK-- 1189
Cdd:TIGR02169 928 ------ALEEELSEIEDPKGEDEEIPEEELSLE-----DVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKra 996
|
330 340
....*....|....*....|..
gi 2015234411 1190 --EEERPQIRGAELEYESLKRQ 1209
Cdd:TIGR02169 997 klEEERKAILERIEEYEKKKRE 1018
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
900-1232 |
3.73e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 65.38 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 900 MAKRELKKLKIEARSVERYKKLHIGMEN-KIMQLQRKVDEQNKDYKCLMEKLTNLEGTYNSETEKLRSDLERLQLSEEEA 978
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEELKKLKLEAEElLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 979 KiatgrvlSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQLVSN--LKEENTLLKQEKEALNHRIVEQAKEMTETM 1056
Cdd:pfam02463 774 K-------ELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAelLEEEQLLIEQEEKIKEEELEELALELKEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1057 EKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmvnvpKPGHKRTDSTHSSNESEYTFSSEIAETEDI 1136
Cdd:pfam02463 847 KLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELES------KEEKEKEEKKELEEESQKLNLLEEKENEIE 920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1137 PSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQvlrsKAKEEERPQIRGAELEYESLK--RQELESE 1214
Cdd:pfam02463 921 ERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLL----LAKEELGKVNLMAIEEFEEKEerYNKDELE 996
|
330
....*....|....*...
gi 2015234411 1215 NKKLKNELNELRKALSEK 1232
Cdd:pfam02463 997 KERLEEEKKKLIRAIIEE 1014
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
956-1374 |
9.15e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.91 E-value: 9.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 956 TYNSETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTRSEKksiEEHADRYKQETEQLvSNLKEENT--L 1033
Cdd:PRK02224 224 RYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERER---EELAEEVRDLRERL-EELEEERDdlL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1034 LKQEKEALNHRIVEQAKemtETMEKKLVEetkqLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmvnvpkpgHKRT 1113
Cdd:PRK02224 300 AEAGLDDADAEAVEARR---EELEDRDEE----LRDRLEECRVAAQAHNEEAESLREDADDLEERAE---------ELRE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1114 DSThssneseyTFSSEIAET-EDIPSRTEEPSEkkvpldmslflkLQKRVTELEQEKQVMQDELDRKEEqvlRSKAKEEE 1192
Cdd:PRK02224 364 EAA--------ELESELEEArEAVEDRREEIEE------------LEEEIEELRERFGDAPVDLGNAED---FLEELREE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1193 RPQIRGaeleyeslKRQELESENKKLKNELNELRKALSEKSSPEVTAPGAPAYRVlmeqltSVSEELDVRKEEVLILRSQ 1272
Cdd:PRK02224 421 RDELRE--------REAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHV------ETIEEDRERVEELEAELED 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1273 LVSQKEAIQPKNTMTDSTILLED-VQKMKDKGEIAQAYIGLKETnrssamdchELNEDGELLlvyEGLKQANRLLESQLQ 1351
Cdd:PRK02224 487 LEEEVEEVEERLERAEDLVEAEDrIERLEERREDLEELIAERRE---------TIEEKRERA---EELRERAAELEAEAE 554
|
410 420
....*....|....*....|....*.
gi 2015234411 1352 SQK---RSHENEAEALRGEIQSLKEE 1374
Cdd:PRK02224 555 EKReaaAEAEEEAEEAREEVAELNSK 580
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
902-1518 |
1.54e-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: 63.45 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 902 KRELKKLKIEARSVERYKKLHigMENKIMQLQRKVDEQNKDYKclmEKLTNLEGTYNSETEKLRSDLERLQLSEEEAKia 981
Cdd:pfam02463 196 KLQELKLKEQAKKALEYYQLK--EKLELEEEYLLYLDYLKLNE---ERIDLLQELLRDEQEEIESSKQEIEKEEEKLA-- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 982 tgRVLSLQEEIAKLRKDLEQTRSEKKSIEE-------HADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVEQAKEMTE 1054
Cdd:pfam02463 269 --QVLKENKEEEKEKKLQEEELKLLAKEEEelksellKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1055 TMEKKLVEETK--QLELDLNDERLRYQNLLNEFSRLEERY---DDLKEEMTLMVNVPKpgHKRTDSTHSSNESEYTFSSE 1129
Cdd:pfam02463 347 LEIKREAEEEEeeELEKLQEKLEQLEEELLAKKKLESERLssaAKLKEEELELKSEEE--KEAQLLLELARQLEDLLKEE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1130 IAETEDIPSRTEEPSEKKVPLDMSLFLKLQK-RVTELEQEKQVMQDELDRKEEQVLRSKAKEEERpqIRGAELEYESLKR 1208
Cdd:pfam02463 425 KKEELEILEEEEESIELKQGKLTEEKEELEKqELKLLKDELELKKSEDLLKETQLVKLQEQLELL--LSRQKLEERSQKE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1209 QELESENKKLKNELNELRKALSEKSSPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKNTMTD 1288
Cdd:pfam02463 503 SKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRL 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1289 STILLEDVQKMKDKGEIAQAYIGLKETNRSSAMDCHE----LNEDGELLLVYEGLKQANRLLESQLQSQKRSHENEAEAL 1364
Cdd:pfam02463 583 LIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDkrakVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKS 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1365 RGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNENLYFEEL-YADDPKKYQSYRISLYKRMIDLMEQLEK 1443
Cdd:pfam02463 663 EVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKkLKLEAEELLADRVQEAQDKINEELKLLK 742
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2015234411 1444 QDKTVR---KLKKQLKVFAKKIGELEVGQMENVSPGQIIDEPIRPVNIpRKEKDFQGMLEYKKEDEQKLVKNLILELK 1518
Cdd:pfam02463 743 QKIDEEeeeEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEE-EKEEKLKAQEEELRALEEELKEEAELLEE 819
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
917-1466 |
1.81e-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: 62.73 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 917 RYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGTYNSETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLR 996
Cdd:TIGR04523 23 GYKNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 997 KDLEQTRSEKKSieehadrykqeTEQLVSNLKEENTLLKQEKEALNHRIveqakemtetmeKKLVEETKQLELDLNDERL 1076
Cdd:TIGR04523 103 SDLSKINSEIKN-----------DKEQKNKLEVELNKLEKQKKENKKNI------------DKFLTEIKKKEKELEKLNN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1077 RYQNLLNEFSRLEERYDDLKEEMTlmvnvpKPGHKRTDSTHSSNESEYTFSSEIAETEDIPSRTEEPSEKKvpldmSLFL 1156
Cdd:TIGR04523 160 KYNDLKKQKEELENELNLLEKEKL------NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELK-----KQNN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1157 KLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEE---RPQIRGAELEYESLKRQELESENKKLKNELNELRKalsEKS 1233
Cdd:TIGR04523 229 QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKikkQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN---QKE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1234 SpevtapgapayrvlmEQLTSVSEELDVRKEEVLILRSQLVSQKEAI--------QPKNTMTDSTilLEDVQKMKDKGEI 1305
Cdd:TIGR04523 306 Q---------------DWNKELKSELKNQEKKLEEIQNQISQNNKIIsqlneqisQLKKELTNSE--SENSEKQRELEEK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1306 AQAYIGLKETNRSSAMDCHEL-NEDGELLLVYEGLKQANRLLESQLQSQkrshENEAEALRGEIQSLKEENNrqqqllaq 1384
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLeSQINDLESKIQNQEKLNQQKDEQIKKL----QQEKELLEKEIERLKETII-------- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1385 nlqlppearieaSLQHEITRLTNENLYFEELYA--DDPKKYQSYRISLYKRMIDLMEQ-LEKQDKTVRKLKKQLKVFAKK 1461
Cdd:TIGR04523 437 ------------KNNSEIKDLTNQDSVKELIIKnlDNTRESLETQLKVLSRSINKIKQnLEQKQKELKSKEKELKKLNEE 504
|
....*
gi 2015234411 1462 IGELE 1466
Cdd:TIGR04523 505 KKELE 509
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
901-1508 |
2.03e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 901 AKRELKKLKIEA-RSVERYKKlhIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGTYNSEtEKLRSDleRLQLSEEEAK 979
Cdd:PTZ00121 1217 ARKAEDAKKAEAvKKAEEAKK--DAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE-EARKAD--ELKKAEEKKK 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 980 IATGRVLSLQEEIAKLRKDLEQTRS--EKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIvEQAKEMTETME 1057
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAEEAKKadEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEA-EAAEEKAEAAE 1370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1058 KKLVEETKQLEL--DLNDERLRYQNLLNEFSRLEERYDDLK---EEMTLMVNVPKPGHKRTDSTHSSNESEYTFSSEIAE 1132
Cdd:PTZ00121 1371 KKKEEAKKKADAakKKAEEKKKADEAKKKAEEDKKKADELKkaaAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK 1450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1133 TEDIPSRTEEPSEKKVpldmslflKLQKRVTELEQ--EKQVMQDELDRKEEQVLR----SKAKEEERPQIRGAELEYESL 1206
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKA--------EEAKKADEAKKkaEEAKKADEAKKKAEEAKKkadeAKKAAEAKKKADEAKKAEEAK 1522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1207 KRQELESENKKLKNElnELRKALSEKSSPEVTApgapayrvlmeqltsvSEEldVRKEEvlilrsqlvSQKEAIQPKNTM 1286
Cdd:PTZ00121 1523 KADEAKKAEEAKKAD--EAKKAEEKKKADELKK----------------AEE--LKKAE---------EKKKAEEAKKAE 1573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1287 TDSTILLEDVQKMKdKGEIAQAYIGLKETNRSSAMDCHELNEDGELLLVYEGLKQANRLLESQLQSQKRSHENEAEAlrG 1366
Cdd:PTZ00121 1574 EDKNMALRKAEEAK-KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA--E 1650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1367 EIQSLKEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNENLYFEELYADDPKKYQSYRISLYKRMIDLMEQLEKQDK 1446
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKI 1730
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2015234411 1447 TVRKLKKQLKVFAKKIGELEVGQMENVSPGQIIDEPIRPVNIPRKEKDFQGMLEYKKEDEQK 1508
Cdd:PTZ00121 1731 KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKR 1792
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
904-1320 |
5.11e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.70 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 904 ELKKLKIEARSVERYKKlHIGMENKIMQLQRKVDEQNK--DYKCLMEKLTNLEGTYNSETEKLRSDleRLQLSEEEAKIA 981
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKK-KAEEKKKADEAKKKAEEAKKadEAKKKAEEAKKAEEAKKKAEEAKKAD--EAKKKAEEAKKA 1485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 982 TgRVLSLQEEIAKLRKDLEQTRSEKKSIEE--HADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVEQAKEMTETMEKK 1059
Cdd:PTZ00121 1486 D-EAKKKAEEAKKKADEAKKAAEAKKKADEakKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK 1564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1060 LVEETKQLELDLNDERLRYQNLLN-EFSRLEERYDDLKEEmtlmvnvpkpghKRTDSTHSSNESEYTFSSEiaetediPS 1138
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEE------------KKMKAEEAKKAEEAKIKAE-------EL 1625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1139 RTEEPSEKKVPLDMSLFLKLQKRVTEL---EQEKQVMQDELDRKEEQVLRS-----KAKEEERPQIRGAELEYESLKRQE 1210
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELkkaEEENKIKAAEEAKKAEEDKKKaeeakKAEEDEKKAAEALKKEAEEAKKAE 1705
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1211 lesENKKLKNElnELRKALSEKSSPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILrSQLVSQKEAIQPKNTMTDST 1290
Cdd:PTZ00121 1706 ---ELKKKEAE--EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI-AHLKKEEEKKAEEIRKEKEA 1779
|
410 420 430
....*....|....*....|....*....|
gi 2015234411 1291 ILLEDVQKmKDKGEIAQAYIGLKETNRSSA 1320
Cdd:PTZ00121 1780 VIEEELDE-EDEKRRMEVDKKIKDIFDNFA 1808
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
902-1466 |
7.04e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.80 E-value: 7.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 902 KRELKKLKIEARSVeryKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEgtynseteklrsdLERLQLSEEEAKIa 981
Cdd:TIGR04523 123 EVELNKLEKQKKEN---KKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELE-------------NELNLLEKEKLNI- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 982 tgrvlslQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQLvSNLKEENTLLKQEKEALNHRIVEQAKEMTETMEK--K 1059
Cdd:TIGR04523 186 -------QKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQI-SELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQlnQ 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1060 LVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVNVPKPG-HKRTDSTHSSNESEYT-FSSEIAETEDIP 1137
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDwNKELKSELKNQEKKLEeIQNQISQNNKII 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1138 SRTEEPSEKkvpldmslflkLQKRVTELEQEKQVMQDELDRKEEQVlrskakeeerpqirgaeleyESLKR--QELESEN 1215
Cdd:TIGR04523 338 SQLNEQISQ-----------LKKELTNSESENSEKQRELEEKQNEI--------------------EKLKKenQSYKQEI 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1216 KKLKNELNELRKALSEKSSPEvtapgapayRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQP-KNTMTDSTILLE 1294
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLN---------QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDlTNQDSVKELIIK 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1295 DVQKMKD---------KGEIAQAYIGLKETNRSSAMDCHEL----NEDGELLLVYEGLKQANRLLES---QLQSQKRSHE 1358
Cdd:TIGR04523 458 NLDNTREsletqlkvlSRSINKIKQNLEQKQKELKSKEKELkklnEEKKELEEKVKDLTKKISSLKEkieKLESEKKEKE 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1359 NEAEALRGEIQSLKEENNRQQQLLAQNLQlppEARIEaSLQHEITRLTNENLYFEELYaddpKKYQsyrislyKRMIDLM 1438
Cdd:TIGR04523 538 SKISDLEDELNKDDFELKKENLEKEIDEK---NKEIE-ELKQTQKSLKKKQEEKQELI----DQKE-------KEKKDLI 602
|
570 580
....*....|....*....|....*...
gi 2015234411 1439 EQLEKQDKTVRKLKKQLKVFAKKIGELE 1466
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAKKENEKLS 630
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
911-1372 |
1.04e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 60.52 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 911 EARSVERYKKLHIGMENKIMQLQRKvdEQNKDYkclMEKLTNLEGTynseTEKLRSDLErlqlseEEAKIATGRVLSLQE 990
Cdd:pfam15921 285 EKASSARSQANSIQSQLEIIQEQAR--NQNSMY---MRQLSDLEST----VSQLRSELR------EAKRMYEDKIEELEK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 991 EIAKLRKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEAlNHRIVEQAKEMTETMEkklveetkQLELD 1070
Cdd:pfam15921 350 QLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQ-NKRLWDRDTGNSITID--------HLRRE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1071 LNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVNVPKPGHKRTDSTHSSNESEYTFSSEIAETEDIPSRTEEPSEKKVPl 1150
Cdd:pfam15921 421 LDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS- 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1151 DMSLFLKLQKRVTE-LEQEKQVMQDELDRKEEQVLRSKAKEEerpQIRGAELEYESLKRQELEsenkklKNELNELRKAL 1229
Cdd:pfam15921 500 DLTASLQEKERAIEaTNAEITKLRSRVDLKLQELQHLKNEGD---HLRNVQTECEALKLQMAE------KDKVIEILRQQ 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1230 SEKSSPEVTAPGAPAYRVLMEQlTSVSEELDVRK---EEVLILRSQLVSQKEAIQPKNtmtdSTILLEDV-------QKM 1299
Cdd:pfam15921 571 IENMTQLVGQHGRTAGAMQVEK-AQLEKEINDRRlelQEFKILKDKKDAKIRELEARV----SDLELEKVklvnagsERL 645
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2015234411 1300 KDKGEIAQAYIGLKETNRSSAMDCHELNEDGELLLV-YEGLKQANRLLESQLQSQKRSHENEAEALRGEIQSLK 1372
Cdd:pfam15921 646 RAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRnFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSME 719
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
904-1510 |
1.17e-08 |
|
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: 60.12 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 904 ELKKLKIEARSVERYKKLHIGMENKIMQLQR---------------KVDEQNKDYKCLMEKLTNLEGTYNSETEKLRSDL 968
Cdd:pfam05483 89 KIKKWKVSIEAELKQKENKLQENRKIIEAQRkaiqelqfenekvslKLEEEIQENKDLIKENNATRHLCNLLKETCARSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 969 ERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTR--SEKKSIEEHAdRYKQETEQlVSNLKEENTLLKQEKEALNHRIV 1046
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRvqAENARLEMHF-KLKEDHEK-IQHLEEEYKKEINDKEKQVSLLL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1047 EQAKEMTETMEKK--LVEETKQLELDLNDE-RLRYQNLlnefSRLEERYDDLKEEMTLMvnvpKPGHKRTDSTHSSNESE 1123
Cdd:pfam05483 247 IQITEKENKMKDLtfLLEESRDKANQLEEKtKLQDENL----KELIEKKDHLTKELEDI----KMSLQRSMSTQKALEED 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1124 YTFSSEI--AETEDIPSRTEEPSEKKVPLDMSlflklqkrVTELEQEKQVMQdELDRKEEQVLRskaKEEERPQIRGAEL 1201
Cdd:pfam05483 319 LQIATKTicQLTEEKEAQMEELNKAKAAHSFV--------VTEFEATTCSLE-ELLRTEQQRLE---KNEDQLKIITMEL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1202 EYESLKRQELESENKKLKNELNELRKALSEKSspevtapgapayRVLME--QLTSVSEELDVRKEEVLIL---RSQLVSQ 1276
Cdd:pfam05483 387 QKKSSELEEMTKFKNNKEVELEELKKILAEDE------------KLLDEkkQFEKIAEELKGKEQELIFLlqaREKEIHD 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1277 KEaIQPKNTMTDSTILLEDVQKMKDKGEIAQayigLKETNRSSAMDchelnedgELLLVYEGLKQANRLLESQLQSQKRS 1356
Cdd:pfam05483 455 LE-IQLTAIKTSEEHYLKEVEDLKTELEKEK----LKNIELTAHCD--------KLLLENKELTQEASDMTLELKKHQED 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1357 HEN---EAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNENLYFEELYADDPKKYQSYRISLYKR 1433
Cdd:pfam05483 522 IINckkQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKK 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1434 MID----LMEQLEKQDKTVRKL----KKQLKVFAKKIGELEvgqMENVSPGQIIDEPIrpvniprkeKDFQGMLEYKKED 1505
Cdd:pfam05483 602 QIEnknkNIEELHQENKALKKKgsaeNKQLNAYEIKVNKLE---LELASAKQKFEEII---------DNYQKEIEDKKIS 669
|
....*
gi 2015234411 1506 EQKLV 1510
Cdd:pfam05483 670 EEKLL 674
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
957-1370 |
1.33e-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: 60.08 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 957 YNSETEKLRSDLERLQLSEEEAKIAtgrvlslqeeIAKLRKDLEQTRSEKksieEHADRYKQeteqLVSNLKE-ENTLLK 1035
Cdd:TIGR02169 168 FDRKKEKALEELEEVEENIERLDLI----------IDEKRQQLERLRRER----EKAERYQA----LLKEKREyEGYELL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1036 QEKEALNHRIVEQAKEMTEtmekkLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVNvpkpghKRTDS 1115
Cdd:TIGR02169 230 KEKEALERQKEAIERQLAS-----LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK------EKIGE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1116 THSsneseytfssEIAETEDIPSRTEEPSEKkvpldmslfLKLQKRVTELEQEKQVMQ-DELDRKEEQVLRSKAKEEERP 1194
Cdd:TIGR02169 299 LEA----------EIASLERSIAEKERELED---------AEERLAKLEAEIDKLLAEiEELEREIEEERKRRDKLTEEY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1195 QIRGAELEYESLKRQELESENKKLKNELNELRKALSEksspevtapgapayrvLMEQLTSVSEELDVRKEEVLILRSQLV 1274
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK----------------LKREINELKRELDRLQEELQRLSEELA 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1275 SQKEAIqpkntmtdsTILLEDVQKMKDKGEIAQAYIGLKETNRSSAMDCHELNEDGelllvYEGLKQANRLLESQLqSQK 1354
Cdd:TIGR02169 424 DLNAAI---------AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE-----LYDLKEEYDRVEKEL-SKL 488
|
410
....*....|....*.
gi 2015234411 1355 RSHENEAEALRGEIQS 1370
Cdd:TIGR02169 489 QRELAEAEAQARASEE 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
928-1259 |
1.62e-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: 60.08 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 928 KIMQLQRKVDEQNKDYKCLMEKLTNLEGTYNSETEKLrSDLERlQLSEEEAKIAtgrvlSLQEEIAKLRKDLEQTRSEKK 1007
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL-SDASR-KIGEIEKEIE-----QLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1008 SIEEHADRYKQETEQLVSNLKEENTLLKQEKEALN--------HRIVEQAKEMTETME--KKLVEETKQLELDLNDERLR 1077
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNdlearlshSRIPEIQAELSKLEEevSRIEARLREIEQKLNRLTLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1078 YQNLLNEFSRLEERYDDLKEEMtlmvnvpkpghkrtdsthssNESEYTFSSEIAETEDIPSRTEEpsekkvpldmslflk 1157
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQI--------------------KSIEKEIENLNGKKEELEEELEE--------------- 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1158 LQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEErpqirgAELEYEsLKRQELESENKKLKNELNELRKALSEKSSPEV 1237
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEE------LEAQIE-KKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
330 340
....*....|....*....|..
gi 2015234411 1238 TAPGAPAYRVLMEQLTSVSEEL 1259
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRVEEEI 967
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
900-1281 |
1.93e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 900 MAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLE-----GTYNSETEKLRSDLERLQLS 974
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllqlLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 975 EEEAKIATGRVLSLQEEIAKLRKDLEQTRSEkksIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIvEQAKEMTE 1054
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEE---LEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL-EEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1055 TMEKKLVEETKQLELDLNDERLRYQN-----------LLNEFSRLEERYDDLKEEMTLMVNVPKPGHKRTDSTHSSNESE 1123
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1124 YTFSSEIAETEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERP--QIRGAEL 1201
Cdd:COG4717 304 AEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1202 EYESLKRQELESENKKLKNELNELRKALSEKSSPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQ 1281
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELE 463
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
901-1098 |
4.11e-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: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 901 AKRELKKL-KIEARSVERYKKLhigmENKIMQLQRKVDEQNKDYKCLMEKLTNLEGTYnsetEKLRSDLERLqlsEEEAK 979
Cdd:TIGR02169 313 KERELEDAeERLAKLEAEIDKL----LAEIEELEREIEEERKRRDKLTEEYAELKEEL----EDLRAELEEV---DKEFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 980 IATGRVLSLQEEiaklrkdLEQTRSEKKSIEEHADRYKQETEQLVSNLKEentlLKQEKEALNHRIVEQAKEMTETME-- 1057
Cdd:TIGR02169 382 ETRDELKDYREK-------LEKLKREINELKRELDRLQEELQRLSEELAD----LNAAIAGIEAKINELEEEKEDKALei 450
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2015234411 1058 KKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEE 1098
Cdd:TIGR02169 451 KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
896-1258 |
4.82e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 58.21 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 896 FRRMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEgtyNSETEKLRSDLERLQLSE 975
Cdd:pfam17380 293 FEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELE---RIRQEERKRELERIRQEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 976 EEAKIATGRVL-----SLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHrivEQAK 1050
Cdd:pfam17380 370 IAMEISRMRELerlqmERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE---ERAR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1051 EMTETMEKKLvEETKQLELDLNDERLRYQNLLnEFSRlEERYDDLKEEMTLMVnVPKPGHKRTDSTHSSNESEYTFSSEI 1130
Cdd:pfam17380 447 EMERVRLEEQ-ERQQQVERLRQQEEERKRKKL-ELEK-EKRDRKRAEEQRRKI-LEKELEERKQAMIEEERKRKLLEKEM 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1131 AETEDipsrteepsekkvpldmSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKakeEERPQIRGAELEYEsLKRQE 1210
Cdd:pfam17380 523 EERQK-----------------AIYEEERRREAEEERRKQQEMEERRRIQEQMRKAT---EERSRLEAMERERE-MMRQI 581
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2015234411 1211 LESENKKLKNELNELRKALSEKSSPEVTAPGAPAYRVLMEQLTSVSEE 1258
Cdd:pfam17380 582 VESEKARAEYEATTPITTIKPIYRPRISEYQPPDVESHMIRFTTQSPE 629
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
901-1456 |
6.01e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 6.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 901 AKRELKKLKIEARSVErykKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGTYNSETEKLRSDLERLQLSEEEAKi 980
Cdd:COG1196 251 LEAELEELEAELAELE---AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 981 atgrvlSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVEQAKEMTETMEKKl 1060
Cdd:COG1196 327 ------ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA- 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1061 vEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEmtlmvnvpkpghkrTDSTHSSNESEYTFSSEIAETEDIPSRT 1140
Cdd:COG1196 400 -AQLEELEEAEEALLERLERLEEELEELEEALAELEEE--------------EEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1141 EEPSEKKVPLDMSLFLKLQKRVTELEQEKQV---MQDELDRKEEQVLRSKAKEEERP------QIRGAELEYESLKRQEL 1211
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLlleAEADYEGFLEGVKAALLLAGLRGlagavaVLIGVEAAYEAALEAAL 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1212 ES--ENKKLKNELNELRKALSEKSSPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQP------K 1283
Cdd:COG1196 545 AAalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVlgdtllG 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1284 NTMTDSTILLEDVQKMKDKGEIAQAYIGLKETNRSSAMDCHELNEDGELLLvyegLKQANRLLESQLQSQKRSHENEAEA 1363
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL----EAEAELEELAERLAEEELELEEALL 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1364 LRGEIQSLKEENNRQQQLLAQNlqlppEARIEASLQHEITRLTNENLYFEELYADDPKKYqsyrislykrmIDLMEQLEK 1443
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELE-----EEALEEQLEAEREELLEELLEEEELLEEEALEE-----------LPEPPDLEE 764
|
570
....*....|...
gi 2015234411 1444 QDKTVRKLKKQLK 1456
Cdd:COG1196 765 LERELERLEREIE 777
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
963-1304 |
7.49e-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: 57.77 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 963 KLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTRSE-KKSIEEhadrYKQETEQLVSNLKEENTLLKQEKEAL 1041
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDaSRKIGE----IEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1042 nhRIVEQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLlnEFSRLEERYDDLKEEMtlmvnvpkpghKRTDSTHSSNE 1121
Cdd:TIGR02169 747 --SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EARLSHSRIPEIQAEL-----------SKLEEEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1122 seytfsseiAETEDIPSRTEEPSEKKVPLDmSLFLKLQKRVTELEQEKQVMQDELdrkEEQVLRSKAKEEERPQIRGAEL 1201
Cdd:TIGR02169 812 ---------ARLREIEQKLNRLTLEKEYLE-KEIQELQEQRIDLKEQIKSIEKEI---ENLNGKKEELEEELEELEAALR 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1202 EYESlKRQELESENKKLKNELNELRKALSEKSSPEVTApgapayRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQ 1281
Cdd:TIGR02169 879 DLES-RLGDLKKERDELEAQLRELERKIEELEAQIEKK------RKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
|
330 340
....*....|....*....|...
gi 2015234411 1282 PkntmtdstilLEDVQKMKDKGE 1304
Cdd:TIGR02169 952 S----------LEDVQAELQRVE 964
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
929-1291 |
1.03e-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: 57.06 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 929 IMQLQRKVDEQNKDYKclMEKLtnlegtynsETEKLRsdlerlQLSEEEAKiatgrvlslqeEIAKLRKDLEQTRSEKKS 1008
Cdd:pfam17380 277 IVQHQKAVSERQQQEK--FEKM---------EQERLR------QEKEEKAR-----------EVERRRKLEEAEKARQAE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1009 IEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVEQakEMTETMEKKLVEETKQLELDLNDERLRyQNLlnEFSRL 1088
Cdd:pfam17380 329 MDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQE--EIAMEISRMRELERLQMERQQKNERVR-QEL--EAARK 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1089 -----EERYDDLKEEMTLMVNVPKpghkrtdsthssneseytfSSEIAETEDIpSRTEEPSEKKVpldmslflklqKRVT 1163
Cdd:pfam17380 404 vkileEERQRKIQQQKVEMEQIRA-------------------EQEEARQREV-RRLEEERAREM-----------ERVR 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1164 ELEQEKQ-----VMQDELDRKEEQVLRSKAK------EEERPQIrgAELEYESLKRQELESENKK--LKNELNELRKALS 1230
Cdd:pfam17380 453 LEEQERQqqverLRQQEEERKRKKLELEKEKrdrkraEEQRRKI--LEKELEERKQAMIEEERKRklLEKEMEERQKAIY 530
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1231 EKSSPEV------TAPGAPAYRVLMEQLTSVSEE---LDVRKEEVLILRSQLVSQKEAIQPKNTMTDSTI 1291
Cdd:pfam17380 531 EEERRREaeeerrKQQEMEERRRIQEQMRKATEErsrLEAMEREREMMRQIVESEKARAEYEATTPITTI 600
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
925-1416 |
1.25e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 925 MENKIMQLQRKVDEQNKDYKCLMEKLTNLEGTYNSETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTRS 1004
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1005 EKKSIEEHADRYKQETEQlvsnLKEENTLLKQEKEALNHRIvEQAKEMTETMEKKLVEetkqLELDLNDERLRYQNLLNE 1084
Cdd:PRK02224 336 AAQAHNEEAESLREDADD----LEERAEELREEAAELESEL-EEAREAVEDRREEIEE----LEEEIEELRERFGDAPVD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1085 FSRLEERYDDLKEEmtlmvnvpkpghkRTDSTHSSNESEYTFSSE---IAETED------------------IPSRTEEP 1143
Cdd:PRK02224 407 LGNAEDFLEELREE-------------RDELREREAELEATLRTArerVEEAEAlleagkcpecgqpvegspHVETIEED 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1144 SEKKVPLDMSL------FLKLQKRVTELEQEKQVmQDELDRKEEQVLRSkakeEERPQIRGAELEYESLKRQELESENKK 1217
Cdd:PRK02224 474 RERVEELEAELedleeeVEEVEERLERAEDLVEA-EDRIERLEERREDL----EELIAERRETIEEKRERAEELRERAAE 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1218 LKNELNELRKALSEKsspevtapgapayrvlmeqltsvSEELDVRKEEVLILRSQLVSQKEAIQPKNTMTDSTILLEDVQ 1297
Cdd:PRK02224 549 LEAEAEEKREAAAEA-----------------------EEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAE 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1298 kmKDKGEIAQAYIGLKETNRSSAMDCHELNEDGELLlvyEGLKQANRLleSQLQSQKRSHENEAEALRGEIQSLKEENNR 1377
Cdd:PRK02224 606 --DEIERLREKREALAELNDERRERLAEKRERKREL---EAEFDEARI--EEAREDKERAEEYLEQVEEKLDELREERDD 678
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2015234411 1378 QQQLLAQNlqlppEARIE--ASLQHEITRLTNENLYFEELY 1416
Cdd:PRK02224 679 LQAEIGAV-----ENELEelEELRERREALENRVEALEALY 714
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
881-1066 |
1.31e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 56.32 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 881 YYRRSIHAIIYLQCcfrRMMAKRELKKLKIEARSVERYKKLHIgmENKIMQLQRKVDEQNKDYKclmEKLTNLEGTYNSE 960
Cdd:PRK12704 23 FVRKKIAEAKIKEA---EEEAKRILEEAKKEAEAIKKEALLEA--KEEIHKLRNEFEKELRERR---NELQKLEKRLLQK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 961 TEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQE--TEQLVSNLKEEntlLKQEK 1038
Cdd:PRK12704 95 EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEeaKEILLEKVEEE---ARHEA 171
|
170 180
....*....|....*....|....*...
gi 2015234411 1039 EALNHRIVEQAKEMTETMEKKLVEETKQ 1066
Cdd:PRK12704 172 AVLIKEIEEEAKEEADKKAKEILAQAIQ 199
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
896-1464 |
1.80e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 56.29 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 896 FRRMMAKRELKKLKIEarsverYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGTYNSETEKLRSDLERLQL-- 973
Cdd:pfam05557 9 ARLSQLQNEKKQMELE------HKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 974 ----------SEEEAKIATGR--VLSLQEEIAKLRK-------DLEQTRSEKKSIEEHADRYK---QETEQLVSNLKEEN 1031
Cdd:pfam05557 83 kylealnkklNEKESQLADARevISCLKNELSELRRqiqraelELQSTNSELEELQERLDLLKakaSEAEQLRQNLEKQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1032 TLLK---QEKEALNHRIVEQA--KEMTETMEKKLVEETkqlELDLNDERLRYQN-LLNEFSR----LEERYDDLKEEMtl 1101
Cdd:pfam05557 163 SSLAeaeQRIKELEFEIQSQEqdSEIVKNSKSELARIP---ELEKELERLREHNkHLNENIEnkllLKEEVEDLKRKL-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1102 mvnvpkpghkrtdsthssnESEYTFSSEIAETEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEE 1181
Cdd:pfam05557 238 -------------------EREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1182 Q-VLRSKAKEEERpqirgaeleyeslKRQELESENKKLKNELNELRKALSEKSSpevtapgapAYRVLMEQLTSVSEELD 1260
Cdd:pfam05557 299 NsSLTSSARQLEK-------------ARRELEQELAQYLKKIEDLNKKLKRHKA---------LVRRLQRRVLLLTKERD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1261 VRKEEVLILRSQLVSQKEAIQPKNTMTDSTILLEDVQKMKDKGEI--AQAYIGLKETNRSSAMDCHEL---------NED 1329
Cdd:pfam05557 357 GYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAqlSVAEEELGGYKQQAQTLERELqalrqqeslADP 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1330 GELLLVYEGLKQANRLLESQLQSQKRshENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEAS------LQHEIT 1403
Cdd:pfam05557 437 SYSKEEVDSLRRKLETLELERQRLRE--QKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRknqlekLQAEIE 514
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2015234411 1404 RLTNENLYFEELYADDPKKYQSYRISLYKRMIDLMEQLEKQDKTVRKLKkqlKVFAKKIGE 1464
Cdd:pfam05557 515 RLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQRLK---EVFQAKIQE 572
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
959-1232 |
4.48e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 54.87 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 959 SETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTRSEKKSIEEHADR------------YKQETEQLVSN 1026
Cdd:pfam02029 50 LKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENneeeensswekeEKRDSRLGRYK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1027 LKEENTLLKQEKEALNHRIVEQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEfsrLEERYDDLK---------- 1096
Cdd:pfam02029 130 EEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKE---KKVKYESKVfldqkrghpe 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1097 ---EEMTLMVNVPKPGHKRTDSTHSSNESEYTFSSEIAETEdipSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEkqvmQ 1173
Cdd:pfam02029 207 vksQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAE---QKLEELRRRRQEKESEEFEKLRQKQQEAELE----L 279
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2015234411 1174 DELDRKEEQvlRSKAKEEERPQiRGAEleyESLKRQELESENKKLKNELNELRKALSEK 1232
Cdd:pfam02029 280 EELKKKREE--RRKLLEEEEQR-RKQE---EAERKLREEEEKRRMKEEIERRRAEAAEK 332
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
813-835 |
5.14e-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: 5.14e-07
|
| Myo5p-like_CBD_Rasip1 |
cd15472 |
cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 ... |
1531-1810 |
5.84e-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: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1531 PAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVL----KKRGD---------------------DFETVSFWLSNTCR 1585
Cdd:cd15472 25 PAFLLCLCIQHSATHFEPGHFGKLLLKIAKRIQEIVwektKELAEkqpehqdpaslsllsiaelapDLQPLLFWMSNSIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1586 FLHCLKQ----YSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmIVSGMLE-----HET 1656
Cdd:cd15472 105 LLYFIQQkvplYEQSMEEELDVGSKESLLSSTLTASEEAMTVLEEVIMYTFQQCVYYLTKTLYV-ALPALLDsnpftAEE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1657 IQGVSG--VKPTGLRkRTSSIADEgtyTLDsILRQLnsfhsvmCQHgmdPELIKQVVKQMFYIVGAVTLNNLLLRKDMCS 1734
Cdd:cd15472 184 RESWSGgsRLPEGVR-RVLEIYQA---TLD-LLRQY-------QVH---PEIASQMFAYLFFFSNASLFNQLMEKGSGGG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1735 ---WSKGMQIRYNVSQLEEWLRDKNLmNSGAKETLEPLIQAAQLLQVKKKTDDDAE--AICSMCNALTTAQIVKVLNLYT 1809
Cdd:cd15472 249 ffqWSRGVQIRANLDLLLDWLQGAGL-GDLAEEFFRKLSSTVNLLATPKEQLLQMSwsSLRAEFPALNPAQLHHLLRQYQ 327
|
.
gi 2015234411 1810 P 1810
Cdd:cd15472 328 L 328
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
902-1227 |
9.62e-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: 53.87 E-value: 9.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 902 KRELKKLKIEARSverYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEgtynSETEKLrsdlerlqlsEEEAKIA 981
Cdd:TIGR04523 369 QNEIEKLKKENQS---YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ----QEKELL----------EKEIERL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 982 TGRVLSLQEEIaklrKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVEQAKEMtetmeKKLV 1061
Cdd:TIGR04523 432 KETIIKNNSEI----KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL-----KKLN 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1062 EETKQLE---LDLNDE----RLRYQNLLNEFSRLEERYDDLKEEMtlmvnvpkpghkrtdsthssNESEYTFSSEIAETE 1134
Cdd:TIGR04523 503 EEKKELEekvKDLTKKisslKEKIEKLESEKKEKESKISDLEDEL--------------------NKDDFELKKENLEKE 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1135 dIPSRTEEPSEKKvpLDMSLFLKLQKRVTELEQEKQVMQDELdrKEEQVLRSKAKEEERPQIRGAELEYEslkrqELESE 1214
Cdd:TIGR04523 563 -IDEKNKEIEELK--QTQKSLKKKQEEKQELIDQKEKEKKDL--IKEIEEKEKKISSLEKELEKAKKENE-----KLSSI 632
|
330
....*....|...
gi 2015234411 1215 NKKLKNELNELRK 1227
Cdd:TIGR04523 633 IKNIKSKKNKLKQ 645
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
898-1363 |
1.50e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.43 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 898 RMMAKRELKKLKIEAR-----SVERYKKLHIGMENKIMQLQRKVDEQNK---DYKCLMEKLTNLEGTYNSETEKLRSDLE 969
Cdd:TIGR00618 415 RTSAFRDLQGQLAHAKkqqelQQRYAELCAAAITCTAQCEKLEKIHLQEsaqSLKEREQQLQTKEQIHLQETRKKAVVLA 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 970 RLQLSEEEAKIATG--------------------RVLSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETE-------- 1021
Cdd:TIGR00618 495 RLLELQEEPCPLCGscihpnparqdidnpgpltrRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQeiqqsfsi 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1022 --QLVSNLKEENTLLKQEKEALNHRIVEQAKEmtetmEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEM 1099
Cdd:TIGR00618 575 ltQCDNRSKEDIPNLQNITVRLQDLTEKLSEA-----EDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1100 TLMVNVPKpghkrtdsthsSNESEYTFSSEIAETEDIPSRTEEPSEKKvpldmSLFLKLQKRVTELEQekqvmQDELDRK 1179
Cdd:TIGR00618 650 ALQLTLTQ-----------ERVREHALSIRVLPKELLASRQLALQKMQ-----SEKEQLTYWKEMLAQ-----CQTLLRE 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1180 EEQVLrskakEEERPQIRGAELEYESLKrQELESENKKLKNELNELRKALSEK-----SSPEVTAPGAPAYRVLMEQLTS 1254
Cdd:TIGR00618 709 LETHI-----EEYDREFNEIENASSSLG-SDLAAREDALNQSLKELMHQARTVlkartEAHFNNNEEVTAALQTGAELSH 782
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1255 VSEELDVRKEEVLILRSQLVSQKEAIQPKntmTDSTILLEDVQKMKDKGEIAQAYIGLKETNRSSAMDCHELNEDGelll 1334
Cdd:TIGR00618 783 LAAEIQFFNRLREEDTHLLKTLEAEIGQE---IPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYE---- 855
|
490 500
....*....|....*....|....*....
gi 2015234411 1335 vyEGLKQanrlLESQLQSQKRSHENEAEA 1363
Cdd:TIGR00618 856 --ECSKQ----LAQLTQEQAKIIQLSDKL 878
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
980-1244 |
1.95e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 980 IATGRVLSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKEentlLKQEKEALNHRIVEQAKEMTETMEK- 1058
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAEl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1059 -KLVEETKQLELDLNDERLRYQNLLNEFSRLEERyddlkEEMTLMVNVPKPghkrTDSTHSSNESEYTFSSEIAETEDIP 1137
Cdd:COG4942 86 aELEKEIAELRAELEAQKEELAELLRALYRLGRQ-----PPLALLLSPEDF----LDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1138 SRTEEpsekkvpldmslflkLQKRVTELEQEKQVMQDELDRKEEQVLR-SKAKEEERPQIRGAELEYESLKRQ--ELESE 1214
Cdd:COG4942 157 ADLAE---------------LAALRAELEAERAELEALLAELEEERAAlEALKAERQKLLARLEKELAELAAElaELQQE 221
|
250 260 270
....*....|....*....|....*....|
gi 2015234411 1215 NKKLKNELNELRKALSEKSSPEVTAPGAPA 1244
Cdd:COG4942 222 AEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
926-1098 |
2.18e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 926 ENKIMQLQRKVDEQNKDYKCLMEKLTNLEGTYNSETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDL-EQTRS 1004
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1005 EKK---------------SIEEHADRYKQeTEQLVSNLKEENTLLKQEKEALNHRI--VEQAKEMTETMEKKLVEETKQL 1067
Cdd:COG3883 95 LYRsggsvsyldvllgseSFSDFLDRLSA-LSKIADADADLLEELKADKAELEAKKaeLEAKLAELEALKAELEAAKAEL 173
|
170 180 190
....*....|....*....|....*....|.
gi 2015234411 1068 ELDLNDERLRYQNLLNEFSRLEERYDDLKEE 1098
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
972-1304 |
3.09e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 972 QLSEEEAKIATGRVLSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRI--VEQA 1049
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQeeLESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1050 KEMTETMEKKLVE---ETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLM---VNVPKPGHKRTDSTHSSNESE 1123
Cdd:COG4372 107 QEEAEELQEELEElqkERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLqeeLAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1124 YTFSSEIAETEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAELEY 1203
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1204 ESLKRQELESENKKLKNELNELRKALSEKSSPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPK 1283
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
330 340
....*....|....*....|.
gi 2015234411 1284 NTMTDSTILLEDVQKMKDKGE 1304
Cdd:COG4372 347 LVGLLDNDVLELLSKGAEAGV 367
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
639-663 |
3.30e-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: 3.30e-06
10 20
....*....|....*....|....*
gi 2015234411 639 FRNSLHLLMETLNATTPHYVRCIKP 663
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
900-1225 |
3.59e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.28 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 900 MAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLegTYNSETEKLRSDLERLQLSEEEAK 979
Cdd:TIGR00618 602 KLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTL--TQERVREHALSIRVLPKELLASRQ 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 980 IATGRVLSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVE-------QAKEM 1052
Cdd:TIGR00618 680 LALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKElmhqartVLKAR 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1053 TETMEKKLVEETKQLELDLNDERLRyQNLLNEFSRLEERYDDLKE-EMTLMVNVPKPGHKRTDSTHSSNESEYTFSSEIA 1131
Cdd:TIGR00618 760 TEAHFNNNEEVTAALQTGAELSHLA-AEIQFFNRLREEDTHLLKTlEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLE 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1132 ETE----DIPSRTEEPSEKKVPLDMSlfLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKE--EERPQIRGAELEYES 1205
Cdd:TIGR00618 839 EKSatlgEITHQLLKYEECSKQLAQL--TQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEitLYANVRLANQSEGRF 916
|
330 340
....*....|....*....|
gi 2015234411 1206 LKRQELESENKKLKNELNEL 1225
Cdd:TIGR00618 917 HGRYADSHVNARKYQGLALL 936
|
|
| fMyo4p_CBD |
cd15479 |
cargo binding domain of fungal myosin 4; Yeast myosin V travels along actin cables, actin ... |
1690-1818 |
4.57e-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: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1690 LNSFHSVMCQHGMDPELIKQVVKQMFYIVGAVTLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKnlmNSGAKETLEPL 1769
Cdd:cd15479 168 LNEFDAVLCKFQVVDSMHTKIFNDTLKYLNVMLFNDLITKCPALNWKYGYEVDRNIERLVSWFEPR---IEDVRPNLIQI 244
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2015234411 1770 IQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERV 1818
Cdd:cd15479 245 IQAVKILQLKISNLNEFKLLFDFWYALNPAQIQAILLKYKPANKGEAGV 293
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
904-1199 |
4.57e-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: 52.04 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 904 ELKKLKI------EARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTN----LEGTYN----------SETEK 963
Cdd:pfam15921 631 ELEKVKLvnagseRLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNkseeMETTTNklkmqlksaqSELEQ 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 964 LRSDLERLQLSEEEA-KIATGrvlsLQEEIAKLRKDLEQTRSEKKSIEEhadrykqeteqLVSNLKEENTLLKQEKEALN 1042
Cdd:pfam15921 711 TRNTLKSMEGSDGHAmKVAMG----MQKQITAKRGQIDALQSKIQFLEE-----------AMTNANKEKHFLKEEKNKLS 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1043 HRI----VEQAK-----EMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVN-VPKPGHkr 1112
Cdd:pfam15921 776 QELstvaTEKNKmagelEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKeLQGPGY-- 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1113 tdSTHSSNESEYTFSSEIAETE-DIPSRTEEPSekkvpldmslFLKLQKRVTELEQE------KQVMQD--ELDRKEEQV 1183
Cdd:pfam15921 854 --TSNSSMKPRLLQPASFTRTHsNVPSSQSTAS----------FLSHHSRKTNALKEdptrdlKQLLQElrSVINEEPTV 921
|
330
....*....|....*.
gi 2015234411 1184 LRSKAKEEERPQIRGA 1199
Cdd:pfam15921 922 QLSKAEDKGRAPSLGA 937
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
901-1099 |
4.82e-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: 51.98 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 901 AKRELKKLKIEARSVERYKKlhiGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGTYNSET---EKLRSDLERLQ----L 973
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLE---SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEeliEELESELEALLneraS 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 974 SEEEAKIATGRVLSLQEEIAKL---RKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKEENTllkqEKEALNHRIVEQAK 1050
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELeskRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS----EEYSLTLEEAEALE 960
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2015234411 1051 EMTETMEKKLVEETKQLELDLNdeRLRYQNL--LNEFSRLEERYDDLKEEM 1099
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIK--ELGPVNLaaIEEYEELKERYDFLTAQK 1009
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1132-1451 |
5.28e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1132 ETEDIPSRTEEPSEKKVPLDMSLfLKLQKRVTELEQEKQVMQDELDRKEEQVlrsKAKEEERPQIRGAELEYESlKRQEL 1211
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDL-ARLEAEVEQLEERIAQLSKELTELEAEI---EELEERLEEAEEELAEAEA-EIEEL 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1212 ESENKKLKNELNELRKALSEKSSpEVTAPGApAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKN-TMTDST 1290
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRA-ELTLLNE-EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaEIEELE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1291 ILLEdvqKMKDKGEIAQAYIGLKETNRSSAMDcHELNEDGELLLVYEGLKQANRLLEsQLQSQKRSHENEAEALRGEIQS 1370
Cdd:TIGR02168 866 ELIE---ELESELEALLNERASLEEALALLRS-ELEELSEELRELESKRSELRRELE-ELREKLAQLELRLEGLEVRIDN 940
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1371 LKEE-NNRQQQLLAQNLQLPPEARIE-ASLQHEITRLTNE-------NLYFEELYADDPKKYQ---SYRISLYKRMIDLM 1438
Cdd:TIGR02168 941 LQERlSEEYSLTLEEAEALENKIEDDeEEARRRLKRLENKikelgpvNLAAIEEYEELKERYDfltAQKEDLTEAKETLE 1020
|
330
....*....|...
gi 2015234411 1439 EQLEKQDKTVRKL 1451
Cdd:TIGR02168 1021 EAIEEIDREARER 1033
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
901-1456 |
6.27e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.51 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 901 AKRELKKLKIEARSVE--------RYKKLHIGMENK-IMQLQRKVDEQNKDYKCLMEKLTNLEGTYN------SETEKLR 965
Cdd:TIGR00618 265 LRARIEELRAQEAVLEetqerinrARKAAPLAAHIKaVTQIEQQAQRIHTELQSKMRSRAKLLMKRAahvkqqSSIEEQR 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 966 SDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTRSEKKSIEeHADRYKQETEQLVSNLKEENTllKQEKEALNHRI 1045
Cdd:TIGR00618 345 RLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKT-TLTQKLQSLCKELDILQREQA--TIDTRTSAFRD 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1046 VEQAKEMTETMEKKLVEETKQLELDLNDErlrYQNLLNEFSRLEERYDDLKEEMTLMVNVpKPGHKRTDSTHSSNESeyt 1125
Cdd:TIGR00618 422 LQGQLAHAKKQQELQQRYAELCAAAITCT---AQCEKLEKIHLQESAQSLKEREQQLQTK-EQIHLQETRKKAVVLA--- 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1126 FSSEIAETE-DIPSRTEEPSEKKV-----PLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQirga 1199
Cdd:TIGR00618 495 RLLELQEEPcPLCGSCIHPNPARQdidnpGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ---- 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1200 ELEYESLKRQELESENKKLKNELNELRKALSEKSSPEVTAPGApaYRVLMEQLTSVSEELDVRKEEVLILRSQ------- 1272
Cdd:TIGR00618 571 SFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE--QHALLRKLQPEQDLQDVRLHLQQCSQELalkltal 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1273 ------LVSQKEAIQPKNTMTDSTILLEDVQKMKDKGE-IAQAYIGLKET--NRSSAMDCHELNE--------------- 1328
Cdd:TIGR00618 649 halqltLTQERVREHALSIRVLPKELLASRQLALQKMQsEKEQLTYWKEMlaQCQTLLRELETHIeeydrefneienass 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1329 ------DGELLLVYEGLKQANRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNlqlppeaRIEASLQHEI 1402
Cdd:TIGR00618 729 slgsdlAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFN-------RLREEDTHLL 801
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 2015234411 1403 TRLTNEnlyFEELYADDPKKYQSYRISLYKRMIDLMEQLEKQDKTVRKLKKQLK 1456
Cdd:TIGR00618 802 KTLEAE---IGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLL 852
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
882-1518 |
7.28e-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: 51.13 E-value: 7.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 882 YRRSIHAIIYLQCCFRRMmaKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGTYNSET 961
Cdd:pfam02463 222 EEEYLLYLDYLKLNEERI--DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELK 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 962 EKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEAL 1041
Cdd:pfam02463 300 SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1042 NHRIVEQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEErydDLKEEMTLMVNVPKPGHKRTDSTHssnE 1121
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEE---LEILEEEEESIELKQGKLTEEKEE---L 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1122 SEYTFSSEIAETEDIPSRTEEPSEKKVPLDMslflKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAEL 1201
Cdd:pfam02463 454 EKQELKLLKDELELKKSEDLLKETQLVKLQE----QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHG 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1202 EYESLKRQELESENKKLKNELNELRKALSEKSS------PEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVS 1275
Cdd:pfam02463 530 RLGDLGVAVENYKVAISTAVIVEVSATADEVEErqklvrALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLD 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1276 QKEA-IQPKNTMTDSTILLEDVQKMKDKGEIAQAYIGlketnRSSAMDCHELNEDGELLLVYEGLKQANRLLESQLQSQK 1354
Cdd:pfam02463 610 KATLeADEDDKRAKVVEGILKDTELTKLKESAKAKES-----GLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEK 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1355 RSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLppEARIEASLQHEItrLTNENLYFEELYADDPKKYQSYRISLYKRM 1434
Cdd:pfam02463 685 AESELAKEEILRRQLEIKKKEQREKEELKKLKLE--AEELLADRVQEA--QDKINEELKLLKQKIDEEEEEEEKSRLKKE 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1435 IDLMEQLEKQDKTVRKLKKQLKVFAKKIGELEVGQMenvspgQIIDEPIRPVNIPRKEKDFQGMLEYKKEDEQKLVKNLI 1514
Cdd:pfam02463 761 EKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKL------KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
....
gi 2015234411 1515 LELK 1518
Cdd:pfam02463 835 LEEL 838
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
960-1374 |
7.43e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 7.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 960 ETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTRSEKKSIEEHADRYK--QETEQLVSNLKEENTLLKQE 1037
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1038 KEALN--HRIVEQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMtlmvnvpkpghKRTDS 1115
Cdd:COG4717 152 EERLEelRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL-----------EEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1116 THSSNESEYTFSSEIAETEDIPSRTEEPSEkkVPLDMSLFLKLqkrvteleqekQVMQDELDRKEEQVL----------- 1184
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARL--LLLIAAALLAL-----------LGLGGSLLSLILTIAgvlflvlglla 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1185 -------RSKAKEEERPQIRGAELEYESLKRQELESENKKLKnelnelrkaLSEKSSPEvtapGAPAYRVLMEQLTSVSE 1257
Cdd:COG4717 288 llflllaREKASLGKEAEELQALPALEELEEEELEELLAALG---------LPPDLSPE----ELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1258 ELDVRKEEVLIlrSQLVSQKEAIQPKNTMTDSTILLEdvqkmkdKGEIAQAYIGLKETNRSSAMDCHELNEDGELLLVYE 1337
Cdd:COG4717 355 EAEELEEELQL--EELEQEIAALLAEAGVEDEEELRA-------ALEQAEEYQELKEELEELEEQLEELLGELEELLEAL 425
|
410 420 430
....*....|....*....|....*....|....*..
gi 2015234411 1338 GLKQANRLLEsQLQSQKRSHENEAEALRGEIQSLKEE 1374
Cdd:COG4717 426 DEEELEEELE-ELEEELEELEEELEELREELAELEAE 461
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
929-1203 |
8.03e-06 |
|
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: 51.20 E-value: 8.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 929 IMQLQRKVDEQNKDYKCLMEKLTNLEG--TYNSETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTRSEK 1006
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQAAKLQGSDLdrTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEK 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1007 KSIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRI-VEQAKEMTETMEKKLV----EETKQLELDLNDERLRYQNL 1081
Cdd:TIGR00606 874 LQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSpLETFLEKDQQEKEELIsskeTSNKKAQDKVNDIKEKVKNI 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1082 LNEFSRLEERYDDLKEEM---------TLMVNVPKPGHKRTDSTHSSNESEYTF-SSEIAET---EDIPSRTEEPSEKKV 1148
Cdd:TIGR00606 954 HGYMKDIENKIQDGKDDYlkqketelnTVNAQLEECEKHQEKINEDMRLMRQDIdTQKIQERwlqDNLTLRKRENELKEV 1033
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2015234411 1149 PLDMSLFLKL--QKRVTELEQEKQVMQDELD--------------RKEEQVLRSKAKEEErPQIRGAELEY 1203
Cdd:TIGR00606 1034 EEELKQHLKEmgQMQVLQMKQEHQKLEENIDlikrnhvlalgrqkGYEKEIKHFKKELRE-PQFRDAEEKY 1103
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
901-1508 |
8.03e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 8.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 901 AKRELKKLKIEARSVERYKklhIGMENKIMQLQRKVDEQNKdykclMEKLTNLEGTYNSETEKLRSDLERLQLS---EEE 977
Cdd:PTZ00121 1092 ATEEAFGKAEEAKKTETGK---AEEARKAEEAKKKAEDARK-----AEEARKAEDARKAEEARKAEDAKRVEIArkaEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 978 AKIATGRVLSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVEQAKEMTEtmE 1057
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAE--E 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1058 KKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVNVPKPGHKRTDSTHSSNESEYTFSSEIAETEDIP 1137
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAK 1321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1138 SRTEEPSEKKVPLDMSLFLKlQKRVTELEQEKQVMQDELDRKEEQVLRSKAK-EEERPQIRGAELEYESLKR-QELESEN 1215
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEA-KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKkEEAKKKADAAKKKAEEKKKaDEAKKKA 1400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1216 KKLKNELNELRKALSEKSSPEVTAPGAPAYRVlMEQLTSVSEEldVRKEEVLILRSQLVSQKEAIQPKNTMTdstillED 1295
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKK-ADEAKKKAEE--AKKADEAKKKAEEAKKAEEAKKKAEEA------KK 1471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1296 VQKMKDKGEIAQAYIGLKETNRSSAMDCHELNEDGELLLVYEGLKQANRLLESQlQSQKRSHENEAEALRG--------E 1367
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD-EAKKAEEAKKADEAKKaeekkkadE 1550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1368 IQSLKEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNE-------NLYFEE--LYADDPKKYQSYRISlykrmidlM 1438
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEarieevmKLYEEEkkMKAEEAKKAEEAKIK--------A 1622
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2015234411 1439 EQLEKQDKtVRKLKKQLkvfaKKIGELEVGQMENVSPGQiIDEPIRPVNIPRK-EKDFQGMLEYKKEDEQK 1508
Cdd:PTZ00121 1623 EELKKAEE-EKKKVEQL----KKKEAEEKKKAEELKKAE-EENKIKAAEEAKKaEEDKKKAEEAKKAEEDE 1687
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
897-1230 |
8.52e-06 |
|
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: 51.20 E-value: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 897 RRMMAKRELKKLKIEARSVERYKKlhiGMENKIMQLQRKVD---EQNKDYKCLME------KLTNLEGTYNSETEKLRSD 967
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQEKT---ELLVEQGRLQLQADrhqEHIRARDSLIQslatrlELDGFERGPFSERQIKNFH 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 968 LERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKEENTLLkQEKEALNHRIVE 1047
Cdd:TIGR00606 397 TLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL-QQLEGSSDRILE 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1048 QAKEMTETM-------EKKLVEETKQLELDLNDERLryqNLLNEFSRLEERYDDLKEEMTLMVNVPKPGHKRTDSTHSSN 1120
Cdd:TIGR00606 476 LDQELRKAErelskaeKNSLTETLKKEVKSLQNEKA---DLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIR 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1121 ESEYTFSSE-IAETEDIP-----SRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKeeerp 1194
Cdd:TIGR00606 553 KIKSRHSDElTSLLGYFPnkkqlEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDK----- 627
|
330 340 350
....*....|....*....|....*....|....*.
gi 2015234411 1195 qirgaelEYESLKRQELESENKKLKNELNELRKALS 1230
Cdd:TIGR00606 628 -------LFDVCGSQDEESDLERLKEEIEKSSKQRA 656
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
926-1098 |
1.08e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 926 ENKIMQLQRKVDEQNKDYKCLMEKLTNLEGTYNSETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTRSE 1005
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1006 ----------------------KKSIEEHADR------YKQETEQLVSNLKEENTLLKQEKEALnhrivEQAKEMTETME 1057
Cdd:COG4942 106 laellralyrlgrqpplalllsPEDFLDAVRRlqylkyLAPARREQAEELRADLAELAALRAEL-----EAERAELEALL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2015234411 1058 KKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEE 1098
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1129-1270 |
1.48e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.86 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1129 EIAETEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLR-----SKAKEEERPQIRgAELEY 1203
Cdd:COG2433 389 ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERlerelSEARSEERREIR-KDREI 467
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2015234411 1204 ESLKR--QELESENKKLKNELNELR------KALSEKSSPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILR 1270
Cdd:COG2433 468 SRLDReiERLERELEEERERIEELKrklerlKELWKLEHSGELVPVKVVEKFTKEAIRRLEEEYGLKEGDVVYLR 542
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1035-1374 |
1.77e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.97 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1035 KQEKEALNHRIVEQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEfSRLEERYDDLKEEMTLMVNvpkpghKRTD 1114
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEK-LELEEEYLLYLDYLKLNEE------RIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1115 STHSSNESEYTFSSEIAETEDipsrtEEPSEKKVpldmslfLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERP 1194
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEK-----EEEKLAQV-------LKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1195 QIRGAELEYESLKRQELESENKKLKNELNELRKALSEKSSPEVtapgapAYRVLMEQLTSVSEELDVRKEEVLILRSQLV 1274
Cdd:pfam02463 310 VDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKRE------AEEEEEEELEKLQEKLEQLEEELLAKKKLES 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1275 SQKEAIQPKNTMTDStILLEDVQKMKDKGEIAQAYIG-LKETNRSSAMDCHELNEDGELLLVYEGLKQANRLLESQLQSQ 1353
Cdd:pfam02463 384 ERLSSAAKLKEEELE-LKSEEEKEAQLLLELARQLEDlLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340
....*....|....*....|.
gi 2015234411 1354 KRSHENEAEALRGEIQSLKEE 1374
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQ 483
|
|
| IQ |
pfam00612 |
IQ calmodulin-binding motif; Calmodulin-binding motif. |
815-835 |
2.38e-05 |
|
IQ calmodulin-binding motif; Calmodulin-binding motif.
Pssm-ID: 459869 Cd Length: 21 Bit Score: 42.69 E-value: 2.38e-05
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
901-1231 |
3.17e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 901 AKRELKKLKIEARSVErykklhigmenKIMQLQRKVDEqnkdYKCLMEKLTNLEgtynsetEKLRS-DLERLQLSEEEAK 979
Cdd:PRK03918 471 IEEKERKLRKELRELE-----------KVLKKESELIK----LKELAEQLKELE-------EKLKKyNLEELEKKAEEYE 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 980 iatgrvlSLQEEIAKLRKDLEQTRSEKKSIEEhadrYKQETEQLVSNLKEentlLKQEKEALNHRIVEQAKEMTETMEKK 1059
Cdd:PRK03918 529 -------KLKEKLIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLDE----LEEELAELLKELEELGFESVEELEER 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1060 L--VEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVNVPKPGHKRTdsthssNESEYTFSSEiaetedip 1137
Cdd:PRK03918 594 LkeLEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL------EELEKKYSEE-------- 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1138 sRTEEPSEKKVPLDMSLFlKLQKRVTELEQEKQVMQDELDRKEEQvlrskaKEEerpqIRGAELEYESLKR-----QELE 1212
Cdd:PRK03918 660 -EYEELREEYLELSRELA-GLRAELEELEKRREEIKKTLEKLKEE------LEE----REKAKKELEKLEKalervEELR 727
|
330
....*....|....*....
gi 2015234411 1213 SENKKLKNELNElrKALSE 1231
Cdd:PRK03918 728 EKVKKYKALLKE--RALSK 744
|
|
| MyosinXI_CBD |
cd15475 |
cargo binding domain of myosin XI; Class XI myosins are a plant specific group, homologous to ... |
1555-1808 |
3.63e-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: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1555 LTSTINSIKKVlkkrGDDFETVSFWLSNTCRFLhCLKQysgeegfmkhntsrqneHCLTnfdlaeyrqvlsdlAIQIYQQ 1634
Cdd:cd15475 52 IIQTIGSAIED----QDNNDHLAYWLSNTSTLL-FLLQ-----------------RSLP--------------ALLFKQQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1635 LVRVLENILqPMI-------VSGMLEhETIQGVSGVKPTGLRKRTSSIADEGTYTL---DSILRQLNSFHSVMCQHGMDP 1704
Cdd:cd15475 96 LTAYVEKIY-GIIrdnlkkeLSPLLS-LCIQAPRTSRGSSSKSSSSANSLGQQSPSshwQSIIKSLNSLLSTLKENHVPP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1705 ELIKQVVKQMF-YIvgAVTL-NNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDknlmnsgAKET--------LEPLIQAAQ 1774
Cdd:cd15475 174 FLVQKIFTQVFsFI--NVQLfNSLLLRRECCSFSNGEYVKAGLAELELWCSQ-------ATEEyagsswdeLKHIRQAVG 244
|
250 260 270
....*....|....*....|....*....|....*
gi 2015234411 1775 LLQVKKKTDDDAEAICS-MCNALTTAQIVKVLNLY 1808
Cdd:cd15475 245 FLVIHQKSRKSYDEITNdLCPVLSVQQLYRICTMY 279
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
911-1306 |
3.96e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 48.66 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 911 EARSVERYKKLHIGMENKIMQL----QRKVDE-------------QNKDYK----CLMEKLTNLE---GTYNSETEKLRS 966
Cdd:pfam10174 273 EIKQMEVYKSHSKFMKNKIDQLkqelSKKESEllalqtkletltnQNSDCKqhieVLKESLTAKEqraAILQTEVDALRL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 967 DLER-----------LQLSEEEAKIATG--------------RVLSLQEEIAKLrkdLEQTRSEKKSIEEHADRYKqETE 1021
Cdd:pfam10174 353 RLEEkesflnkktkqLQDLTEEKSTLAGeirdlkdmldvkerKINVLQKKIENL---QEQLRDKDKQLAGLKERVK-SLQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1022 QLVSNlkeENTLLKQEKEAL--NHRIVEQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEM 1099
Cdd:pfam10174 429 TDSSN---TDTALTTLEEALseKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHA 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1100 TlmvNVPKPGHKRtDSTHSSNEseytfsSEIAETEDIPSRTEEPSEKKVPLDMSLFLK--LQKRVTELEQEKQVMQDELD 1177
Cdd:pfam10174 506 S---SLASSGLKK-DSKLKSLE------IAVEQKKEECSKLENQLKKAHNAEEAVRTNpeINDRIRLLEQEVARYKEESG 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1178 RKEEQV------LRSKAKEEERPQIRGAELeyESLKRQELESENKK---LKNELNELRK---ALSEKSSPEVTAPGAPAY 1245
Cdd:pfam10174 576 KAQAEVerllgiLREVENEKNDKDKKIAEL--ESLTLRQMKEQNKKvanIKHGQQEMKKkgaQLLEEARRREDNLADNSQ 653
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2015234411 1246 RVLMEQLTsvsEELDVRKEEVLILRSQLVSQKEAIQPKNTMTDSTIL-----LEDVQKMKDKGEIA 1306
Cdd:pfam10174 654 QLQLEELM---GALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAerrkqLEEILEMKQEALLA 716
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
906-1081 |
4.34e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 906 KKLKIEARSVERYKKlHIGMENkimqlqRKVDEqnkdykcLMEKLTNLE---GTYNSETEKLRSDLERLQLSEEEAKIat 982
Cdd:PRK00409 495 KRLGLPENIIEEAKK-LIGEDK------EKLNE-------LIASLEELErelEQKAEEAEALLKEAEKLKEELEEKKE-- 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 983 grvlSLQEEIAKLRKDLEQ-----TRSEKKSIEEHADRYKQETEQLVSNLKEentllKQEKEAlnHRIVEQAKEMTEtmE 1057
Cdd:PRK00409 559 ----KLQEEEDKLLEEAEKeaqqaIKEAKKEADEIIKELRQLQKGGYASVKA-----HELIEA--RKRLNKANEKKE--K 625
|
170 180
....*....|....*....|....
gi 2015234411 1058 KKLVEETKQLELDLNDeRLRYQNL 1081
Cdd:PRK00409 626 KKKKQKEKQEELKVGD-EVKYLSL 648
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
904-1277 |
4.41e-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: 48.15 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 904 ELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEqnkdykcLMEKLTNLEGT---YNSETEKLRSDLERLQLSEEEAKI 980
Cdd:pfam05622 36 ENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQ-------LQEENFRLETArddYRIKCEELEKEVLELQHRNEELTS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 981 ATGRVLSLQEEIAKLR------KDLEQT-RSEKKSIEEHADRYKQeteqlVSNLKEENTLLKQEKEALNhrivEQAKEMT 1053
Cdd:pfam05622 109 LAEEAQALKDEMDILRessdkvKKLEATvETYKKKLEDLGDLRRQ-----VKLLEERNAEYMQRTLQLE----EELKKAN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1054 ------ETMEKKLVEetkqLELDLNDERLRYQNLLNEFSRLEERYDDL-KEEMTLMVnvpkpghkRTDSTHSSNE----- 1121
Cdd:pfam05622 180 alrgqlETYKRQVQE----LHGKLSEESKKADKLEFEYKKLEEKLEALqKEKERLII--------ERDTLRETNEelrca 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1122 --SEYTFSSEIAETEDIPSRTEEPSEKKVPLDmslflkLQKRVTELEQEKQVMQdeldrkeeqvLRSKAKEEERPQIRGA 1199
Cdd:pfam05622 248 qlQQAELSQADALLSPSSDPGDNLAAEIMPAE------IREKLIRLQHENKMLR----------LGQEGSYRERLTELQQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1200 ELEYESLKRQELESENKK-------LKNELNELRKALSEKSS-PEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRS 1271
Cdd:pfam05622 312 LLEDANRRKNELETQNRLanqrileLQQQVEELQKALQEQGSkAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEP 391
|
....*.
gi 2015234411 1272 QLVSQK 1277
Cdd:pfam05622 392 KQDSNL 397
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
925-1205 |
7.16e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 925 MENKIMQLQRKVDEQNKDYKCLMEKLTNLEGTYNSETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTRS 1004
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1005 EKKSIEEHADRYKQETEQLVSNLKEENTLLKQ---EKEALNHRIVEQAKEMTETMEKKLVEETKQLELDLNDERLRYQNL 1081
Cdd:COG4372 123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKEleeQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEEL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1082 LNEFSRLEERYDDLKEEMTLMVNVPKPGHKRTDSTHSSNESEYTFSSEIAETEDIPSRTEEPSEKKVPLDMSLFLKLQKR 1161
Cdd:COG4372 203 AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAA 282
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2015234411 1162 VTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAELEYES 1205
Cdd:COG4372 283 LELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
971-1099 |
1.07e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 971 LQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVEQAK 1050
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2015234411 1051 ------------------------EMTETM---EKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEM 1099
Cdd:COG3883 98 sggsvsyldvllgsesfsdfldrlSALSKIadaDADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
923-1129 |
1.20e-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: 46.98 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 923 IGMENKIMqlqrKVDEQNKdYKCLMEKLTNLEGTYnSETEKLRSDLERLQlseeEAKIATGRVLSLQEEIAKLRKDLEQT 1002
Cdd:pfam05911 624 SSMEDEIK----KHDCIDK-VTLSENKVAQVDNGC-SEIDNLSSDPEIPS----DGPLVSGSNDLKTEENKRLKEEFEQL 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1003 RSEKKSIEEHADRYK----------QETEQLVSNLKEENTLLKQekeaLNHRIVEQAKEMTEtMEKKLVEETKQLELDLN 1072
Cdd:pfam05911 694 KSEKENLEVELASCTenlestksqlQESEQLIAELRSELASLKE----SNSLAETQLKCMAE-SYEDLETRLTELEAELN 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2015234411 1073 DERLRYQNLLNEFS-------RLEERYDDLKEEMTLMVNVPKPGHKRTDS-THSSNESEYTFSSE 1129
Cdd:pfam05911 769 ELRQKFEALEVELEeekncheELEAKCLELQEQLERNEKKESSNCDADQEdKKLQQEKEITAASE 833
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1156-1465 |
1.28e-04 |
|
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: 46.97 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1156 LKLQKRVTELEQEKQVMQDELDrKEEQVLRSKAKEEERPQIRGAELEYESlKRQELESENKKLKNELNELRKALSEKSSP 1235
Cdd:TIGR02168 205 LERQAEKAERYKELKAELRELE-LALLVLRLEELREELEELQEELKEAEE-ELEELTAELQELEEKLEELRLEVSELEEE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1236 EVTAPGApayrvlMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIqpkntmtdSTILLEDVQKMKDKGEIAQAyiglKET 1315
Cdd:TIGR02168 283 IEELQKE------LYALANEISRLEQQKQILRERLANLERQLEEL--------EAQLEELESKLDELAEELAE----LEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1316 NRSSAMDCHELNEdgELLLVYEGLKQAnrlLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLlaqnlqlppEARIE 1395
Cdd:TIGR02168 345 KLEELKEELESLE--AELEELEAELEE---LESRLEELEEQLETLRSKVAQLELQIASLNNEIERL---------EARLE 410
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2015234411 1396 aSLQHEITRLTNENLYFEELYADDPKKYQSYRISLYKRMI--------DLMEQLEKQDKTVRKLKKQLKVFAKKIGEL 1465
Cdd:TIGR02168 411 -RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELeelqeeleRLEEALEELREELEEAEQALDAAERELAQL 487
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
926-1095 |
1.92e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 926 ENKIMQLQRKVDEQNKDYKCLMEKLTNLEGTYnSETEKLRSDLErLQLSEEEAKIATGRVL-----------SLQEEIAK 994
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTEL-EDLEKEIKRLE-LEIEEVEARIKKYEEQlgnvrnnkeyeALQKEIES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 995 LRKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVEQAKEmtetmEKKLVEETKQLELDLNDE 1074
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE-----LEELEAEREELAAKIPPE 175
|
170 180
....*....|....*....|.
gi 2015234411 1075 rlryqnLLNEFSRLEERYDDL 1095
Cdd:COG1579 176 ------LLALYERIRKRKNGL 190
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
960-1098 |
2.13e-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: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 960 ETEKLRSDLERL-----QLSEEEAKIATGRVLSLQEEIAKLRKDLEQTRsekKSIEEHADRYKQETEQLvsNLKEENTLL 1034
Cdd:pfam08614 22 ENAKLQSEPESVlpstsSSKLSKASPQSASIQSLEQLLAQLREELAELY---RSRGELAQRLVDLNEEL--QELEKKLRE 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2015234411 1035 KQEKEALNHRIVEQAKEMTETMEKKLVEETKQLElDLNDErlrYQNLLNEFSRLEERYDDLKEE 1098
Cdd:pfam08614 97 DERRLAALEAERAQLEEKLKDREEELREKRKLNQ-DLQDE---LVALQLQLNMAEEKLRKLEKE 156
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
959-1480 |
2.18e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 959 SETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEqtrSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEK 1038
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQ---LLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1039 EALNH----RIVEQAKEMTETMEKKLVEETKQLE-----LDLNDERLRYQ----NLLNEFSRL-------EERYDDLKEE 1098
Cdd:TIGR00618 240 QSHAYltqkREAQEEQLKKQQLLKQLRARIEELRaqeavLEETQERINRArkaaPLAAHIKAVtqieqqaQRIHTELQSK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1099 MTLMVNVPKPGHKRTDSTHSSNESEYTFSSEIAETEDIPSRTEEPSEKKVPLDMSL-----FLKLQKRVTELEQEKQVMQ 1173
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHtltqhIHTLQQQKTTLTQKLQSLC 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1174 DELDRKEEQVLRSKAKEEERPQIRG----------AELEYESLKRQELESENKKLKNE---LNELRKALSEKSSPEVTAp 1240
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDLQGqlahakkqqeLQQRYAELCAAAITCTAQCEKLEkihLQESAQSLKEREQQLQTK- 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1241 gapayRVLMEQLTSVSEELDVRKEEVLILRSQLvsQKEAIQPKNTMTDSTIL---------LEDVQKMKDKGEIAQAYIG 1311
Cdd:TIGR00618 479 -----EQIHLQETRKKAVVLARLLELQEEPCPL--CGSCIHPNPARQDIDNPgpltrrmqrGEQTYAQLETSEEDVYHQL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1312 LKETNRSSAMDCHELNEDGELLLV----------YEGLKQANRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQL 1381
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQSFSILtqcdnrskedIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1382 LAQNLQLPPEARIEASLQHEITRLTNENLYFEELYA-DDPKKYQSYRISLYKRMIDLMEQLEKQDKTVRKLKKQLKVFAK 1460
Cdd:TIGR00618 632 LHLQQCSQELALKLTALHALQLTLTQERVREHALSIrVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELET 711
|
570 580
....*....|....*....|..
gi 2015234411 1461 KIGEL--EVGQMENVSPGQIID 1480
Cdd:TIGR00618 712 HIEEYdrEFNEIENASSSLGSD 733
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
902-1231 |
2.20e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 902 KRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGTYNSETEKLRSDLERLQLSEEEAkia 981
Cdd:PRK01156 345 KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDI--- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 982 TGRVLSLQEEIAKLRKDLEQTRSEKKSI--------------EEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVE 1047
Cdd:PRK01156 422 SSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVD 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1048 QaKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEE---RYDDLKEEMTLM---------------------V 1103
Cdd:PRK01156 502 L-KKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDkhdKYEEIKNRYKSLkledldskrtswlnalavislI 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1104 NVPKPGHKRTDSTHSSNESEYTFSSEIAETEDIPSRTE-------------EPSEKKVPLDMSLFLKLQKRVTELEQEKQ 1170
Cdd:PRK01156 581 DIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDksireieneannlNNKYNEIQENKILIEKLRGKIDNYKKQIA 660
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2015234411 1171 VMQDELDRKEEQVLRSKAKEEERPQIRGAeLEYESLKRQELESENKKLKNELNELRKALSE 1231
Cdd:PRK01156 661 EIDSIIPDLKEITSRINDIEDNLKKSRKA-LDDAKANRARLESTIEILRTRINELSDRIND 720
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
906-1231 |
2.21e-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: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 906 KKLKIEARSVE-RYKKlhigMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGTYNSETEKLRSdLERLQLsEEEAKIATGR 984
Cdd:pfam01576 120 QKLQLEKVTTEaKIKK----LEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKS-LSKLKN-KHEAMISDLE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 985 VLSLQEEiaKLRKDLEQTRseKKSIEEHADRYKQ--ETEQLVSNLKEENTLLKQEKEALNHRIVEQAKEMTETMEK--KL 1060
Cdd:pfam01576 194 ERLKKEE--KGRQELEKAK--RKLEGESTDLQEQiaELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKirEL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1061 VEETKQLELDLNDERLRYqnllnefSRLEERYDDLKEEMTLMvnvpkpghkRTdsthssnESEYTFSSEIAETEDIPSRT 1140
Cdd:pfam01576 270 EAQISELQEDLESERAAR-------NKAEKQRRDLGEELEAL---------KT-------ELEDTLDTTAAQQELRSKRE 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1141 EEPSEKKVPLDmSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAK--------EEERPQIRgAELEYESLKRQELE 1212
Cdd:pfam01576 327 QEVTELKKALE-EETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANlekakqalESENAELQ-AELRTLQQAKQDSE 404
|
330
....*....|....*....
gi 2015234411 1213 SENKKLKNELNELRKALSE 1231
Cdd:pfam01576 405 HKRKKLEGQLQELQARLSE 423
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
899-1295 |
2.41e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 899 MMAKRELKKLKIEARSVERYKklhigMENKIMQLQRKVDEQ-------NKDYKCLMEKLTNLEgtynSETEKLRSDLERL 971
Cdd:PRK02224 298 LLAEAGLDDADAEAVEARREE-----LEDRDEELRDRLEECrvaaqahNEEAESLREDADDLE----ERAEELREEAAEL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 972 Q--LSEEEAKIATGR--VLSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEAL--NHRI 1045
Cdd:PRK02224 369 EseLEEAREAVEDRReeIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVeeAEAL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1046 VEQAK-----------EMTETMEKKLvEETKQLELDLNDERLRYQNLLNEFSRLEE------RYDDLKEEMTLMVNVPKP 1108
Cdd:PRK02224 449 LEAGKcpecgqpvegsPHVETIEEDR-ERVEELEAELEDLEEEVEEVEERLERAEDlveaedRIERLEERREDLEELIAE 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1109 GHKRTDSTH----SSNESEYTFSSEIAETEDIPSRTEEPSEKKvpldmslflklQKRVTELEQEKQVMQDELDRKEEQVL 1184
Cdd:PRK02224 528 RRETIEEKReraeELRERAAELEAEAEEKREAAAEAEEEAEEA-----------REEVAELNSKLAELKERIESLERIRT 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1185 RSKAKEEERPQIrgAELEYESLKRQELESENKKLKNELNELRKALSEKSSPEVTApGAPAYRVLMEQ-LTSVSEELDVRK 1263
Cdd:PRK02224 597 LLAAIADAEDEI--ERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIE-EAREDKERAEEyLEQVEEKLDELR 673
|
410 420 430
....*....|....*....|....*....|..
gi 2015234411 1264 EEVLILRSQLVSQKEAIQPKNTMTDSTILLED 1295
Cdd:PRK02224 674 EERDDLQAEIGAVENELEELEELRERREALEN 705
|
|
| IQCD |
cd23767 |
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
809-838 |
2.87e-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: 39.83 E-value: 2.87e-04
10 20 30
....*....|....*....|....*....|
gi 2015234411 809 AKFLRRTKAATIIQKYWRMYVARRRYKIMR 838
Cdd:cd23767 3 EELQRMNRAATLIQALWRGYKVRKELKKKK 32
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
926-1374 |
2.92e-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: 45.94 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 926 ENKIMQLQRKVDEQNKDYKCLMEKLTNLEGtYNSEtekLRSDLERLQLSEEEAkiaTGRVLSLQEEIAKLRKDLEQT--- 1002
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEA-QISE---LQEDLESERAARNKA---EKQRRDLGEELEALKTELEDTldt 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1003 -------RSE--------KKSIEEHADRYKQE---------------TEQLvSNLKEENTLLKQEKEALNHRIVEQAKEM 1052
Cdd:pfam01576 315 taaqqelRSKreqevtelKKALEEETRSHEAQlqemrqkhtqaleelTEQL-EQAKRNKANLEKAKQALESENAELQAEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1053 TETMEKKLVEET--KQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEM----TLMVNVPKPGHKRTDSTHSsneseytF 1126
Cdd:pfam01576 394 RTLQQAKQDSEHkrKKLEGQLQELQARLSESERQRAELAEKLSKLQSELesvsSLLNEAEGKNIKLSKDVSS-------L 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1127 SSEIAETEDIpsRTEEPSEKkvpldmslfLKLQKRVTELEQEKQVMQDELDrKEEQVLRSKAKEEERPQIRGAE----LE 1202
Cdd:pfam01576 467 ESQLQDTQEL--LQEETRQK---------LNLSTRLRQLEDERNSLQEQLE-EEEEAKRNVERQLSTLQAQLSDmkkkLE 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1203 YESLKRQELESENKKLKNELNELRKALSEKSSpevtapgapAYRVLMEQLTSVSEELDVRKEEVLILRsQLVSQKEAIQP 1282
Cdd:pfam01576 535 EDAGTLEALEEGKKRLQRELEALTQQLEEKAA---------AYDKLEKTKNRLQQELDDLLVDLDHQR-QLVSNLEKKQK 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1283 KNtmtdSTILLED---VQKMKDKGEIAQAYIGLKETNRSSAmdCHELNEDGELLlvyEGLKQANRLLES----------- 1348
Cdd:pfam01576 605 KF----DQMLAEEkaiSARYAEERDRAEAEAREKETRALSL--ARALEEALEAK---EELERTNKQLRAemedlvsskdd 675
|
490 500 510
....*....|....*....|....*....|..
gi 2015234411 1349 ------QLQSQKRSHENEAEALRGEIQSLKEE 1374
Cdd:pfam01576 676 vgknvhELERSKRALEQQVEEMKTQLEELEDE 707
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
925-1273 |
2.99e-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: 45.94 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 925 MENKIMQLQRKVDEQNKDYKCLMEKLTNLEGtynsETEKLRSDLERLQLSEEE----AKIATGRVLSLQEEIAKLRKDLE 1000
Cdd:pfam01576 775 LELDLKELEAQIDAANKGREEAVKQLKKLQA----QMKDLQRELEEARASRDEilaqSKESEKKLKNLEAELLQLQEDLA 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1001 QTRSEKKSIEEHADRYKQEteqlVSNLKEENTLLKQEKEALNHRIVEQAKEMTE---TME------KKLVEETKQLELDL 1071
Cdd:pfam01576 851 ASERARRQAQQERDELADE----IASGASGKSALQDEKRRLEARIAQLEEELEEeqsNTEllndrlRKSTLQVEQLTTEL 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1072 NDERLRYQNLLNEFSRLEERYDDLKEEMTLMVNVPKPGHKRTDSthssneseyTFSSEIAETE---DIPSRTEEPSEKKV 1148
Cdd:pfam01576 927 AAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIA---------ALEAKIAQLEeqlEQESRERQAANKLV 997
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1149 pldmslflklqkRVTELEQEKQVMQDELDRKEeqvlrskaKEEERPQIRGAELEYESLKRQELESENkklknelnelrka 1228
Cdd:pfam01576 998 ------------RRTEKKLKEVLLQVEDERRH--------ADQYKDQAEKGNSRMKQLKRQLEEAEE------------- 1044
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2015234411 1229 lseksspEVTAPGApAYRVLMEQLTSVSEELDVRKEEVLILRSQL 1273
Cdd:pfam01576 1045 -------EASRANA-ARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
900-1504 |
3.42e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.81 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 900 MAKRELKKLKIEARSVERYkklhigMENKIMQLQRKVDEqnkdYKCLMEKLTNLEGTYNSETEK---LRSDLERLQLSEE 976
Cdd:TIGR00606 423 LKQEQADEIRDEKKGLGRT------IELKKEILEKKQEE----LKFVIKELQQLEGSSDRILELdqeLRKAERELSKAEK 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 977 EAKIAT--GRVLSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQeTEQLVSNLKEENTLLKQEKEALNHRIVEQA----- 1049
Cdd:TIGR00606 493 NSLTETlkKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQ-MEMLTKDKMDKDEQIRKIKSRHSDELTSLLgyfpn 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1050 KEMTETMEKKLVEETKQLELDLNDERLRYQNL-------LNEFSRLEERYDDLKEEM--------------TLMVNVPKP 1108
Cdd:TIGR00606 572 KKQLEDWLHSKSKEINQTRDRLAKLNKELASLeqnknhiNNELESKEEQLSSYEDKLfdvcgsqdeesdleRLKEEIEKS 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1109 GHKRTDSTHSSNeseyTFSSEIAETEDipsrteePSEKKVPLDMSLF---LKLQKRVTELEQEKQVMQDELDRKEEQVlr 1185
Cdd:TIGR00606 652 SKQRAMLAGATA----VYSQFITQLTD-------ENQSCCPVCQRVFqteAELQEFISDLQSKLRLAPDKLKSTESEL-- 718
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1186 sKAKEEERPQI------RGAELEYESLKRQELESENKKLKNELNELRKALSEKSSP-EVTAPGAPAYRVLMEQLTsVSEE 1258
Cdd:TIGR00606 719 -KKKEKRRDEMlglapgRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlGTIMPEEESAKVCLTDVT-IMER 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1259 LDVRKEEVLILRSQLVSQKEAIQPKNTMTDSTILLEDVQ----KMKDKGEIAQAYIglKETNRSSAMDCHELNEDG-ELL 1333
Cdd:TIGR00606 797 FQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQheldTVVSKIELNRKLI--QDQQEQIQHLKSKTNELKsEKL 874
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1334 LVYEGLKQANRLLE------SQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQHEitRLTN 1407
Cdd:TIGR00606 875 QIGTNLQRRQQFEEqlvelsTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKE--KVKN 952
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1408 ENLYFEELY------ADDPKKYQSYRIS---------------------LYKRMIDLMEQLE----------KQDKTVRK 1450
Cdd:TIGR00606 953 IHGYMKDIEnkiqdgKDDYLKQKETELNtvnaqleecekhqekinedmrLMRQDIDTQKIQErwlqdnltlrKRENELKE 1032
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 2015234411 1451 LKKQLKVFAKKIGELEVGQMENVSpgQIIDEPIRpvNIPRKE-KDFQGMLEYKKE 1504
Cdd:TIGR00606 1033 VEEELKQHLKEMGQMQVLQMKQEH--QKLEENID--LIKRNHvLALGRQKGYEKE 1083
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
931-1458 |
3.43e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.60 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 931 QLQRKVDEQNKDYKCLMEKLTNLEGTYNSETEKLRSDLERL--QLSEEEAKIATGRVLSLQEEiaklRKDLEQTRSEKKS 1008
Cdd:pfam12128 351 SWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDiaGIKDKLAKIREARDRQLAVA----EDDLQALESELRE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1009 IEEHADR-YKQETEQLVSNLKEENTLLKQ----EKEALNhriVEQAKEMTETMEKKLVEETKQLElDLNDERLRYQNLLN 1083
Cdd:pfam12128 427 QLEAGKLeFNEEEYRLKSRLGELKLRLNQatatPELLLQ---LENFDERIERAREEQEAANAEVE-RLQSELRQARKRRD 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1084 EFS--------RLEERYDDLKEEMTLMVnvPKPGH-------------------------KRTD----STHSSNESEYTF 1126
Cdd:pfam12128 503 QASealrqasrRLEERQSALDELELQLF--PQAGTllhflrkeapdweqsigkvispellHRTDldpeVWDGSVGGELNL 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1127 ------------SSEIAETEDIPSR---------TEEPSEKKVPLDMSLF-LKLQKRVTELEQEKQ-------------- 1170
Cdd:pfam12128 581 ygvkldlkridvPEWAASEEELRERldkaeealqSAREKQAAAEEQLVQAnGELEKASREETFARTalknarldlrrlfd 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1171 VMQDELDRKEEQVLRSKAKEEERpqirgaeleyeslkRQELESENKKLKNELNELRKALSEKSSpEVTAPGAPAYRVLME 1250
Cdd:pfam12128 661 EKQSEKDKKNKALAERKDSANER--------------LNSLEAQLKQLDKKHQAWLEEQKEQKR-EARTEKQAYWQVVEG 725
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1251 QLtsvSEELDVRKEEVLILRSQLVSQKEAIQPKNTmtdstilledvQKMKDKGEIAQAYIGLKETNRSSAMDCHELNEDG 1330
Cdd:pfam12128 726 AL---DAQLALLKAAIAARRSGAKAELKALETWYK-----------RDLASLGVDPDVIAKLKREIRTLERKIERIAVRR 791
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1331 ELLLVYEGLKQANRLLESQ-LQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNEN 1409
Cdd:pfam12128 792 QEVLRYFDWYQETWLQRRPrLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSK 871
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2015234411 1410 LYFEELYADDpkkyQSYRISLYKRMIDLMEQLEKQDKTVRKLKKQLKVF 1458
Cdd:pfam12128 872 LATLKEDANS----EQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHF 916
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
969-1098 |
3.52e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 969 ERLQLSE---EEAK-IATGRVLSLQEEIAKL---RKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKE--ENTLLKQEKE 1039
Cdd:PRK00409 495 KRLGLPEniiEEAKkLIGEDKEKLNELIASLeelERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEeeDKLLEEAEKE 574
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2015234411 1040 AlnHRIVEQAKEMTETMEKKLVEETKQLELDLNDerlryQNLLNEFSRLEERYDDLKEE 1098
Cdd:PRK00409 575 A--QQAIKEAKKEADEIIKELRQLQKGGYASVKA-----HELIEARKRLNKANEKKEKK 626
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
971-1104 |
4.08e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 971 LQLSEEEAK-IATGRVLSLQEEIAKLRKDLEQTRSEKKS-IEEHADRYKQETEQL---VSNLKEENTLLKQEKEALNHRI 1045
Cdd:PRK12704 44 LEEAKKEAEaIKKEALLEAKEEIHKLRNEFEKELRERRNeLQKLEKRLLQKEENLdrkLELLEKREEELEKKEKELEQKQ 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2015234411 1046 vEQAKEMTETMEKKLVEETKQLEldlnderlRYQNLLNEFSR---LEERYDDLKEEMTLMVN 1104
Cdd:PRK12704 124 -QELEKKEEELEELIEEQLQELE--------RISGLTAEEAKeilLEKVEEEARHEAAVLIK 176
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
907-1076 |
4.56e-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: 45.02 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 907 KLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDykclMEK-------LTNLEGTYNSETEKLRSDLERLQLSEEEAK 979
Cdd:pfam05701 273 KLKEEADGEGNEKKTSTSIQAALASAKKELEEVKAN----IEKakdevncLRVAAASLRSELEKEKAELASLRQREGMAS 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 980 IAtgrVLSLQEEIAKLRKDLEQTRS-EKKSIEEHADRYK------QETEQLVSNLKEENTLLKQEKEAlnhriVEQAKEM 1052
Cdd:pfam05701 349 IA---VSSLEAELNRTKSEIALVQAkEKEAREKMVELPKqlqqaaQEAEEAKSLAQAAREELRKAKEE-----AEQAKAA 420
|
170 180
....*....|....*....|....
gi 2015234411 1053 TETMEKKLVEETKQLELDLNDERL 1076
Cdd:pfam05701 421 ASTVESRLEAVLKEIEAAKASEKL 444
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
959-1098 |
4.69e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 959 SETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEK 1038
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2015234411 1039 EALNHRIVEQAKEMTEtmEKKLVEETKQLELDLndERLRYQNL--LNEFSRLEERYDDLKEE 1098
Cdd:COG1196 746 ELLEEEALEELPEPPD--LEELERELERLEREI--EALGPVNLlaIEEYEELEERYDFLSEQ 803
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
928-1047 |
5.31e-04 |
|
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: 43.03 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 928 KIMQLQrkVDEQNKDYKCLMEKLTNLEgTYNSETEKLRSDLERL-QLSEEEAKiatgrvlsLQEEIAKLRKDLEQTRSEK 1006
Cdd:pfam05266 57 KVKKLQ--VDDSRSVFESLMESFAELE-KHGFDVKAPQSRINKLlSLKDRQTK--------LLEELKKLEKKIAEEESEK 125
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2015234411 1007 KSIEEHADrykqETEQLVSNLKEENTLLKQEKEALNHRIVE 1047
Cdd:pfam05266 126 RKLEEEID----ELEKKILELERQLALAKEKKEAADKEIAR 162
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
960-1052 |
6.04e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 960 ETEKLRSDLERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKE 1039
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
90
....*....|...
gi 2015234411 1040 ALNHRIVEQAKEM 1052
Cdd:COG4942 231 RLEAEAAAAAERT 243
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
925-1072 |
7.73e-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: 43.85 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 925 MENKIMQLQRKVDEQNKDYKCLMEKLTNLEGTYNSETEK---LRSDLERL-QLSEEEAKIATGRVLSLQEEIAKLRKDLE 1000
Cdd:smart00787 142 LEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRkdaLEEELRQLkQLEDELEDCDPTELDRAKEKLKKLLQEIM 221
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2015234411 1001 QtrsEKKSIEEhadrYKQETEQLVSNLKEENTLLKQEKEALNH--RIVEQAKEMTETMEKKLVEETKQLELDLN 1072
Cdd:smart00787 222 I---KVKKLEE----LEEELQELESKIEDLTNKKSELNTEIAEaeKKLEQCRGFTFKEIEKLKEQLKLLQSLTG 288
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
931-1212 |
9.10e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 931 QLQRKVDEQNKDYKCLMEKLTNLEgtynSETEKLRSDLERLQlseEEAKIATGRVLSLQEEIAKLRKDLEQTRSEKKSIE 1010
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLE----EELEQARSELEQLE---EELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1011 EHADRYKQETEQlvsnLKEENTLLKQEKEALNHRIVEQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEE 1090
Cdd:COG4372 115 EELEELQKERQD----LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1091 RYDDLKEEMTLMVNVPKPGHKRTDSTHSSNESEYTFSSEIAETEDIPSRTEEPSEKKvpLDMSLFLKLQKRVTELEQEKQ 1170
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEED--KEELLEEVILKEIEELELAIL 268
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2015234411 1171 VMQDELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQELE 1212
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
988-1322 |
1.18e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 988 LQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKEentllkqekealnhrIVEQAKEMTETMeKKLVEETKQl 1067
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE---------------LREEAQELREKR-DELNEKVKE- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1068 eldLNDERlryQNLLNEFSRLEERYDDLKEEMtlmvnvpkpghkrtDSTHSSNESEYTFSSEIAETEDipsrteepsekk 1147
Cdd:COG1340 76 ---LKEER---DELNEKLNELREELDELRKEL--------------AELNKAGGSIDKLRKEIERLEW------------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1148 vpldmslflKLQKRVTELEQEKQVMqDELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQElesenKKLKNELNELRK 1227
Cdd:COG1340 124 ---------RQQTEVLSPEEEKELV-EKIKELEKELEKAKKALEKNEKLKELRAELKELRKEA-----EEIHKKIKELAE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1228 ALSEKSspevtapgapayrvlmEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKNTMTDstilledvQKMKDKGEIAQ 1307
Cdd:COG1340 189 EAQELH----------------EEMIELYKEADELRKEADELHKEIVEAQEKADELHEEII--------ELQKELRELRK 244
|
330
....*....|....*
gi 2015234411 1308 AYIGLKETNRSSAMD 1322
Cdd:COG1340 245 ELKKLRKKQRALKRE 259
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
962-1099 |
1.24e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 962 EKLRSDL-ERLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQlVSNLKE------ENTLL 1034
Cdd:COG1579 23 EHRLKELpAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-VRNNKEyealqkEIESL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2015234411 1035 KQEKEALNHRI------VEQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEM 1099
Cdd:COG1579 102 KRRISDLEDEIlelmerIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
925-1018 |
1.43e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 925 MENKIMQLQRKVDE---QNKDykcLMEKLTNLEgtynSETEKLRSDLERLQlSEEEAKIATGRVLS-LQEEIAKLRKDLE 1000
Cdd:COG2433 411 EEEEIRRLEEQVERleaEVEE---LEAELEEKD----ERIERLERELSEAR-SEERREIRKDREISrLDREIERLERELE 482
|
90
....*....|....*...
gi 2015234411 1001 QTRSEKKSIEEHADRYKQ 1018
Cdd:COG2433 483 EERERIEELKRKLERLKE 500
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
932-1224 |
1.62e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 932 LQRKVDEQNKDYKCLMEKLTNLegtyNSETEKLRS--DLERLQLSEEEAKIATGRVL--SLQEEIAKLRKDLEQTRSEKK 1007
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDEL----NEELKELAEkrDELNAQVKELREEAQELREKrdELNEKVKELKEERDELNEKLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1008 SIEEHADRYKQETEQLVSNLKEENTlLKQEKEALNHRIveQAKEMTETMEKKLVEETKQLELDLnDERLRYQNLLNEFSR 1087
Cdd:COG1340 89 ELREELDELRKELAELNKAGGSIDK-LRKEIERLEWRQ--QTEVLSPEEEKELVEKIKELEKEL-EKAKKALEKNEKLKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1088 LEERYDDLKEEMTlmvnvpkpghkrtdsthssneseyTFSSEIAET-EDIPSRTEEPSEKKVPLDmslflKLQKRVTELE 1166
Cdd:COG1340 165 LRAELKELRKEAE------------------------EIHKKIKELaEEAQELHEEMIELYKEAD-----ELRKEADELH 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2015234411 1167 QEKQVMQDELDRKEEQVLRSKAKEEE-RPQIRGAELEYESLKRQELESENKKLKNELNE 1224
Cdd:COG1340 216 KEIVEAQEKADELHEEIIELQKELRElRKELKKLRKKQRALKREKEKEELEEKAEEIFE 274
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
932-1091 |
1.81e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 932 LQRKVDEQNKDYKCLMEKLTNLEgtynSETEKLRSDLERLQlsEEEAKIATGRVLSLQEEIAKLRKDLEQtrsekksIEE 1011
Cdd:COG4913 293 LEAELEELRAELARLEAELERLE----ARLDALREELDELE--AQIRGNGGDRLEQLEREIERLERELEE-------RER 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1012 HADRYkqetEQLVSNLKEENTLLKQEKEALnHRIVEQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEER 1091
Cdd:COG4913 360 RRARL----EALLAALGLPLPASAEEFAAL-RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| Paralemmin |
pfam03285 |
Paralemmin; |
1160-1282 |
1.83e-03 |
|
Paralemmin;
Pssm-ID: 460875 Cd Length: 301 Bit Score: 42.42 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1160 KRVTELEQEKQvmQDELDRKEEQVLRSKAKEE----ERPQIRGAElEYESLKRQELESENKK--LKNELNELRKALSEKS 1233
Cdd:pfam03285 5 KRQTEIENKRR--QLEDDRRQLQHLKSKALRErwllEGPPSSASE-EDEARRRQEEEDEQKKklLEEIIRRLEEEIELLE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1234 SPEVtapgAPAYR-VLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQP 1282
Cdd:pfam03285 82 EESS----ISAKKeNLAEKLLEITVEKDKVTGETRVLSSTTLLPDDVQPQ 127
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
943-1100 |
1.86e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 42.36 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 943 YKCLMEKLTNLEGTYNSET-EKLRSDLerLQLSEEEAKIATGrvlsLQEEIAKLRKDL----EQTRSEKKSIEEHADRYK 1017
Cdd:cd22656 93 YAEILELIDDLADATDDEElEEAKKTI--KALLDDLLKEAKK----YQDKAAKVVDKLtdfeNQTEKDQTALETLEKALK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1018 QETEqlvsnlKEENTLLKQEKEALNHRIVEQAKEMTETMEKKLvEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKE 1097
Cdd:cd22656 167 DLLT------DEGGAIARKEIKDLQKELEKLNEEYAAKLKAKI-DELKALIADDEAKLAAALRLIADLTAADTDLDNLLA 239
|
...
gi 2015234411 1098 EMT 1100
Cdd:cd22656 240 LIG 242
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
765-786 |
1.90e-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: 1.90e-03
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
904-1069 |
1.91e-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: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 904 ELKKL--KIEARSVERYKKlHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGTYN---SETEKLRSDLERLQLSEEEa 978
Cdd:pfam15905 160 ELMKLrnKLEAKMKEVMAK-QEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIeekSETEKLLEYITELSCVSEQ- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 979 kiatgrVLSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEALnhriVEQAKEMTETMEK 1058
Cdd:pfam15905 238 ------VEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEEL----LREYEEKEQTLNA 307
|
170
....*....|.
gi 2015234411 1059 KLVEETKQLEL 1069
Cdd:pfam15905 308 ELEELKEKLTL 318
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
943-1085 |
2.18e-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: 42.18 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 943 YKCLMEKLTNLEGTYNSETEKLRSDLERLQL------SEEEAKIATGRVLSLQE-EIAKLRKDLEQTRSEKKSIEEHADR 1015
Cdd:cd16269 144 YQLYLEDREKLVEKYRQVPRKGVKAEEVLQEflqskeAEAEAILQADQALTEKEkEIEAERAKAEAAEQERKLLEEQQRE 223
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1016 YKQETEQLVSNLKEENTLLKQEKEAlnhRIVEQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEF 1085
Cdd:cd16269 224 LEQKLEDQERSYEEHLRQLKEKMEE---ERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSL 290
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
902-1090 |
2.38e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 902 KRELKKLKIEARSVER----YKKlhigmENKIMQLqrkvDEQNKDykcLMEKLTNLEGTYN---SETEKLRSDLERLQLS 974
Cdd:COG3206 181 EEQLPELRKELEEAEAaleeFRQ-----KNGLVDL----SEEAKL---LLQQLSELESQLAearAELAEAEARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 975 EEEAKIATGRVL------SLQEEIAKLRKDLEQTRSE-----------KKSIEEHADRYKQETEQLVSNLKEENTLLKQE 1037
Cdd:COG3206 249 LGSGPDALPELLqspviqQLRAQLAELEAELAELSARytpnhpdvialRAQIAALRAQLQQEAQRILASLEAELEALQAR 328
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2015234411 1038 KEALNHRIVEQAKEMTETMEKKLveETKQLELDLNDERLRYQNLLNefsRLEE 1090
Cdd:COG3206 329 EASLQAQLAQLEARLAELPELEA--ELRRLEREVEVARELYESLLQ---RLEE 376
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
969-1214 |
2.62e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 969 ERLQLSEEEAKIATGRvlsLQEEIAKLRKDLEQTrsekksiEEHADRYKQETEqlVSNLKEENTLLKQEKEALNHRIVE- 1047
Cdd:COG3206 164 QNLELRREEARKALEF---LEEQLPELRKELEEA-------EAALEEFRQKNG--LVDLSEEAKLLLQQLSELESQLAEa 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1048 -----QAKEMTETMEKKLVEETKQLELDLNDErlRYQNLLNEFSRLEERYDDLKEEMTlmvnvpkPGHKRTDSThssnes 1122
Cdd:COG3206 232 raelaEAEARLAALRAQLGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSARYT-------PNHPDVIAL------ 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1123 eytfSSEIAETED-IPSRTEEpsekkvpldmsLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEE----RPQIR 1197
Cdd:COG3206 297 ----RAQIAALRAqLQQEAQR-----------ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAElrrlEREVE 361
|
250
....*....|....*....
gi 2015234411 1198 GAELEYESL--KRQELESE 1214
Cdd:COG3206 362 VARELYESLlqRLEEARLA 380
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
998-1371 |
2.64e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 42.37 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 998 DLEQTRSEKksiEEHADRYkQETEQLVSNLKEENTLLKQEKEALNHRI--VEQAKEMTETMEKK----------LVEETK 1065
Cdd:pfam05622 1 DLSEAQEEK---DELAQRC-HELDQQVSLLQEEKNSLQQENKKLQERLdqLESGDDSGTPGGKKylllqkqleqLQEENF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1066 QLELDLNDERLRYQNLLNEFSRLEERYDDLkeemtlmvnvpkpghkrtdstHSSNESEYTFSSEI---AETEDIPSRTEE 1142
Cdd:pfam05622 77 RLETARDDYRIKCEELEKEVLELQHRNEEL---------------------TSLAEEAQALKDEMdilRESSDKVKKLEA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1143 PSE--KKVPLDMSlflKLQKRVTELEQEKQV-MQDELDRKEE----QVLRSKAkEEERPQIRG--AELEYESLKRQELES 1213
Cdd:pfam05622 136 TVEtyKKKLEDLG---DLRRQVKLLEERNAEyMQRTLQLEEElkkaNALRGQL-ETYKRQVQElhGKLSEESKKADKLEF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1214 ENKKLKNELNELRKalsEKsspevtapgapayrvlmEQLTSvseELDVRKEEVLILRSQLVSQKEAIQPKNTMTDSTILL 1293
Cdd:pfam05622 212 EYKKLEEKLEALQK---EK-----------------ERLII---ERDTLRETNEELRCAQLQQAELSQADALLSPSSDPG 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2015234411 1294 EDVQKMKDKGEIAQAYIGLKETNRssAMDCH-ELNEDGELLLVYEGLKQANRLLEsQLQSQKRSHENEAEALRGEIQSL 1371
Cdd:pfam05622 269 DNLAAEIMPAEIREKLIRLQHENK--MLRLGqEGSYRERLTELQQLLEDANRRKN-ELETQNRLANQRILELQQQVEEL 344
|
|
| CBD_MYO6-like |
cd21759 |
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ... |
767-794 |
2.81e-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: 40.18 E-value: 2.81e-03
10 20
....*....|....*....|....*...
gi 2015234411 767 RAACIRIQKTIRGWLLRKKYlRMRKAAI 794
Cdd:cd21759 45 REALIKIQKTVRGYLARKKH-RPRIKGL 71
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
862-883 |
3.11e-03 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 36.53 E-value: 3.11e-03
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
923-1099 |
3.39e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 923 IGMEN--KIMQLQRKVDEQNKDYKCLMEKLTNLEGTYNsETEKLRSDLERL-QLSEEEAKIAtgrvlSLQEEIAKLRKDL 999
Cdd:COG4913 604 LGFDNraKLAALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLaEYSWDEIDVA-----SAEREIAELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1000 EQTRSEKKSIEEHADRYKQETEQLVSnLKEENTLLKQEKEALNHRIvEQAKEMTETMEKKLVEETKQLELDLN---DERL 1076
Cdd:COG4913 678 ERLDASSDDLAALEEQLEELEAELEE-LEEELDELKGEIGRLEKEL-EQAEEELDELQDRLEAAEDLARLELRallEERF 755
|
170 180
....*....|....*....|....*..
gi 2015234411 1077 RY---QNLLNEFSR-LEERYDDLKEEM 1099
Cdd:COG4913 756 AAalgDAVERELREnLEERIDALRARL 782
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
954-1042 |
3.44e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 954 EGTYNSETEKLRSDLERLQLSEEEakiatgrvlSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKEENTL 1033
Cdd:PRK05771 188 ELSDEVEEELKKLGFERLELEEEG---------TPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEI 258
|
....*....
gi 2015234411 1034 LKQEKEALN 1042
Cdd:PRK05771 259 ELERAEALS 267
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
900-1281 |
3.68e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 900 MAKRELKKLKIEArSVERYKKLHIGMENKIMQLQRKVDEqnkdYKCLMEKLTNLEgtynseTEKLRSDLERLQlseeeak 979
Cdd:COG5185 217 SESTLLEKAKEII-NIEEALKGFQDPESELEDLAQTSDK----LEKLVEQNTDLR------LEKLGENAESSK------- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 980 iatgrvlSLQEEIAKLRKDLEQTrseKKSIEEhadrYKQETEQLVSNLKEENTLLKQEKEALnhriVEQAKEMTETMEKK 1059
Cdd:COG5185 279 -------RLNENANNLIKQFENT---KEKIAE----YTKSIDIKKATESLEEQLAAAEAEQE----LEESKRETETGIQN 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1060 LVEEtkqLELDLNDERLRYQNLLNEFSRL--EERYDDLKEEM-----TLMVNVPKPGHKRTDSTHSSNESEYTFSSEI-- 1130
Cdd:COG5185 341 LTAE---IEQGQESLTENLEAIKEEIENIvgEVELSKSSEELdsfkdTIESTKESLDEIPQNQRGYAQEILATLEDTLka 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1131 ---------AETEDIPSRTEEPSEKKVPLDMSlflkLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERpqirgael 1201
Cdd:COG5185 418 adrqieelqRQIEQATSSNEEVSKLLNELISE----LNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNE-------- 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1202 eyeslKRQELESENKKLKNELNELRKALSEKSSpevtapgaPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQ 1281
Cdd:COG5185 486 -----ELTQIESRVSTLKATLEKLRAKLERQLE--------GVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQ 552
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1039-1275 |
4.06e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1039 EALNHRIVEQAKEMTETMeKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMtlmvnvpkpghKRTDSTHS 1118
Cdd:pfam07888 30 ELLQNRLEECLQERAELL-QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEEL-----------RQSREKHE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1119 SNESEYT----FSSEIAETEDIPSRTEEPSEKKVpldmslfLKLQKRVTELEQEKQVMQDELDRKEEQVLRS----KAKE 1190
Cdd:pfam07888 98 ELEEKYKelsaSSEELSEEKDALLAQRAAHEARI-------RELEEDIKTLTQRVLERETELERMKERAKKAgaqrKEEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1191 EERPQIRgAELEYESLKRQELESENKKLKNELNE-------LRKALSEKSSPEVTAPGAPA-YRVLMEQLTSVSEELDVR 1262
Cdd:pfam07888 171 AERKQLQ-AKLQQTEEELRSLSKEFQELRNSLAQrdtqvlqLQDTITTLTQKLTTAHRKEAeNEALLEELRSLQERLNAS 249
|
250
....*....|...
gi 2015234411 1263 KEEVLILRSQLVS 1275
Cdd:pfam07888 250 ERKVEGLGEELSS 262
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
788-810 |
4.47e-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: 4.47e-03
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
987-1103 |
4.63e-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: 40.27 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 987 SLQEEIAKLRKDleqtrsekksiEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVEQAKEMTETMEKKlvEETKQ 1066
Cdd:pfam13851 30 SLKEEIAELKKK-----------EERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLK--ARLKV 96
|
90 100 110
....*....|....*....|....*....|....*..
gi 2015234411 1067 LELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMV 1103
Cdd:pfam13851 97 LEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAI 133
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
987-1472 |
4.73e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 987 SLQEEIAKLRK-----------DLEQTRSEKKSIEEHADRYKQETEQLvSNLKEENTLLKQEKEALNHRIveqakemtet 1055
Cdd:COG4717 50 RLEKEADELFKpqgrkpelnlkELKELEEELKEAEEKEEEYAELQEEL-EELEEELEELEAELEELREEL---------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1056 mekklveETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmvnvpkpghkrtdsthssneseytfssEIAEted 1135
Cdd:COG4717 119 -------EKLEKLLQLLPLYQELEALEAELAELPERLEELEERLE----------------------------ELRE--- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1136 ipsrteepsekkvpldmslflkLQKRVTELEQEKQVMQDELDRKEEQVlrskaKEEERPQIRGAELEYESL--KRQELES 1213
Cdd:COG4717 161 ----------------------LEEELEELEAELAELQEELEELLEQL-----SLATEEELQDLAEELEELqqRLAELEE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1214 ENKKLKNELNELRKALSEKSSPEVTA------------PGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQ 1281
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAaleerlkearllLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1282 PKNTmtdstillEDVQKMKDKGEIAQAYIGLKETNRSSAMDCHELNEDGELLLVYEGLKQANRLLESQLQSQKRSHENEA 1361
Cdd:COG4717 294 AREK--------ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1362 EALRGEIQSLKEENNrqqqllaqnlQLPPEARIEASLQH-EITRLTNENLYFEELYADDPKKYQSYRISLYKRmiDLMEQ 1440
Cdd:COG4717 366 EELEQEIAALLAEAG----------VEDEEELRAALEQAeEYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEE 433
|
490 500 510
....*....|....*....|....*....|....
gi 2015234411 1441 LEKQDKTVRKLKKQLKVFAKKIGEL--EVGQMEN 1472
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELeaELEQLEE 467
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
962-1098 |
5.44e-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: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 962 EKLRSDLER--------LQLSEEEAKIATGRVLSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQlvsnlkeentL 1033
Cdd:pfam05262 184 EALREDNEKgvnfrrdmTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQ----------K 253
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2015234411 1034 LKQEKEALNHRIVEQAKEMTETMEKKLVE-ETKQLELDLNDERLRYQNllnefsrlEERYDDLKEE 1098
Cdd:pfam05262 254 QQEAKNLPKPADTSSPKEDKQVAENQKREiEKAQIEIKKNDEEALKAK--------DHKAFDLKQE 311
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
937-1212 |
5.53e-03 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 41.65 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 937 DEQNKDYKCLMEKLT-NLEGTYNSETEKLRSDLErLQLSEEEAKIATGRVLSLQEEIAKLRKDLEQ------TRSEKKSI 1009
Cdd:COG5192 438 SDENEDVDFTGKKGAiNNEDESDNEEVAFDSDSQ-FDESEGNLRWKEGLASKLAYSQSGKRGRNIQkifydeSLSPEECI 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1010 EEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVEQAKEMTETMEkKLVEETKQleLDLNDERLRYQNLLNEFSRLE 1089
Cdd:COG5192 517 EEYKGESAKSSESDLVVQDEPEDFFDVSKVANESISSNHEKLMESEFE-ELKKKWSS--LAQLKSRFQKDATLDSIEGEE 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1090 ERYDDLkEEMTLMVNVPKPGHKRTDSTHSSNESEYTFSSEIAETEDIPSRTEEPSEKKVPLDMSLflklqkrvtELEQEK 1169
Cdd:COG5192 594 ELIQDD-EKGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVDYETEREENARKKEELRGNF---------ELEERG 663
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2015234411 1170 QVMQDELDRKEEQvlrsKAKEEErpQIRGAELEYESL---KRQELE 1212
Cdd:COG5192 664 DPEKKDVDWYTEE----KRKIEE--QLKINRSEFETMvpeSRVVIE 703
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
968-1316 |
5.83e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.55 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 968 LERLQLSEEEAKiatgrvlSLQEEIAKLRKDLEQTRSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEALnhrivE 1047
Cdd:pfam05701 34 VERRKLVELELE-------KVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQDS-----E 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1048 QAKEMTETMEKKLVEETK-----QLELdlndERLRYQNLLNEFSRLEERYDDLKEEMTLMVNVPKPGHKRT-DSTHSSNE 1121
Cdd:pfam05701 102 LAKLRVEEMEQGIADEASvaakaQLEV----AKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAeEAVSASKE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1122 SEYTFssEIAETEDIPSRTE---------EPSEKKVPLDMSL---FLKLQKrvtELEQekqvMQDELDRKEEQVLRSKAK 1189
Cdd:pfam05701 178 IEKTV--EELTIELIATKESlesahaahlEAEEHRIGAALAReqdKLNWEK---ELKQ----AEEELQRLNQQLLSAKDL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1190 EeerpqirgAELEYESLKRQELESE-NKKLKNELNELRKALSEKSSPEVTAPGApayrvlmeqLTSVSEEL-DVR----- 1262
Cdd:pfam05701 249 K--------SKLETASALLLDLKAElAAYMESKLKEEADGEGNEKKTSTSIQAA---------LASAKKELeEVKaniek 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2015234411 1263 -KEEVLI-------LRSQLVSQKE---AIQPKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETN 1316
Cdd:pfam05701 312 aKDEVNClrvaaasLRSELEKEKAelaSLRQREGMASIAVSSLEAELNRTKSEIALVQAKEKEAR 376
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
932-1214 |
5.89e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 41.24 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 932 LQRKVDEQNKDYKCLMEKLTNLEGTYNSEteklRSDLERLQLS-EEEAKIATGRVLSLQEEIAKLRKDLEQTRSEKKSIE 1010
Cdd:pfam03528 6 LQQRVAELEKENAEFYRLKQQLEAEFNQK----RAKFKELYLAkEEDLKRQNAVLQEAQVELDALQNQLALARAEMENIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1011 EHA---DRYKQET-EQLVSNLKEENTLLK-------QEKEALNHRIVEQAK----EMTETMEKKLVEETKQLEldlndER 1075
Cdd:pfam03528 82 AVAtvsENTKQEAiDEVKSQWQEEVASLQaimketvREYEVQFHRRLEQERaqwnQYRESAEREIADLRRRLS-----EG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1076 LRYQNLLNEFSRLEERYDDLKE-EMTLMVNVPKPGHKRTDSTHSSNESEYTFSSEIAETEDipsrteepSEKKVPLDMSL 1154
Cdd:pfam03528 157 QEEENLEDEMKKAQEDAEKLRSvVMPMEKEIAALKAKLTEAEDKIKELEASKMKELNHYLE--------AEKSCRTDLEM 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2015234411 1155 FlklqkrVTELEQEKQVMQDELD--RKEEQVLRSKAkEEERPQIRGAELEYESLKRQELESE 1214
Cdd:pfam03528 229 Y------VAVLNTQKSVLQEDAEklRKELHEVCHLL-EQERQQHNQLKHTWQKANDQFLESQ 283
|
|
| CBD_MYO6-like |
cd21759 |
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ... |
810-835 |
6.17e-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: 6.17e-03
10 20
....*....|....*....|....*.
gi 2015234411 810 KFLRRTKAATIIQKYWRMYVARRRYK 835
Cdd:cd21759 40 KILYRREALIKIQKTVRGYLARKKHR 65
|
|
| CBD_MYO6-like |
cd21759 |
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ... |
859-972 |
6.40e-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: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 859 KIL-REHKAVIIQKWVRGWLARTYYRRSIHAIIYLqccfrRMMAKReLKKLKieaRSVERYKKLHIGMENKIMQLQRKVD 937
Cdd:cd21759 40 KILyRREALIKIQKTVRGYLARKKHRPRIKGLRKI-----RALEKQ-LKEME---EIASQLKKDKDKWTKQVKELKKEID 110
|
90 100 110
....*....|....*....|....*....|....*.
gi 2015234411 938 EQNKDYKCL-MEKLTNLEGTYNSETEKLRSDLERLQ 972
Cdd:cd21759 111 ALIKKIKTNdMITRKEIDKLYNALVKKVDKQLAELQ 146
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
901-1087 |
6.56e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 41.28 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 901 AKRELKKLKIEARSVERYKKL-HIGMENKIMQLQRKVDE----QNKDYKCLMEKLTNLEGTYNSETEKLRSDLERLQLSE 975
Cdd:pfam09731 231 VEEKVEKAQSLAKLVDQYKELvASERIVFQQELVSIFPDiipvLKEDNLLSNDDLNSLIAHAHREIDQLSKKLAELKKRE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 976 EEAkiatgrvlsLQEEIAKLRKDLEQTRSE-KKSIEEHADRYKQETEqlvsnlkeentlLKQEKEalnhrIVEQAKEMTE 1054
Cdd:pfam09731 311 EKH---------IERALEKQKEELDKLAEElSARLEEVRAADEAQLR------------LEFERE-----REEIRESYEE 364
|
170 180 190
....*....|....*....|....*....|....
gi 2015234411 1055 TMEKKLVEETKQLELDLNDE-RLRYQNLLNEFSR 1087
Cdd:pfam09731 365 KLRTELERQAEAHEEHLKDVlVEQEIELQREFLQ 398
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
925-1226 |
6.66e-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: 41.38 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 925 MENKIMQLQRKVDEQNKDYKCLM----EKLTNLEGTYNseteklrsdlerlQLSEEEAKIATgrvLSLQEEIAKLRKDLE 1000
Cdd:pfam06160 184 LEEETDALEELMEDIPPLYEELKtelpDQLEELKEGYR-------------EMEEEGYALEH---LNVDKEIQQLEEQLE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1001 QTRSEKKSIEehadryKQETEQLVSNLKEE-NTLLKQ-EKEALNHRIVEQAKEMTETMEKKLVEETKQLELDL------- 1071
Cdd:pfam06160 248 ENLALLENLE------LDEAEEALEEIEERiDQLYDLlEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELervqqsy 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1072 ---NDERLRYQNLLNEFSRLEERYDDLKEEMTlmvnvpkpghkrtdsthssnESEYTFSSEIAETEDIPSRTEEPSEKKV 1148
Cdd:pfam06160 322 tlnENELERVRGLEKQLEELEKRYDEIVERLE--------------------EKEVAYSELQEELEEILEQLEEIEEEQE 381
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2015234411 1149 pldmslflKLQKRVTELEQEKQVMQDELDRKEEQVLRSKaKEEERPQIRGAELEYESLKRqELESENKKLKNELNELR 1226
Cdd:pfam06160 382 --------EFKESLQSLRKDELEAREKLDEFKLELREIK-RLVEKSNLPGLPESYLDYFF-DVSDEIEDLADELNEVP 449
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
904-1277 |
7.28e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 904 ELKKLKIEARSVE--------RYKKLhigmENKIMQLQRKVDEQNKDYKCLMEKLTNLEGTYNS------ETE----KLR 965
Cdd:pfam01576 385 ENAELQAELRTLQqakqdsehKRKKL----EGQLQELQARLSESERQRAELAEKLSKLQSELESvssllnEAEgkniKLS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 966 SDLERL---------QLSEE-EAKIA-TGRVLSLQEEIAKLRKDLEQTRSEKKSIEEHAdrykQETEQLVSNLKEentll 1034
Cdd:pfam01576 461 KDVSSLesqlqdtqeLLQEEtRQKLNlSTRLRQLEDERNSLQEQLEEEEEAKRNVERQL----STLQAQLSDMKK----- 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1035 KQEKEALNHRIVEQAKemtetmeKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDD----LKEEMTLMVNVPKPgH 1110
Cdd:pfam01576 532 KLEEDAGTLEALEEGK-------KRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDllvdLDHQRQLVSNLEKK-Q 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1111 KRTDSTHSsneSEYTFSSEIAETEDipsRTEEPSEKKVPLDMSLFLKL---QKRVTELEQEKQVMQDELdrkeEQVLRSK 1187
Cdd:pfam01576 604 KKFDQMLA---EEKAISARYAEERD---RAEAEAREKETRALSLARALeeaLEAKEELERTNKQLRAEM----EDLVSSK 673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1188 ------AKEEERPQiRGAELEYESLKRQ--ELE-----SENKKLKNELN-ELRKALSEKSSPEVTAPGAPAYRVLMEQLT 1253
Cdd:pfam01576 674 ddvgknVHELERSK-RALEQQVEEMKTQleELEdelqaTEDAKLRLEVNmQALKAQFERDLQARDEQGEEKRRQLVKQVR 752
|
410 420
....*....|....*....|....*
gi 2015234411 1254 SVSEEL-DVRKEevlilRSQLVSQK 1277
Cdd:pfam01576 753 ELEAELeDERKQ-----RAQAVAAK 772
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
959-1097 |
7.60e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 38.39 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 959 SETEKLRSDLERLQLSEEEAkiatgrvlslQEEIAKLRKDLEQTRSEKKSIEEhadRYKQE------TEQLVSNLKEENT 1032
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADA----------EAQLQKLQEDLEKQAEIAREAQQ---NYERElvlhaeDIKALQALREELN 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2015234411 1033 LLKQEKEALNHRiVEQAKEMTETMEKKLVEETKQLEldlnderlryqnllNEFSRLEERYDDLKE 1097
Cdd:pfam07926 68 ELKAEIAELKAE-AESAKAELEESEESWEEQKKELE--------------KELSELEKRIEDLNE 117
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
902-1226 |
7.61e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 902 KRELKKLK-IEARSVERYKKLhigmENKIMQLQRKVDEQNKDY----KCLMEKLTNLEGTYnSETEKLRSDLERLQLSE- 975
Cdd:PRK04778 125 LEELQELLeSEEKNREEVEQL----KDLYRELRKSLLANRFSFgpalDELEKQLENLEEEF-SQFVELTESGDYVEAREi 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 976 -EEAKIATGRVLSLQEEIAKLRKDLEQT--------------------RSEKKSIEEHADRYKQETEQLVSNL------- 1027
Cdd:PRK04778 200 lDQLEEELAALEQIMEEIPELLKELQTElpdqlqelkagyrelveegyHLDHLDIEKEIQDLKEQIDENLALLeeldlde 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1028 -KEENTLLKQ---------EKEALNHRIVEQAKEMTETMEKKLVEETKQLELDL----------NDERLRYQNLLNEFSR 1087
Cdd:PRK04778 280 aEEKNEEIQEridqlydilEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIdrvkqsytlnESELESVRQLEKQLES 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1088 LEERYDDLKEEMTlmvnvpkpghkrtdsthssnESEYTFSSEIAETEDIPSRTEEPSEKKVpldmslflKLQKRVTELEQ 1167
Cdd:PRK04778 360 LEKQYDEITERIA--------------------EQEIAYSELQEELEEILKQLEEIEKEQE--------KLSEMLQGLRK 411
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2015234411 1168 EKQVMQDELDRKEEQVLRSKAKEEER-----PQirgaelEYESLKrQELESENKKLKNELNELR 1226
Cdd:PRK04778 412 DELEAREKLERYRNKLHEIKRYLEKSnlpglPE------DYLEMF-FEVSDEIEALAEELEEKP 468
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
910-1219 |
8.07e-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: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 910 IEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKC-LMEKLTNLEGTYNSETEKLRS---DLERLQLSEEEAKIATGRV 985
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACeIRDQITSKEAQLESSREIVKSyenELDPLKNRLKEIEHNLSKI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 986 LSLQEEIA----------KLRKDLEQ--------TRSEKKSIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVE 1047
Cdd:TIGR00606 265 MKLDNEIKalksrkkqmeKDNSELELkmekvfqgTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1048 QAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFsrleERYDDLKEEMTLMVNVPKPGHKRTDSTHSSNESEYTFS 1127
Cdd:TIGR00606 345 LLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGF----ERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSK 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015234411 1128 SEIAETEdipsrTEEPSEKKVPLDMSLFLK---LQKRVTELEQEKQVMQ------DELDRKEEQVLRSKA---KEEERPQ 1195
Cdd:TIGR00606 421 ERLKQEQ-----ADEIRDEKKGLGRTIELKkeiLEKKQEELKFVIKELQqlegssDRILELDQELRKAERelsKAEKNSL 495
|
330 340
....*....|....*....|....
gi 2015234411 1196 IRGAELEYESLKRQELESENKKLK 1219
Cdd:TIGR00606 496 TETLKKEVKSLQNEKADLDRKLRK 519
|
|
| IQ |
pfam00612 |
IQ calmodulin-binding motif; Calmodulin-binding motif. |
840-858 |
8.95e-03 |
|
IQ calmodulin-binding motif; Calmodulin-binding motif.
Pssm-ID: 459869 Cd Length: 21 Bit Score: 35.37 E-value: 8.95e-03
|
| |
