|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
81-741 |
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: 1203.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFAESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01380 1 PAVLHNLKVRFCQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 161 GESGAGKTVSARYAMRYFATVSKSGSN-AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMST 239
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATVGGSSSGeTQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDF 319
Cdd:cd01380 161 YLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 320 QMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARD 399
Cdd:cd01380 241 QMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 400 ALAKKIYAHLFDFIVERINQALQF--SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 477
Cdd:cd01380 321 ALAKHIYAQLFDWIVDRINKALASpvKEKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNR-NPLFEKPRMSNTSFVIQHFADKVE 556
Cdd:cd01380 401 EEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTAFIVKHFADDVE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 557 YKCEGFLEKNRDTVYDMLVEILRASKFHlcanffqenptppspfgsmitvksakqviKPnskhfrtTVGSKFRSSLYLLM 636
Cdd:cd01380 481 YQVEGFLEKNRDTVSEEHLNVLKASKNR-----------------------------KK-------TVGSQFRDSLILLM 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 637 ETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKEV 716
Cdd:cd01380 525 ETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRDDKKKT 604
|
650 660
....*....|....*....|....*
gi 294862453 717 CKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd01380 605 CENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
62-752 |
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: 962.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 62 NPDILVGENDLTALSYLHEPAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVA 141
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRY-LKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 142 EEAYKQMARNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSGSNA-HVEDKVLASNPITEAVGNAKTTRNDNSSRFGK 220
Cdd:smart00242 80 DNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVgSVEDQILESNPILEAFGNAKTLRNNNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 221 YTEISFDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDR 300
Cdd:smart00242 160 FIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 301 AEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNE-RSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIV 379
Cdd:smart00242 240 EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDnAASTVKDKEELSNAAELLGVDPEELEKALTKRKIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 380 TSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKL 459
Cdd:smart00242 320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 460 QQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNRNPLFEK 538
Cdd:smart00242 400 QQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKpPGILSLLDEECRFPKGTDQTFLEKLNQHH-KKHPHFSK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 539 P-RMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQEnptppspfgsmitvksakQVIKPNS 617
Cdd:smart00242 479 PkKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS------------------GVSNAGS 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 618 KHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYS 697
Cdd:smart00242 541 KKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQ 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 294862453 698 RYGILMTKQELSFS-DKKEVCKVVLHRLIQDSNQYQFGKTKIFFRAGQVAYLEKLR 752
Cdd:smart00242 621 RYRVLLPDTWPPWGgDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
70-741 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 915.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 70 NDLTALSYLHEPAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMA 149
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYK-SDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 150 RNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSGSN---AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISF 226
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAgnvGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 227 DEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVET 306
Cdd:pfam00063 161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 307 QKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVV 386
Cdd:pfam00063 241 DKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETVS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 387 KPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQF-SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNM 465
Cdd:pfam00063 321 KPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVkTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 466 HVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNRNPLFEKPR-MSN 543
Cdd:pfam00063 401 HMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKpLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHFQKPRlQGE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 544 TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQEnptpPSPFGSMITVKSAKQVIKPNSKHFRTT 623
Cdd:pfam00063 480 THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPD----YETAESAAANESGKSTPKRTKKKRFIT 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 624 VGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILM 703
Cdd:pfam00063 556 VGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILA 635
|
650 660 670
....*....|....*....|....*....|....*....
gi 294862453 704 TK-QELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:pfam00063 636 PKtWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
12-1324 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 894.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 12 RVWIPDPEEVWKSAEIAK-DYRVGDKVLRLLLEDGtELDySVNPESLPPLR-NPDILVGENDLTALSYLHEPAVLHNLRI 89
Cdd:COG5022 11 GCWIPDEEKGWIWAEIIKeAFNKGKVTEEGKKEDG-ESV-SVKKKVLGNDRiKLPKFDGVDDLTELSYLNEPAVLHNLEK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 90 RFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTV 169
Cdd:COG5022 89 RY-NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 170 SARYAMRYFATVSKSGSN--AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYLLEKSRV 247
Cdd:COG5022 168 NAKRIMQYLASVTSSSTVeiSSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 248 VFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKIL 327
Cdd:COG5022 248 VHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKIL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 328 AAILHLGNVQITAVGNERSSVSeDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYA 407
Cdd:COG5022 328 AAILHIGNIEFKEDRNGAAIFS-DNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYS 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 408 HLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDF 487
Cdd:COG5022 407 NLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 488 YDNQPVIDLIEAK--MGILELLDEECLLPHGTDENWLQKLYNNF-VNRNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLE 564
Cdd:COG5022 487 FDNQPCIDLIEKKnpLGILSLLDEECVMPHATDESFTSKLAQRLnKNSNPKFKKSRFRDNKFVVKHYAGDVEYDVEGFLD 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 565 KNRDTVYDMLVEILRASKFHLCANFFQENptppspfgsmitvksakqvIKPNSKHFRTTVGSKFRSSLYLLMETLNATTP 644
Cdd:COG5022 567 KNKDPLNDDLLELLKASTNEFVSTLFDDE-------------------ENIESKGRFPTLGSRFKESLNSLMSTLNSTQP 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 645 HYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILM-----TKQELSFSDKKEVCKV 719
Cdd:COG5022 628 HYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSpskswTGEYTWKEDTKNAVKS 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 720 VLHRLIQDSNQYQFGKTKIFFRAGQVAYLEKLRLDKLRQSCVMVQKHMRGWLQRKKFLRERRaaliIQQYFRGQQTVRKA 799
Cdd:COG5022 708 ILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALK----RIKKIQVIQHGFRL 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 800 ITAVAlKEAW--AAIIIQKHCRGYLVRSlYQLIRMATITMQAYS--RGFLARRRYRKMLEEHKAVILQKYARAWLARRRF 875
Cdd:COG5022 784 RRLVD-YELKwrLFIKLQPLLSLLGSRK-EYRSYLACIIKLQKTikREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRF 861
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 876 QSIRRFVLNIQLTYRVQRLQKKLEDQNKEnhglVEKLTSLAALRAGDVEKIQKLEAELEKaaTHRRNYEEKgkryrdavE 955
Cdd:COG5022 862 SLLKKETIYLQSAQRVELAERQLQELKID----VKSISSLKLVNLELESEIIELKKSLSS--DLIENLEFK--------T 927
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 956 EKLAKLQKHN--------SELETQKEQIQLKLQEKTEELKE---KMDNLTKQLfdDVQKEERQRMLLE-KSFELKTQDYE 1023
Cdd:COG5022 928 ELIARLKKLLnnidleegPSIEYVKLPELNKLHEVESKLKEtseEYEDLLKKS--TILVREGNKANSElKNFKKELAELS 1005
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1024 KQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDgLKAEVARLSKQVKTISEFEKEIELLQAQKIDVekhvqSQKREMREKM 1103
Cdd:COG5022 1006 KQYGALQESTKQLKELPVEVAELQSASKIISS-ESTELSILKPLQKLKGLLLLENNQLQARYKAL-----KLRRENSLLD 1079
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1104 SeitkqlLESYDIEDVRSRLSVedlehLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHL 1183
Cdd:COG5022 1080 D------KQLYQLESTENLLKT-----INVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQK 1148
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1184 QKLFREENDINESIRHEVTRLTsenmmIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKA 1263
Cdd:COG5022 1149 LSVLQLELDGLFWEANLEALPS-----PPPFAALSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFSGWPRGDKL 1223
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 294862453 1264 LEAQNEIHTKEKEKlidkiQEMQEASDHLKKQFETESEVKCNFRQEASRL--TLENRDLEEEL 1324
Cdd:COG5022 1224 KKLISEGWVPTEYS-----TSLKGFNNLNKKFDTPASMSNEKLLSLLNSIdnLLSSYKLEEEV 1281
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
81-741 |
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: 826.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMG-DMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd00124 1 AAILHNLRERYARDL-IYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 160 SGESGAGKTVSARYAMRYFATVSKSGSNAH------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQII 233
Cdd:cd00124 80 SGESGAGKTETTKLVLKYLAALSGSGSSKSsssassIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 234 GANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEE----FNYTRMGGNTVIEGVNDRAEMVETQKT 309
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSyyylNDYLNSSGCDRIDGVDDAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 310 FTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNE--RSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVK 387
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 388 PMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQH--TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNM 465
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 466 HVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSNT 544
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKpLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAKL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 545 SFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAskfhlcanffqenptppspfgsmitvksakqvikpnskhfrttv 624
Cdd:cd00124 480 EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS-------------------------------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 625 GSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMT 704
Cdd:cd00124 516 GSQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAP 595
|
650 660 670
....*....|....*....|....*....|....*...
gi 294862453 705 K-QELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd00124 596 GaTEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
81-741 |
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: 750.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01377 1 ASVLHNLRERY-YSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 161 GESGAGKTVSARYAMRYFATVSKSGSNAH--------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQI 232
Cdd:cd01377 80 GESGAGKTENTKKVIQYLASVAASSKKKKesgkkkgtLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 233 IGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTL 312
Cdd:cd01377 160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 313 LGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 393 QAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQ 472
Cdd:cd01377 320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 473 EEYMKEDIPWTLIDF-YDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMS--NTSFVI 548
Cdd:cd01377 400 EEYKKEGIEWTFIDFgLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKPKksEAHFIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 549 QHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFqENPTPPSPFGSMITVKSAKqvikpnskhFRtTVGSKF 628
Cdd:cd01377 480 KHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLF-KDYEESGGGGGKKKKKGGS---------FR-TVSQLH 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 629 RSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILM-TKQE 707
Cdd:cd01377 549 KEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILApNAIP 628
|
650 660 670
....*....|....*....|....*....|....
gi 294862453 708 LSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd01377 629 KGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
81-741 |
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: 705.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd01384 1 PGVLHNLKVRY-ELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 160 SGESGAGKTVSARYAMRYFATVSK--SGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANM 237
Cdd:cd01384 80 SGESGAGKTETTKMLMQYLAYMGGraVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 238 STYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKE 317
Cdd:cd01384 160 RTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 318 DFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDS---HLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd01384 240 EEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKsefHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 395 VNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEE 474
Cdd:cd01384 320 TLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 475 YMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFVNrNPLFEKPRMSNTSFVIQHFAD 553
Cdd:cd01384 400 YTKEEIDWSYIEFVDNQDVLDLIEKKPgGIIALLDEACMFPRSTHETFAQKLYQTLKD-HKRFSKPKLSRTDFTIDHYAG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 554 KVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFqenptPPSPFGSmiTVKSAKqvikpnskhFrTTVGSKFRSSLY 633
Cdd:cd01384 479 DVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLF-----PPLPREG--TSSSSK---------F-SSIGSRFKQQLQ 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 634 LLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDK 713
Cdd:cd01384 542 ELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLKGSDDE 621
|
650 660
....*....|....*....|....*...
gi 294862453 714 KEVCKVVLHRLiqDSNQYQFGKTKIFFR 741
Cdd:cd01384 622 KAACKKILEKA--GLKGYQIGKTKVFLR 647
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
81-741 |
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: 687.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDmdPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01383 1 PSVLHNLEYRY-SQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKLLDS--PHVYAVADTAYREMMRDEINQSIIIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 161 GESGAGKTVSARYAMRYFATVSkSGSNAhVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTY 240
Cdd:cd01383 78 GESGAGKTETAKIAMQYLAALG-GGSSG-IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 241 LLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQ 320
Cdd:cd01383 156 LLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKEDQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 321 MDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDA 400
Cdd:cd01383 236 EHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 401 LAKKIYAHLFDFIVERINQALQFSGKQH-TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKED 479
Cdd:cd01383 316 LAKAIYASLFDWLVEQINKSLEVGKRRTgRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 480 IPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLyNNFVNRNPLFEKPRmsNTSFVIQHFADKVEYK 558
Cdd:cd01383 396 IDWTKVDFEDNQECLDLIEKKpLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCFKGER--GGAFTIRHYAGEVTYD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 559 CEGFLEKNRDTVYDMLVEILRASKFHLcanffqenptpPSPFGSMITVKSAKQ--VIKPNSKHF-RTTVGSKFRSSLYLL 635
Cdd:cd01383 473 TSGFLEKNRDLLHSDLIQLLSSCSCQL-----------PQLFASKMLDASRKAlpLTKASGSDSqKQSVATKFKGQLFKL 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 636 METLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKE 715
Cdd:cd01383 542 MQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDPLS 621
|
650 660
....*....|....*....|....*.
gi 294862453 716 VCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd01383 622 TSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
82-741 |
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: 683.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd01378 2 AINENLKKRF-ENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 162 ESGAGKTVSARYAMRYFATVSKSGSN--AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMST 239
Cdd:cd01378 81 ESGAGKTEASKRIMQYIAAVSGGSESevERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDF 319
Cdd:cd01378 161 YLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 320 QMDVFKILAAILHLGNVQITAVGNERSSVSeDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSE---TVVKPMTRPQAVN 396
Cdd:cd01378 241 QDSIFRILAAILHLGNIQFAEDEEGNAAIS-DTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGgrsVYEVPLNVEQAAY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 397 ARDALAKKIYAHLFDFIVERINQALQFSGKQH-TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEY 475
Cdd:cd01378 320 ARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEEY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 476 MKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPH-GTDENWLQKLyNNFVNRNPLFEKP----RMSNTSFVIQ 549
Cdd:cd01378 400 VREGIEWTPIKYFNNKIICDLIEEKpPGIFAILDDACLTAGdATDQTFLQKL-NQLFSNHPHFECPsghfELRRGEFRIK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 550 HFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPtppspfgsmitvksakqviKPNSKHFRTTVGSKFR 629
Cdd:cd01378 479 HYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGV-------------------DLDSKKRPPTAGTKFK 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 630 SSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELS 709
Cdd:cd01378 540 NSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPA 619
|
650 660 670
....*....|....*....|....*....|...
gi 294862453 710 FS-DKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd01378 620 WDgTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| Myo5c_CBD |
cd15476 |
Cargo binding domain of myosin 5C; Class V myosins are well studied unconventional myosins, ... |
1369-1736 |
0e+00 |
|
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: 680.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1369 EDEAKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSNT 1448
Cdd:cd15476 1 EDEAKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRHADYLNDANKLKSLMNAIITGVKQVIKEHQEDFEMLSFWLSNT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1449 CHFLNCLKQYSGEEEFMKHNSPQQNKNCLNNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPiivpgmleyeslqgisgl 1528
Cdd:cd15476 81 YHFLNCLKQYSGEEEFMKHNTPRQNKNCLKNFDLSEHRQILSDLAIRIYHQFISVMENNLQP------------------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1529 kptgfrkrsssiddtdgyTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRC 1608
Cdd:cd15476 143 ------------------TISSILQQLSYFYSTMCQHGMDPELIKQAVKQLFFLIGAVTLNSIFLRKDMCSCRKGMQIRC 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1609 NISYLEEWLKDKNLQNSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPIDDFEKRVTPSFV 1688
Cdd:cd15476 205 NISYLEEWLKEKNLQNSNAKETLEPLSQAAWLLQVNKTTDDDAKEICERCTELSAVQIVKILNSYTPIDDFEKRVTPSFV 284
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 294862453 1689 RKVQALLNSREDSSQLMLDTKYLFQVTFPFTPSPHALEMIQIPSSFKL 1736
Cdd:cd15476 285 RKVQSLLQNREGSSQLMLDTKYRFQVTFPFCPSPQALEMLQVPSSLKL 332
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
82-741 |
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: 678.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 82 AVLHNLRIRFAEsKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd01381 2 GILRNLLIRYRE-KLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 162 ESGAGKTVSARYAMRYFATVSksGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYL 241
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAIS--GQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 242 LEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQM 321
Cdd:cd01381 159 LEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 322 DVFKILAAILHLGNVQITA--VGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARD 399
Cdd:cd01381 239 DIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 400 ALAKKIYAHLFDFIVERINQAL-QFSGKQH--TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYM 476
Cdd:cd01381 319 AFVKGIYGRLFIWIVNKINSAIyKPRGTDSsrTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEYD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 477 KEDIPWTLIDFYDNQPVIDLI-EAKMGILELLDEECLLPHGTDENWLQKLYNNFVNrNPLFEKPRM-SNTSFVIQHFADK 554
Cdd:cd01381 399 KEGINWQHIEFVDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGN-NKNYLKPKSdLNTSFGINHFAGV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 555 VEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENptppSPFGSmitvKSAKQVIkpnskhfrtTVGSKFRSSLYL 634
Cdd:cd01381 478 VFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNED----ISMGS----ETRKKSP---------TLSSQFRKSLDQ 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 635 LMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGIL------MTKQEL 708
Cdd:cd01381 541 LMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLvpgippAHKTDC 620
|
650 660 670
....*....|....*....|....*....|...
gi 294862453 709 SFSDKKEVCKVVLHrliqDSNqYQFGKTKIFFR 741
Cdd:cd01381 621 RAATRKICCAVLGG----DAD-YQLGKTKIFLK 648
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
82-741 |
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: 650.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14883 2 GINTNLKVRYK-KDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 162 ESGAGKTVSARYAMRYFATVSKSGSnaHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYL 241
Cdd:cd14883 81 ESGAGKTETTKLILQYLCAVTNNHS--WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 242 LEKSRVVFQSENERNYHIFYQLCASAQQS-EFKH-LKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDF 319
Cdd:cd14883 159 LEQSRITFQAPGERNYHVFYQLLAGAKHSkELKEkLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPEEM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 320 QMDVFKILAAILHLGNVQITAVGNERSSVSEDDSH-LKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNAR 398
Cdd:cd14883 239 QEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEiLKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 399 DALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKE 478
Cdd:cd14883 319 DAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 479 DIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNRNPLFEKP--RMSNTSFVIQHFADKV 555
Cdd:cd14883 399 GINWSHIVFTDNQECLDLIEKPpLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPdrRRWKTEFGVKHYAGEV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 556 EYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFF--QENPTPPSPFGSMITVKSAKQvikpnSKHFRTTVGSKFRSSLY 633
Cdd:cd14883 478 TYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtyPDLLALTGLSISLGGDTTSRG-----TSKGKPTVGDTFKHQLQ 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 634 LLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTK-QELSFSD 712
Cdd:cd14883 553 SLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRaRSADHKE 632
|
650 660
....*....|....*....|....*....
gi 294862453 713 KKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14883 633 TCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
81-741 |
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: 612.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14872 1 AMIVHNLRKRFKNDQ-IYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 161 GESGAGKTVSARYAMRYFATVSksGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTY 240
Cdd:cd14872 80 GESGAGKTEATKQCLSFFAEVA--GSTNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 241 LLEKSRVVFQSENERNYHIFYQLCASAQQSefKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQ 320
Cdd:cd14872 158 LLEKSRVVYQIKGERNFHIFYQLLASPDPA--SRGGWGSSAAYGYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFDDADI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 321 MDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCE---LLGLESGRVAQWLCNRKI-VTSSETVVKPMTRPQAVN 396
Cdd:cd14872 236 NNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSRLMeIKGCDPTRIPLTPAQATD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 397 ARDALAKKIYAHLFDFIVERINQAL-QFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEY 475
Cdd:cd14872 316 ACDALAKAAYSRLFDWLVKKINESMrPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEALY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 476 MKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNF-VNRNPLFEKPRMSNTSFVIQHFAD 553
Cdd:cd14872 396 QSEGVKFEHIDFIDNQPVLDLIEKKQpGLMLALDDQVKIPKGSDATFMIAANQTHaAKSTFVYAEVRTSRTEFIVKHYAG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 554 KVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFqenptPPSpfgsmitvksakqviKPNSKHFRTTVGSKFRSSLY 633
Cdd:cd14872 476 DVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF-----PPS---------------EGDQKTSKVTLGGQFRKQLS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 634 LLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSF-SD 712
Cdd:cd14872 536 ALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVKTIAKRVgPD 615
|
650 660
....*....|....*....|....*....
gi 294862453 713 KKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14872 616 DRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
81-741 |
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: 603.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14903 1 AAILYNVKKRFL-RKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 160 SGESGAGKTVSARYAMRYFATVSkSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMST 239
Cdd:cd14903 80 SGESGAGKTETTKILMNHLATIA-GGLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEfkHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDF 319
Cdd:cd14903 159 YLLEKTRVISHERPERNYHIFYQLLASPDVEE--RLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 320 QMDVFKILAAILHLGNVQITAVGN--ERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNA 397
Cdd:cd14903 237 QEVLFEVLAGILHLGQLQIQSKPNddEKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDC 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 398 RDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 477
Cdd:cd14903 317 RDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSNTSFVIQHFADKVEY 557
Cdd:cd14903 397 EGIRWAHIDFADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSRTQFTIKHYAGPVTY 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 558 KCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGSMITVKSAKQVIKPNSKhfrTTVGSKFRSSLYLLME 637
Cdd:cd14903 477 ESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGGALTT---TTVGTQFKDSLNELMT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 638 TLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKEVC 717
Cdd:cd14903 554 TIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGRNTDVPVAERC 633
|
650 660
....*....|....*....|....*
gi 294862453 718 KVVLHRL-IQDSNQYQFGKTKIFFR 741
Cdd:cd14903 634 EALMKKLkLESPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
84-741 |
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: 590.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 84 LHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd01382 4 LNNIRVRYSKDK-IYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 163 SGAGKTVSARYAMRYFaTVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYLL 242
Cdd:cd01382 83 SGAGKTESTKYILRYL-TESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 243 EKSRVVFQSENERNYHIFYQLCASAQQSEFKHLklgsaeefnytrmggnTVIEGVNDRAEMVETQKTFTLLGFKEDFQMD 322
Cdd:cd01382 162 EKSRICVQSKEERNYHIFYRLCAGAPEDLREKL----------------LKDPLLDDVGDFIRMDKAMKKIGLSDEEKLD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 323 VFKILAAILHLGNVQITAVGNER---SSVSEDDSH-LKVFCELLGLESGRVAQWLCNRKIVTSSE----TVVK-PMTRPQ 393
Cdd:cd01382 226 IFRVVAAVLHLGNIEFEENGSDSgggCNVKPKSEQsLEYAAELLGLDQDELRVSLTTRVMQTTRGgakgTVIKvPLKVEE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 394 AVNARDALAKKIYAHLFDFIVERINQALQFSGKQHtFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQE 473
Cdd:cd01382 306 ANNARDALAKAIYSKLFDHIVNRINQCIPFETSSY-FIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKEEQE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 474 EYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFVNrNPLFEKPRMS---------- 542
Cdd:cd01382 385 LYEKEGLGVKEVEYVDNQDCIDLIEAKLvGILDLLDEESKLPKPSDQHFTSAVHQKHKN-HFRLSIPRKSklkihrnlrd 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 543 NTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSpfgsmitvKSAKQVIKPNSKhfrt 622
Cdd:cd01382 464 DEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNK--------DSKQKAGKLSFI---- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 623 TVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGIL 702
Cdd:cd01382 532 SVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKY 611
|
650 660 670
....*....|....*....|....*....|....*....
gi 294862453 703 MTKqELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd01382 612 LPP-KLARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
84-741 |
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: 587.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 84 LHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGES 163
Cdd:cd01385 4 LENLRARFKHGK-IYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 164 GAGKTVSARYAMRYFATVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYLLE 243
Cdd:cd01385 83 GSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 244 KSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDV 323
Cdd:cd01385 163 KSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQRQI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 324 FKILAAILHLGNVQI---TAVGNERSSVSEDDShLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDA 400
Cdd:cd01385 243 FSVLSAVLHLGNIEYkkkAYHRDESVTVGNPEV-LDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 401 LAKKIYAHLFDFIVERINQALQ----FSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYM 476
Cdd:cd01385 322 MAKCLYSALFDWIVLRINHALLnkkdLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 477 KEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKlYNNFVNRNPLFEKPRMSNTSFVIQHFADKV 555
Cdd:cd01385 402 KEGISWHNIEYTDNTGCLQLISKKpTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQVMEPAFIIAHYAGKV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 556 EYKCEGFLEKNRDTVYDMLVEILRASK-----------------------FHLCANFFQE----NPTPPSPFGSMITVKS 608
Cdd:cd01385 481 KYQIKDFREKNLDLMRPDIVAVLRSSSsafvreligidpvavfrwavlraFFRAMAAFREagrrRAQRTAGHSLTLHDRT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 609 AKQVIKPNSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPS 688
Cdd:cd01385 561 TKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSV 640
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 294862453 689 RWTYIEFYSRYGILMTKQELSfsdKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd01385 641 RYTFQEFITQFQVLLPKGLIS---SKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
82-741 |
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: 577.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMAR----NNRNQS 156
Cdd:cd14890 2 SLLHTLRLRY-ERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 157 IIVSGESGAGKTVSARYAMRYFATVSK-----------SGSNAH------VEDKVLASNPITEAVGNAKTTRNDNSSRFG 219
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSgfaqgasgegeAASEAIeqtlgsLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 220 KYTEISFDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVND 299
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLR-GECSSIPSCDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 300 RAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVgnERSSVSEDDS---HLKVFCELLGLESGRVAQWLCNR 376
Cdd:cd14890 240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESE--NDTTVLEDATtlqSLKLAAELLGVNEDALEKALLTR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 377 KIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYAN 456
Cdd:cd14890 318 QLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 457 EKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM----GILELLDEECLLpHGTDEN--WLQKLYNNF- 529
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVngkpGIFITLDDCWRF-KGEEANkkFVSQLHASFg 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 530 -----------VNRNPLFEKPRMSNT-SFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASkfhlcanffqenptpp 597
Cdd:cd14890 477 rksgsggtrrgSSQHPHFVHPKFDADkQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQS---------------- 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 598 spfGSMITVKSakqvikpnskhfrttVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLE 677
Cdd:cd14890 541 ---RRSIREVS---------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMME 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 294862453 678 TIRISAQSYPSRWTYIEFYSRYGILMTKQElsfsDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14890 603 AIQIRQQGFALREEHDSFFYDFQVLLPTAE----NIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
82-741 |
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: 577.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd01387 2 TVLWNLKTRY-ERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 162 ESGAGKTVSARYAMRYFATVSKSGSNAhVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFdEQNQIIGANMSTYL 241
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNL-VTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAITSQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 242 LEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQM 321
Cdd:cd01387 159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 322 DVFKILAAILHLGNV-----QITAvGNERSSVSEDdSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVN 396
Cdd:cd01387 239 SIFRILASVLHLGNVyfhkrQLRH-GQEGVSVGSD-AEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 397 ARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYM 476
Cdd:cd01387 317 ARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 477 KEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNRNPLFEKPRMSNTSFVIQHFADKV 555
Cdd:cd01387 397 REQIDWTEIAFADNQPVINLISKKpVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPRMPLPEFTIKHYAGQV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 556 EYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQ------ENPTPPSPFGSMITVKsakqvikpnskhFRT-TVGSKF 628
Cdd:cd01387 476 WYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSshraqtDKAPPRLGKGRFVTMK------------PRTpTVAARF 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 629 RSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMtKQEL 708
Cdd:cd01387 544 QDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLV-ALKL 622
|
650 660 670
....*....|....*....|....*....|....*
gi 294862453 709 SFSDKKEVCKVVLHRL--IQDSNQYQFGKTKIFFR 741
Cdd:cd01387 623 PRPAPGDMCVSLLSRLctVTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
82-741 |
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: 572.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14873 2 SIMYNLFQRYKRNQ-IYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 161 GESGAGKTVSARYAMRYFATVSK-------SGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQII 233
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQqslelslKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 234 GANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLL 313
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 314 GFKEDFQMDVFKILAAILHLGNVQ-ITAVGNERSsvseDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEfITAGGAQVS----FKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 393 QAVNARDALAKKIYAHLFDFIVERINQALQfsGKQH-TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLE 471
Cdd:cd14873 317 QAVDSRDSLAMALYARCFEWVIKKINSRIK--GKEDfKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 472 QEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNrNPLFEKPRMSNTSFVIQHF 551
Cdd:cd14873 395 QLEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHAN-NHFYVKPRVAVNNFGVKHY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 552 ADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQEnptppspfgsmITVKSAKQVIKPNSKHFRTTVGSKFRSS 631
Cdd:cd14873 474 AGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEH-----------VSSRNNQDTLKCGSKHRRPTVSSQFKDS 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 632 LYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMtKQELSFS 711
Cdd:cd14873 543 LHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLM-RNLALPE 621
|
650 660 670
....*....|....*....|....*....|
gi 294862453 712 DKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14873 622 DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
81-741 |
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: 571.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFAESkLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01379 1 DTIVSQLQKRYSRD-QIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 161 GESGAGKTVSARYAMRYFATVSKSgSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTY 240
Cdd:cd01379 80 GESGAGKTESANLLVQQLTVLGKA-NNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 241 LLEKSRVVFQSENERNYHIFYQLCAS-AQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVND---RAEMVETQKTFTLLGFK 316
Cdd:cd01379 159 LLEKSRVVHQAIGERNFHIFYYIYAGlAEDKKLAKYKLPENKPPRYLQNDGLTVQDIVNNsgnREKFEEIEQCFKVIGFT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 317 EDFQMDVFKILAAILHLGNVQITAVGNE----RSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd01379 239 KEEVDSVYSILAAILHIGDIEFTEVESNhqtdKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 393 QAVNARDALAKKIYAHLFDFIVERINQALQFS----GKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVF 468
Cdd:cd01379 319 EATDARDAMAKALYGRLFSWIVNRINSLLKPDrsasDEPLS-IGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 469 KLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvnRNPLFEKPRMSNTSFV 547
Cdd:cd01379 398 AWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKpMGLLALLDEESRFPKATDQTLVEKFHNNI--KSKYYWRPKSNALSFG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 548 IQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASkfhlcanffqENPTppspfgsmitvksakqvikpnskhFRTTVGSK 627
Cdd:cd01379 476 IHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSS----------ENPL------------------------VRQTVATY 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 628 FRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQE 707
Cdd:cd01379 522 FRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKWN 601
|
650 660 670
....*....|....*....|....*....|....
gi 294862453 708 LSFSDKKEVCKVVLHRLIQDSnqYQFGKTKIFFR 741
Cdd:cd01379 602 EEVVANRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| Myo5_CBD |
cd15470 |
Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, ... |
1369-1735 |
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: 568.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1369 EDEAKLIQNLILDLKPRGVVvNMIPGLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSNT 1448
Cdd:cd15470 1 EDESRLIKNLITDLKPRGAV-GLLPGLPAYILFMCIRHADYVNDEAKVRSLLTATINAIKKVLKKHSEDFEMLSFWLVNT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1449 CHFLNCLKQYSGEEEFMKHNSPQQNKNCLNNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPiivpgmleyeslqgisgl 1528
Cdd:cd15470 80 CRLLNCLKQYSGEEEFMKHNTPKQNEHCLKNFDLSEYRQVLSDLAIQIYQQLIKRAEEILQP------------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1529 kptgfrkrsssiddtdgyTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRC 1608
Cdd:cd15470 142 ------------------TLDSLLQQLNSFHTTLTQHGLDPELIKQVFRQLFYLICASTLNNLLLRKDLCSWSKGMQIRY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1609 NISYLEEWLKDKNLQNSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPIDDFEKRVTPSFV 1688
Cdd:cd15470 204 NVSQLEEWLRDKGLQDSGARETLEPLIQAAQLLQVKKTTEEDAQSICEMCTKLTTAQIVKILNLYTPVDDFEERVTPSFI 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 294862453 1689 RKVQALLNSREDSS--QLMLDTKYLFQVTFPFTPSPHALEMIQIPSSFK 1735
Cdd:cd15470 284 RKVQARLNERADSNqlQLLMDTKYIFPVTFPFNPSPVALEELQIPPSLH 332
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
81-741 |
1.39e-180 |
|
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: 558.40 E-value: 1.39e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14904 1 PSILFNLKKRFAASK-PYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 160 SGESGAGKTVSARYAMRYFATVSkSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMST 239
Cdd:cd14904 80 SGESGAGKTETTKIVMNHLASVA-GGRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYtrMGGN---TVIEGVNDRAEMVETQKTFTLLGFK 316
Cdd:cd14904 159 YLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQY--LGDSlaqMQIPGLDDAKLFASTQKSLSLIGLD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 317 EDFQMDVFKILAAILHLGNVQITAVGnERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVN 396
Cdd:cd14904 237 NDAQRTLFKILSGVLHLGEVMFDKSD-ENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 397 ARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEY 475
Cdd:cd14904 316 NRDALAKAIYSKLFDWMVVKINAAISTDDDRiKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 476 MKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNR--NPLFEKPRMSNTSFVIQHFAD 553
Cdd:cd14904 396 IREGLQWDHIEYQDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQTKkdNESIDFPKVKRTQFIINHYAG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 554 KVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGSmitvKSAKQVIKPNSkhfrttVGSKFRSSLY 633
Cdd:cd14904 476 PVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSETKEG----KSGKGTKAPKS------LGSQFKTSLS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 634 LLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGIlMTKQELSFSDK 713
Cdd:cd14904 546 QLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAI-MFPPSMHSKDV 624
|
650 660
....*....|....*....|....*....
gi 294862453 714 KEVCKVVLHRLIQDSN-QYQFGKTKIFFR 741
Cdd:cd14904 625 RRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
81-739 |
3.38e-180 |
|
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: 557.48 E-value: 3.38e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAY---SGQNMGD---MDPHIFAVAEEAYKQMARNNR- 153
Cdd:cd14901 1 PSILHVLRRRF-AHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehGERRAAGerkLPPHVYAVADKAFRAMLFASRg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 154 ---NQSIIVSGESGAGKTVSARYAMRYFATVS---KSGSNA----HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTE 223
Cdd:cd14901 80 qkcDQSILVSGESGAGKTETTKIIMNYLASVSsatTHGQNAtereNVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 224 ISFDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTV-IEGVNDRAE 302
Cdd:cd14901 160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDrRDGVDDSVQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 303 MVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQ-ITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTS 381
Cdd:cd14901 240 YAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCfVKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 382 SETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQF--SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKL 459
Cdd:cd14901 320 GEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYseSTGASRFIGIVDIFGFEIFATNSLEQLCINFANEKL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 460 QQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNRNPL-FE 537
Cdd:cd14901 400 QQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARpTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHASFsVS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 538 KPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCAnffqenptppspfgsmitvksakqvikpns 617
Cdd:cd14901 480 KLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS------------------------------ 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 618 khfrTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYS 697
Cdd:cd14901 530 ----STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVH 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 294862453 698 RYGILMTKQElsfSDKKEVCKVVLHR---------LIQDSNQYQFGKTKIF 739
Cdd:cd14901 606 TYSCLAPDGA---SDTWKVNELAERLmsqlqhselNIEHLPPFQVGKTKVF 653
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
87-741 |
6.13e-177 |
|
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: 548.98 E-value: 6.13e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 87 LRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMD---PHIFAVAEEAYKQM----ARNNRNQSIIV 159
Cdd:cd14892 7 LRRRY-ERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATASsppPHVFSIAERAYRAMkgvgKGQGTPQSIVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 160 SGESGAGKTVSARYAMRYFATVSKSGS---------NAH--VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDE 228
Cdd:cd14892 86 SGESGAGKTEASKYIMKYLATASKLAKgastskgaaNAHesIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 229 QNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQK 308
Cdd:cd14892 166 DGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVDGVDDATEFKQLRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 309 TFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKV--FCELLGLESGRVAQWLCNRKIVTSSETVV 386
Cdd:cd14892 246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNVakAAGLLGVDAAELMFKLVTQTTSTARGSVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 387 K-PMTRPQAVNARDALAKKIYAHLFDFIVERINQALQ----------FSGKQHTFIGVLDIYGFETFDVNSFEQFCINYA 455
Cdd:cd14892 326 EiKLTAREAKNALDALCKYLYGELFDWLISRINACHKqqtsgvtggaASPTFSPFIGILDIFGFEIMPTNSFEQLCINFT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 456 NEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPH-GTDENWLQKLYNNFVNRN 533
Cdd:cd14892 406 NEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKpLGLLPLLEEQMLLKRkTTDKQLLTIYHQTHLDKH 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 534 PLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASkfhlcanffqenptppspfgsmitvksakqvi 613
Cdd:cd14892 486 PHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSS-------------------------------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 614 kpnskhfrttvgSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYI 693
Cdd:cd14892 534 ------------SKFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFE 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 294862453 694 EFYSRYGIL---MTKQELSFSDK------KEVCKVVLHRLiqDSNQYQFGKTKIFFR 741
Cdd:cd14892 602 EFYEKFWPLarnKAGVAASPDACdattarKKCEEIVARAL--ERENFQLGRTKVFLR 656
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
81-741 |
1.89e-175 |
|
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: 545.44 E-value: 1.89e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSgQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14888 1 ASILHSLNLRFDIDE-IYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 160 SGESGAGKTVSARYAMRYFATVsksGSNA-----HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQN---- 230
Cdd:cd14888 79 SGESGAGKTESTKYVMKFLACA---GSEDikkrsLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLKskrm 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 231 -----QIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQS-------EFKHLKLG----------------SAEE 282
Cdd:cd14888 156 sgdrgRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAkntglsyEENDEKLAkgadakpisidmssfePHLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 283 FNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQ-ITAVGNERSSV--SEDDSHLKVFC 359
Cdd:cd14888 236 FRYLTKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILfENNEACSEGAVvsASCTDDLEKVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 360 ELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHT-FIGVLDIYG 438
Cdd:cd14888 316 SLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLlFCGVLDIFG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 439 FETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGT 517
Cdd:cd14888 396 FECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKpLGIFCMLDEECFVPGGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 518 DENWLQKLYNNFVNrNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKfhlcanffqeNPTPP 597
Cdd:cd14888 476 DQGLCNKLCQKHKG-HKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSK----------NPFIS 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 598 SPFGSMItvkSAKQVIKPNSKHFRtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLE 677
Cdd:cd14888 545 NLFSAYL---RRGTDGNTKKKKFV-TVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQ 620
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 294862453 678 TIRISAQSYPSRWTYIEFYSRYGILMTKQE-LSFSdkkevckvvlhrliqdsnQYQFGKTKIFFR 741
Cdd:cd14888 621 AVQVSRAGYPVRLSHAEFYNDYRILLNGEGkKQLS------------------IWAVGKTLCFFK 667
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
82-741 |
9.10e-168 |
|
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: 524.96 E-value: 9.10e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14920 2 SVLHNLKDRYY-SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 162 ESGAGKTVSARYAMRYFATVSKS--GSNAH-----VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIG 234
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASShkGRKDHnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 235 ANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVNDRAEMVETQKTFTLLG 314
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIMG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 315 FKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14920 240 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 395 VNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQE 473
Cdd:cd14920 320 DFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 474 EYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNRNPLFEKPRM--SNTSFV 547
Cdd:cd14920 400 EYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQE-QGSHSKFQKPRQlkDKADFC 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 548 IQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQE-NPTPPSPFGSMITVKSAKQVIKPNSKHFRtTVGS 626
Cdd:cd14920 479 IIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvDRIVGLDQVTGMTETAFGSAYKTKKGMFR-TVGQ 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 627 KFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQ 706
Cdd:cd14920 558 LYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 637
|
650 660 670
....*....|....*....|....*....|....*.
gi 294862453 707 -ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14920 638 iPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
82-741 |
1.04e-166 |
|
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: 522.21 E-value: 1.04e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14927 2 SVLHNLRRRYS-RWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 162 ESGAGKTVSARYAMRYFATVSKSGSN-------------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDE 228
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGpgkkaqflatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 229 QNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQ 307
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQI-LSGKKPELQDMLLVSMNPYDYHFCSqGVTTVDNMDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 308 KTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVK 387
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 388 PMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHV 467
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 468 FKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSN--- 543
Cdd:cd14927 400 FILEQEEYKREGIEWVFIDFgLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKkrk 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 544 --TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFqENptppspFGSMITVKSAKQVIKPNSKHFR 621
Cdd:cd14927 480 yeAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY-EN------YVGSDSTEDPKSGVKEKRKKAA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 622 T--TVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRY 699
Cdd:cd14927 553 SfqTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRY 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 294862453 700 GILMTKQ--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14927 633 RILNPSAipDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
81-741 |
5.41e-164 |
|
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: 514.60 E-value: 5.41e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14913 1 PAVLYNLKDRYT-SWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 161 GESGAGKTVSARYAMRYFATVSKSGSNAH---------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQ 231
Cdd:cd14913 80 GESGAGKTVNTKRVIQYFATIAATGDLAKkkdskmkgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 232 IIGANMSTYLLEKSRVVFQSENERNYHIFYQLCaSAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQKTF 310
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQIL-SNKKPELIELLLITTNPYDYPFISqGEILVASIDDAEELLATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 311 TLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMT 390
Cdd:cd14913 239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 391 RPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKL 470
Cdd:cd14913 319 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 471 EQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRM----SNTS 545
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVvkgrAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 546 FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFqenptppSPFGSMITVKSAKQVIKPNSKHFRtTVG 625
Cdd:cd14913 479 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY-------ATFATADADSGKKKVAKKKGSSFQ-TVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 626 SKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTK 705
Cdd:cd14913 551 ALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNAS 630
|
650 660 670
....*....|....*....|....*....|....*...
gi 294862453 706 Q--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14913 631 AipEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
81-741 |
9.69e-164 |
|
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: 513.75 E-value: 9.69e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14929 1 ASVLHTLRRRY-DHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 161 GESGAGKTVSARYAMRYFATVSKSGSN----AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGAN 236
Cdd:cd14929 80 GESGAGKTVNTKHIIQYFATIAAMIESkkklGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 237 MSTYLLEKSRVVFQSENERNYHIFYQLCASAQqsEFKHLKLGSA--EEFNYTRMGGNTViEGVNDRAEMVETQKTFTLLG 314
Cdd:cd14929 160 IDIYLLEKSRVIFQQPGERNYHIFYQILSGKK--ELRDLLLVSAnpSDFHFCSCGAVAV-ESLDDAEELLATEQAMDILG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 315 FKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14929 237 FLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 395 VNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEE 474
Cdd:cd14929 317 TYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 475 YMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSNTSFVIQ---- 549
Cdd:cd14929 397 YRKEGIDWVSIDFgLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHfelv 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 550 HFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPS--PFGSmitvksaKQVIKPNSKHfrtTVGSK 627
Cdd:cd14929 477 HYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSaiQFGE-------KKRKKGASFQ---TVASL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 628 FRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTK-- 705
Cdd:cd14929 547 HKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRtf 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 294862453 706 QELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14929 627 PKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| Myo5b_CBD |
cd15477 |
Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, ... |
1368-1739 |
4.23e-162 |
|
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: 497.85 E-value: 4.23e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1368 REDEAKLIQNLILDLKPRgVVVNMIPGLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSN 1447
Cdd:cd15477 1 KEDEALLIRNLVTDLKPQ-AVSATVPCLPAYILYMCIRHADYINDDQKVHSLLTSTINGIKKVLKKHNDDFEMTSFWLAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1448 TCHFLNCLKQYSGEEEFMKHNSPQQNKNCLNNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPIIVPGMLEYESLQGISG 1527
Cdd:cd15477 80 TCRLLHCLKQYSGDEGFMTQNTAKQNEHCLKNFDLTEYRQVLSDLSIQIYQQLIKIAEGILQPMIVSAMLENESIQGLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1528 LKPTGFRKRSSSIDDTD-GYTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQI 1606
Cdd:cd15477 160 VKPMGYRKRSSSMADGDnSYTLEALIRQLNTFHSIMCDQGLDPEIIQQVFKQLFYMINAVTLNNLLLRKDVCSWSTGMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1607 RCNISYLEEWLKDKNLQNSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPIDDFEKRVTPS 1686
Cdd:cd15477 240 RYNISQLEEWLRGRNLHQSGAAQTMEPLIQAAQLLQLKKKTSEDAEAICSLCTALSTQQIVKILNLYTPLNEFEERVTVS 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 294862453 1687 FVRKVQALLNSREDSSQLMLDTKYLFQVTFPFTPSPHALEMIQIPSSFKLGFL 1739
Cdd:cd15477 320 FIRTIQAQLQERNDPPQLLLDTKHMFPVLFPFNPSALTLDSIHIPASLNLDFL 372
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
81-741 |
9.07e-162 |
|
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: 508.61 E-value: 9.07e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14909 1 ASVLHNLRQRY-YAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 161 GESGAGKTVSARYAMRYFATVSKS-------GSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQII 233
Cdd:cd14909 80 GESGAGKTENTKKVIAYFATVGASkktdeaaKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 234 GANMSTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQKTFTL 312
Cdd:cd14909 160 GADIETYLLEKARVISQQSLERSYHIFYQI-MSGSVPGVKEMCLLSDNIYDYYIVSqGKVTVPNVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 313 LGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 393 QAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQ 472
Cdd:cd14909 319 QVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 473 EEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSNTS-----F 546
Cdd:cd14909 399 EEYKREGIDWAFIDFgMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGqqaahF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 547 VIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGsmitvkSAKQVIKPNSKHFrTTVGS 626
Cdd:cd14909 479 AIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGE------QAKGGRGKKGGGF-ATVSS 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 627 KFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQ 706
Cdd:cd14909 552 AYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAG 631
|
650 660 670
....*....|....*....|....*....|....*
gi 294862453 707 ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14909 632 IQGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| Myo5a_CBD |
cd15478 |
Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, ... |
1368-1742 |
1.91e-160 |
|
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: 493.78 E-value: 1.91e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1368 REDEAKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSN 1447
Cdd:cd15478 1 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1448 TCHFLNCLKQYSGEEEFMKHNSPQQNKNCLNNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPIIVPGMLEYESLQGISG 1527
Cdd:cd15478 81 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1528 LKPTGFRKRSSSIDDTDGYTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIR 1607
Cdd:cd15478 161 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1608 CNISYLEEWLKDKNLQNSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPIDDFEKRVTPSF 1687
Cdd:cd15478 241 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 294862453 1688 VRKVQALLNSREDSSQLMLDTKYLFQVTFPFTPSPHALEMIQIPSSFKLGFLNRL 1742
Cdd:cd15478 321 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 375
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
82-741 |
5.58e-155 |
|
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: 490.65 E-value: 5.58e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14911 2 SVLHNIKDRYY-SGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 162 ESGAGKTVSARYAMRYFATVS-----KSGSNAH-----------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEIS 225
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAaskpkGSGAVPHpavnpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 226 FDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVNDRAEMVE 305
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLS-NGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 306 TQKTFTLLGF-KEDFQMdVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSET 384
Cdd:cd14911 240 TVKSMNIMGMtSEDFNS-IFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 385 VVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQF 463
Cdd:cd14911 319 VTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 464 NMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFvNRNPLFEKPRMS 542
Cdd:cd14911 399 NHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFMKTDFR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 543 NTS-FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGSMITVKSAKQVIKpnsKHFR 621
Cdd:cd14911 478 GVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQFGARTRK---GMFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 622 tTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGI 701
Cdd:cd14911 555 -TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 294862453 702 LMTKQ-ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14911 634 LTPNViPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
83-741 |
1.23e-154 |
|
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: 489.54 E-value: 1.23e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP---------IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14907 3 LLINLKKRYQQDK-IFTYVGPTLIVMNPYKQIDnlfseevmqMYKEQIIQNGEYFDIKKEPPHIYAIAALAFKQLFENNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 154 NQSIIVSGESGAGKTVSARYAMRYFATVS------------------KSGSNAHVEDKVLASNPITEAVGNAKTTRNDNS 215
Cdd:cd14907 82 KQAIVISGESGAGKTENAKYAMKFLTQLSqqeqnseevltltssiraTSKSTKSIEQKILSCNPILEAFGNAKTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 216 SRFGKYTEISFDEQNQ-IIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKL---GSAEEFNYTRMGGN 291
Cdd:cd14907 162 SRFGKYVSILVDKKKRkILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLknqLSGDRYDYLKKSNC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 292 TVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQI---TAVGNERSSVSeDDSHLKVFCELLGLESGR 368
Cdd:cd14907 242 YEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFddsTLDDNSPCCVK-NKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 369 VAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQAL--QFSGKQHTF------IGVLDIYGFE 440
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpKDEKDQQLFqnkylsIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 441 TFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTL--IDFYDNQPVIDLIE-AKMGILELLDEECLLPHGT 517
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSYTDNQDVIDLLDkPPIGIFNLLDDSCKLATGT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 518 DENWLQKLYNNFvNRNPLFEKPRMSN-TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENptp 596
Cdd:cd14907 481 DEKLLNKIKKQH-KNNSKLIFPNKINkDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE--- 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 597 pspFGSMITVKSAKQVIKPNSKhfrtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVL 676
Cdd:cd14907 557 ---DGSQQQNQSKQKKSQKKDK----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVL 629
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 294862453 677 ETIRISAQSYPSRWTYIEFYSRYGILmtkqelsfsdkkevckvvlhrliqdSNQYQFGKTKIFFR 741
Cdd:cd14907 630 ESIRVRKQGYPYRKSYEDFYKQYSLL-------------------------KKNVLFGKTKIFMK 669
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
81-741 |
8.03e-153 |
|
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: 484.61 E-value: 8.03e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14917 1 PAVLYNLKERYA-SWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 161 GESGAGKTVSARYAMRYFATVSKSGSNAH---------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQ 231
Cdd:cd14917 80 GESGAGKTVNTKRVIQYFAVIAAIGDRSKkdqtpgkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 232 IIGANMSTYLLEKSRVVFQSENERNYHIFYQLCaSAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQKTF 310
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYQIL-SNKKPELLDMLLITNNPYDYAFISqGETTVASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 311 TLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMT 390
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 391 RPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKL 470
Cdd:cd14917 319 VQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 471 EQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPR----MSNTS 545
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRnikgKPEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 546 FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPfgsmitVKSAKQVIKPNSKHfrTTVG 625
Cdd:cd14917 479 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAP------IEKGKGKAKKGSSF--QTVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 626 SKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTK 705
Cdd:cd14917 551 ALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 630
|
650 660 670
....*....|....*....|....*....|....*...
gi 294862453 706 Q--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14917 631 AipEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
83-741 |
2.25e-152 |
|
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: 482.87 E-value: 2.25e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 83 VLHNLRIRFAESkLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQM----ARNNRNQSII 158
Cdd:cd14889 3 LLEVLKVRFMQS-NIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMlgrlARGPKNQCIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 159 VSGESGAGKTVSARYAMRYFATVSKSgsNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFdEQNQIIGANMS 238
Cdd:cd14889 82 ISGESGAGKTESTKLLLRQIMELCRG--NSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 239 TYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKED 318
Cdd:cd14889 159 EYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYDEVCNAMDMVGFTEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 319 FQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSH-LKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNA 397
Cdd:cd14889 239 EEVDMFTILAGILSLGNITFEMDDDEALKVENDSNGwLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAEDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 398 RDALAKKIYAHLFDFIVERINQAL----QFSGKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQE 473
Cdd:cd14889 319 RDSIAKVAYGRVFGWIVSKINQLLapkdDSSVELRE-IGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLMEQK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 474 EYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNRNPLFEKPRMSNTSFVIQHFA 552
Cdd:cd14889 398 EYKKEGIDWKEITYKDNKPILDLFLNKpIGILSLLDEQSHFPQATDESFVDKLNIHF-KGNSYYGKSRSKSPKFTVNHYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 553 DKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQenpTPPSPFGSMITVKSAKQVIKPNSKHFR-TTVGSKFRSS 631
Cdd:cd14889 477 GKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFT---ATRSRTGTLMPRAKLPQAGSDNFNSTRkQSVGAQFKHS 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 632 LYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFS 711
Cdd:cd14889 554 LGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILLCEPALPGT 633
|
650 660 670
....*....|....*....|....*....|
gi 294862453 712 dkKEVCKVVLHRliQDSNQYQFGKTKIFFR 741
Cdd:cd14889 634 --KQSCLRILKA--TKLVGWKCGKTRLFFK 659
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
83-741 |
1.18e-150 |
|
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: 477.26 E-value: 1.18e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDM-DPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14897 3 IVQTLKSRYNKDK-FYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVRSQrPPHLFWIADQAYRRLLETGRNQCILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 162 ESGAGKTVSARYAMRYFATVSKSgSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYL 241
Cdd:cd14897 82 ESGAGKTESTKYMIKHLMKLSPS-DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 242 LEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVNDRAEMVETQKTFT-------LLG 314
Cdd:cd14897 161 LEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILR-DDNRNRPVFNDSEELEYYRQMFHdltnimkLIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 315 F-KEDFQMdVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14897 240 FsEEDISV-IFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 394 AVNARDALAKKIYAHLFDFIVERINQAL----QFSGK-QHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVF 468
Cdd:cd14897 319 ANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMtRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 469 KLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLyNNFVNRNPLFEKPRMSNTSFV 547
Cdd:cd14897 399 PRERSEYEIEGIEWRDIEYHDNDDVLELFFKKpLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESPRYVASPGNRVAFG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 548 IQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFqenptppspfgsmitvksakqvikpnSKHfrttvgsk 627
Cdd:cd14897 478 IRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF--------------------------TSY-------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 628 FRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQE 707
Cdd:cd14897 524 FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFSN 603
|
650 660 670
....*....|....*....|....*....|....
gi 294862453 708 LSFSDKKEVCKVVLHrlIQDSNQYQFGKTKIFFR 741
Cdd:cd14897 604 KVRSDDLGKCQKILK--TAGIKGYQFGKTKVFLK 635
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
81-741 |
1.18e-150 |
|
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: 479.02 E-value: 1.18e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAY------SGQNM---GDMDPHIFAVAEEAYKQMARN 151
Cdd:cd14908 1 PAILHSLSRRFFRGI-IYTWTGPVLIAVNPFQRLPLYGKEILESYrqegllRSQGIespQALGPHVFAIADRSYRQMMSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 152 NR-NQSIIVSGESGAGKTVSARYAMRYFATVSKSGSNAHVE----------DKVLASNPITEAVGNAKTTRNDNSSRFGK 220
Cdd:cd14908 80 IRaSQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEgeelgklsimDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 221 YTEISFDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGS--------AEEFNYTRMGGNT 292
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDgitgglqlPNEFHYTGQGGAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 293 VIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVS---EDDSHLKVFCELLGLESGRV 369
Cdd:cd14908 240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIaeeGNEKCLARVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 370 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ--HTFIGVLDIYGFETFDVNSF 447
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKdiRSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 448 EQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEA-KMGILELLDEECLLP-HGTDENWLQKL 525
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAkKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 526 YNNFVNRNP--LFEKPRMSNTS-------FVIQHFADKVEYKCE-GFLEKNRDTVydmlveilraskfhlcanffqenpt 595
Cdd:cd14908 480 YETYLPEKNqtHSENTRFEATSiqktkliFAVRHFAGQVQYTVEtTFCEKNKDEI------------------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 596 ppspfgsmitvksakqvikPNSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGV 675
Cdd:cd14908 535 -------------------PLTADSLFESGQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGV 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 676 LETIRISAQSYPSRWTYIEFYSRYGILMT---KQELSFSDK---------KEVCKV-VLHRLIQD--------SNQYQFG 734
Cdd:cd14908 596 LEAVRVARSGYPVRLPHKDFFKRYRMLLPlipEVVLSWSMErldpqklcvKKMCKDlVKGVLSPAmvsmknipEDTMQLG 675
|
....*..
gi 294862453 735 KTKIFFR 741
Cdd:cd14908 676 KSKVFMR 682
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
81-741 |
5.66e-150 |
|
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: 476.92 E-value: 5.66e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14918 1 PGVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 161 GESGAGKTVSARYAMRYFATVSKSGS---------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQ 231
Cdd:cd14918 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 232 IIGANMSTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQKTF 310
Cdd:cd14918 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQI-TSNKKPDLIEMLLITTNPYDYAFVSqGEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 311 TLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMT 390
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 391 RPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKL 470
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 471 EQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRM----SNTS 545
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVvkgkAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 546 FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFqenptppSPFGSMITVKSAKQVIKPNSKHFRtTVG 625
Cdd:cd14918 479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLF-------STYASAEADSGAKKGAKKKGSSFQ-TVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 626 SKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTK 705
Cdd:cd14918 551 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 630
|
650 660 670
....*....|....*....|....*....|....*...
gi 294862453 706 Q--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14918 631 AipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
82-741 |
6.32e-150 |
|
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: 476.44 E-value: 6.32e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14934 2 SVLDNLRQRYTNMR-IYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 162 ESGAGKTVSARYAMRYFATVSKSGSNA-----HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGAN 236
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSsdgkgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 237 MSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKL-GSAEEFNYTRMGgNTVIEGVNDRAEMVETQKTFTLLGF 315
Cdd:cd14934 161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQG-VTVVDNMDDGEELQITDVAFDVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 316 KEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAV 395
Cdd:cd14934 240 SAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 396 NARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEY 475
Cdd:cd14934 320 NSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 476 MKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKP-----RMSNTSFVIQ 549
Cdd:cd14934 400 KREGIEWVFIDFgLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPkggkgKGPEAHFELV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 550 HFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSpfgsmitvkSAKQviKPNSKHFrtTVGSKFR 629
Cdd:cd14934 480 HYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAG---------SKKQ--KRGSSFM--TVSNFYR 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 630 SSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQ-EL 708
Cdd:cd14934 547 EQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNViPQ 626
|
650 660 670
....*....|....*....|....*....|...
gi 294862453 709 SFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14934 627 GFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
81-741 |
2.44e-149 |
|
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: 475.38 E-value: 2.44e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14912 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 161 GESGAGKTVSARYAMRYFATVSKSGS-----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQ 229
Cdd:cd14912 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 230 NQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQK 308
Cdd:cd14912 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-TSNKKPELIEMLLITTNPYDYPFVSqGEISVASIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 309 TFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14912 239 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 389 MTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVF 468
Cdd:cd14912 319 QTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 469 KLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRM----SN 543
Cdd:cd14912 399 VLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVvkgkAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 544 TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGSmitvKSAKQVIKPNSKHFRtT 623
Cdd:cd14912 479 AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAG----GGAKKGGKKKGSSFQ-T 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 624 VGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILM 703
Cdd:cd14912 554 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 633
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 294862453 704 TKQ--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14912 634 ASAipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
82-741 |
3.39e-149 |
|
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: 474.90 E-value: 3.39e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14932 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 162 ESGAGKTVSARYAMRYFATVSKSG-----------SNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQN 230
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 231 QIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLgsaEEFNYTRM--GGNTVIEGVNDRAEMVETQK 308
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCL---EDYSKYRFlsNGNVTIPGQQDKELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 309 TFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 389 MTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHV 467
Cdd:cd14932 318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 468 FKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNFVNrNPLFEKPR--M 541
Cdd:cd14932 398 FILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQGN-NPKFQKPKklK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 542 SNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGSMITVKSAKQVIKPNSKHFR 621
Cdd:cd14932 477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHGAFKTRKGMFR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 622 tTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGI 701
Cdd:cd14932 557 -TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 294862453 702 LM-TKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14932 636 LTpNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
81-741 |
6.23e-149 |
|
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: 474.16 E-value: 6.23e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14916 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 161 GESGAGKTVSARYAMRYFATVSKSG----------SNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQN 230
Cdd:cd14916 80 GESGAGKTVNTKRVIQYFASIAAIGdrskkenpnaNKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 231 QIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCaSAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQKT 309
Cdd:cd14916 160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQIL-SNKKPELLDMLLVTNNPYDYAFVSqGEVSVASIDDSEELLATDSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 310 FTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPM 389
Cdd:cd14916 239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 390 TRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFK 469
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 470 LEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPR----MSNT 544
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRnvkgKQEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 545 SFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSpfGSMITVKSAKQvikpNSKHFRtTV 624
Cdd:cd14916 479 HFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADT--GDSGKGKGGKK----KGSSFQ-TV 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 625 GSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGIL-- 702
Cdd:cd14916 552 SALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILnp 631
|
650 660 670
....*....|....*....|....*....|....*....
gi 294862453 703 MTKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14916 632 AAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
81-741 |
2.47e-148 |
|
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: 472.68 E-value: 2.47e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14910 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 161 GESGAGKTVSARYAMRYFATVSKSGS-----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQ 229
Cdd:cd14910 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 230 NQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQK 308
Cdd:cd14910 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-MSNKKPDLIEMLLITTNPYDYAFVSqGEITVPSIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 309 TFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14910 239 AIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 389 MTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVF 468
Cdd:cd14910 319 QTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 469 KLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSN---- 543
Cdd:cd14910 399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKgkve 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 544 TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGsmitvkSAKQVIKPNSKHFRtT 623
Cdd:cd14910 479 AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEG------GGKKGGKKKGSSFQ-T 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 624 VGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILM 703
Cdd:cd14910 552 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 631
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 294862453 704 TKQ--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14910 632 ASAipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
81-741 |
1.42e-146 |
|
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: 466.83 E-value: 1.42e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFA-ESKLIYTYSGIILVAMNPYKQLPiygDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNN---RNQS 156
Cdd:cd14891 1 AGILHNLEERSKlDNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSgrmQNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 157 IIVSGESGAGKTVSARYAMRYFATVS-----------------KSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFG 219
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAvggkkasgqdieqsskkRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 220 KYTEISF-DEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVN 298
Cdd:cd14891 158 KFMKLQFtKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 299 DRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQI----TAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLC 374
Cdd:cd14891 238 DAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFdeedTSEGEAEIASESDKEALATAAELLGVDEEALEKVIT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 375 NRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFD-VNSFEQFCIN 453
Cdd:cd14891 318 QREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLIN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 454 YANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFvNR 532
Cdd:cd14891 398 YANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPnGILPLLDNEARNPNPSDAKLNETLHKTH-KR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 533 NPLF--EKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKfhlcanffqenptppspfgsmitvksak 610
Cdd:cd14891 477 HPCFprPHPKDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASSA---------------------------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 611 qvikpnskhfrttvgsKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRW 690
Cdd:cd14891 529 ----------------KFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRV 592
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 294862453 691 TYIEFYSRYGILMTKQELSF--SDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14891 593 TYAELVDVYKPVLPPSVTRLfaENDRTLTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
81-741 |
1.24e-145 |
|
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: 465.31 E-value: 1.24e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14923 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 161 GESGAGKTVSARYAMRYFATVSKSGS----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQN 230
Cdd:cd14923 80 GESGAGKTVNTKRVIQYFATIAVTGDkkkeqqpgkmQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 231 QIIGANMSTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQKT 309
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQI-MSNKKPELIDLLLISTNPFDFPFVSqGEVTVASIDDSEELLATDNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 310 FTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPM 389
Cdd:cd14923 239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 390 TRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFK 469
Cdd:cd14923 319 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 470 LEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPR----MSNT 544
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKpakgKAEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 545 SFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGSmitvkSAKQVIKPNSKHFRtTV 624
Cdd:cd14923 479 HFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSG-----GSKKGGKKKGSSFQ-TV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 625 GSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMT 704
Cdd:cd14923 553 SAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNA 632
|
650 660 670
....*....|....*....|....*....|....*....
gi 294862453 705 KQ--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14923 633 SAipEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
81-741 |
1.46e-145 |
|
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: 464.97 E-value: 1.46e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14915 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 161 GESGAGKTVSARYAMRYFATVSKSGS-----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQ 229
Cdd:cd14915 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeaasgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 230 NQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQK 308
Cdd:cd14915 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-MSNKKPELIEMLLITTNPYDFAFVSqGEITVPSIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 309 TFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14915 239 AVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 389 MTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVF 468
Cdd:cd14915 319 QTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 469 KLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPR----MSN 543
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKpakgKAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 544 TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGsmitvkSAKQVIKPNSKHFRtT 623
Cdd:cd14915 479 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGG------GGKKGGKKKGSSFQ-T 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 624 VGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILM 703
Cdd:cd14915 552 VSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 631
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 294862453 704 TKQ--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14915 632 ASAipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
82-741 |
2.56e-144 |
|
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: 461.79 E-value: 2.56e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14921 2 SVLHNLRERYF-SGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 162 ESGAGKTVSARYAMRYFATVSKSGSN-------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIG 234
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGkkdtsitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 235 ANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLgsaEEF-NYTRMG-GNTVIEGVNDRAEMVETQKTFTL 312
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLL---EGFnNYTFLSnGFVPIPAAQDDEMFQETLEAMSI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 313 LGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd14921 238 MGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 393 QAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLE 471
Cdd:cd14921 318 QADFAIEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 472 QEEYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNFVNrNPLFEKPRM--SNTS 545
Cdd:cd14921 398 QEEYQREGIEWNFIDFgLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQGN-HPKFQKPKQlkDKTE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 546 FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQE-NPTPPSPFGSMITVKSAKQVIKPNSKHFRtTV 624
Cdd:cd14921 477 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDvDRIVGLDQMAKMTESSLPSASKTKKGMFR-TV 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 625 GSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMT 704
Cdd:cd14921 556 GQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 635
|
650 660 670
....*....|....*....|....*....|....*...
gi 294862453 705 KQ-ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14921 636 NAiPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
82-741 |
6.28e-142 |
|
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: 454.94 E-value: 6.28e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14930 2 SVLHNLRERYY-SGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 162 ESGAGKTVSARYAMRYFATVSKS-------GSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIG 234
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSpkgrkepGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 235 ANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTviEGVNDRAEMVETQKTFTLLG 314
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSS--SPGQERELFQETLESLRVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 315 FKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14930 239 FSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 395 VNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQE 473
Cdd:cd14930 319 DFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 474 EYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNRNPLFEKPR--MSNTSFV 547
Cdd:cd14930 399 EYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQE-QGGHPKFQRPRhlRDQADFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 548 IQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSpFGSMITVKSAKQVIKPNSKHFRtTVGSK 627
Cdd:cd14930 478 VLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVG-LEQVSSLGDGPPGGRPRRGMFR-TVGQL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 628 FRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQ- 706
Cdd:cd14930 556 YKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAi 635
|
650 660 670
....*....|....*....|....*....|....*
gi 294862453 707 ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14930 636 PKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
81-741 |
2.00e-139 |
|
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: 449.73 E-value: 2.00e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAY--------SGQNMGDMDPHIFAVAEEAYKQMARN 151
Cdd:cd14902 1 AALLQALSERF-EHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFGGLLKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 152 NR-NQSIIVSGESGAGKTVSARYAMRYFATV-------SKSGSNA-HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYT 222
Cdd:cd14902 80 ERrNQSILVSGESGSGKTESTKFLMQFLTSVgrdqsstEQEGSDAvEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 223 EISFDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEF----NYTRMGGNTVIEGVN 298
Cdd:cd14902 160 KIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYellnSYGPSFARKRAVADK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 299 DRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVS---EDDSHLKVFCELLGLESGRVAQWLCN 375
Cdd:cd14902 240 YAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAvtaASRFHLAKCAELMGVDVDKLETLLSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 376 RKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTF---------IGVLDIYGFETFDVNS 446
Cdd:cd14902 320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSIsdedeelatIGILDIFGFESLNRNG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 447 FEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKL 525
Cdd:cd14902 400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSnGLFSLLDQECLMPKGSNQALSTKF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 526 YNNFVNRNplfekprmsntSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCAnFFQENPTPPSPfgsmiT 605
Cdd:cd14902 480 YRYHGGLG-----------QFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVV-AIGADENRDSP-----G 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 606 VKSAKQVIKPNSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQS 685
Cdd:cd14902 543 ADNGAAGRRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHG 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 686 YPSRWTYIEFYSRYGILMTKQELSFSDKK-------------EVCKVVLHRLIQDSNQ---------------------- 730
Cdd:cd14902 623 YSVRLAHASFIELFSGFKCFLSTRDRAAKmnnhdlaqalvtvLMDRVLLEDGVEREEKnpgaltavtgdgsgtafendcr 702
|
730
....*....|....
gi 294862453 731 ---YQFGKTKIFFR 741
Cdd:cd14902 703 rkdVQVGRTLVFCK 716
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
82-741 |
3.05e-139 |
|
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: 447.62 E-value: 3.05e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14919 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 162 ESGAGKTVSARYAMRYFATVSKSGSN----AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANM 237
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSkkdqGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 238 STYLLEKSRVVFQSENERNYHIFYQLCASAQQsefkHLKLG-SAEEFNYTRM--GGNTVIEGVNDRAEMVETQKTFTLLG 314
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGE----HLKTDlLLEPYNKYRFlsNGHVTIPGQQDKDMFQETMEAMRIMG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 315 FKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14919 237 IPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 395 VNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQE 473
Cdd:cd14919 317 DFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 474 EYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNRNPLFEKPRM--SNTSFV 547
Cdd:cd14919 397 EYQREGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQE-QGTHPKFQKPKQlkDKADFC 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 548 IQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQEnptpPSPFGSMITVKSAKQVIKPNSKHFRT----T 623
Cdd:cd14919 476 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD----VDRIIGLDQVAGMSETALPGAFKTRKgmfrT 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 624 VGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILM 703
Cdd:cd14919 552 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 631
|
650 660 670
....*....|....*....|....*....|....*....
gi 294862453 704 TKQ-ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14919 632 PNSiPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
81-741 |
4.90e-139 |
|
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: 448.25 E-value: 4.90e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDaiIHAYSGQNMGDMD--PHIFAVAEEAYKQMARNN------ 152
Cdd:cd14895 1 PAFVDYLAQRYGVDQ-VYCRSGAVLIAVNPFKHIPGLYD--LHKYREEMPGWTAlpPHVFSIAEGAYRSLRRRLhepgas 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 153 -RNQSIIVSGESGAGKTVSARYAMRYFATVSKSG--------SNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTE 223
Cdd:cd14895 78 kKNQTILVSGESGAGKTETTKFIMNYLAESSKHTtatssskrRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 224 ISF-----DEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFK--HLKLGSAEEFNYTRMGGNTVI-E 295
Cdd:cd14895 158 MFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLelQLELLSAQEFQYISGGQCYQRnD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 296 GVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVqitAVGNERSSVSEDDS---------------------H 354
Cdd:cd14895 238 GVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNV---LFVASSEDEGEEDNgaasapcrlasaspssltvqqH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 355 LKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQA---LQFSGKQHT-- 429
Cdd:cd14895 315 LDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSAspqRQFALNPNKaa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 430 ------FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MG 502
Cdd:cd14895 395 nkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRpSG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 503 ILELLDEECLLPHGTDENWLQKLYNNFVNRNPlFEKPR--MSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEIL-R 579
Cdd:cd14895 475 IFSLLDEECVVPKGSDAGFARKLYQRLQEHSN-FSASRtdQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLgK 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 580 ASKFHL--CANFFQENPTPPSPFGSMITVKSAKQVIKpnskhfrTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKL 657
Cdd:cd14895 554 TSDAHLreLFEFFKASESAELSLGQPKLRRRSSVLSS-------VGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESA 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 658 PFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKEVCKvVLHRLiqdsnQYQFGKTK 737
Cdd:cd14895 627 SDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIE-TLKVD-----HAELGKTR 700
|
....
gi 294862453 738 IFFR 741
Cdd:cd14895 701 VFLR 704
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
71-791 |
5.07e-139 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 452.18 E-value: 5.07e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 71 DLTALSYLHEPAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAY-SGQNMGDMDPHIFAVAEEAYKQMA 149
Cdd:PTZ00014 100 DIGLLPHTNIPCVLDFLKHRY-LKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYrDAKDSDKLPPHVFTTARRALENLH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 150 RNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQ 229
Cdd:PTZ00014 179 GVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 230 NQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYtrMGGNTV-IEGVNDRAEMVETQK 308
Cdd:PTZ00014 259 GGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKY--INPKCLdVPGIDDVKDFEEVME 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 309 TFTLLGFKEDFQMDVFKILAAILHLGNVQITavGNERSSVSE----DDSHLKVF---CELLGLESGRVAQWLCNRKIVTS 381
Cdd:PTZ00014 337 SFDSMGLSESQIEDIFSILSGVLLLGNVEIE--GKEEGGLTDaaaiSDESLEVFneaCELLFLDYESLKKELTVKVTYAG 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 382 SETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQ 461
Cdd:PTZ00014 415 NQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQK 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 462 QFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPR 540
Cdd:PTZ00014 495 NFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGkSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKV 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 541 MSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQenptppspfGSMITV-KSAK-QVIkpnsk 618
Cdd:PTZ00014 575 DSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFE---------GVEVEKgKLAKgQLI----- 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 619 hfrttvGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSR 698
Cdd:PTZ00014 641 ------GSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQ 714
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 699 YGIL-MTKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR---AGQVAYLEKLRLDKLRQSCVMVQKHMRGWLQRK 774
Cdd:PTZ00014 715 FKYLdLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKR 794
|
730
....*....|....*..
gi 294862453 775 KFLRERRAALIIQQYFR 791
Cdd:PTZ00014 795 KVRKNIKSLVRIQAHLR 811
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
83-739 |
1.44e-138 |
|
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: 445.45 E-value: 1.44e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 83 VLHNLRIRFAESkLIYTYSGIILVAMNPYKQLP-IYGDAIIHAY-SGQNMGDMDPHIFAVAEEAYK--QMARNNRNQSII 158
Cdd:cd14880 3 VLRCLQARYTAD-TFYTNAGCTLVALNPFKPVPqLYSPELMREYhAAPQPQKLKPHIFTVGEQTYRnvKSLIEPVNQSIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 159 VSGESGAGKTVSARYAMRYFATVSKSGSN-------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQ 231
Cdd:cd14880 82 VSGESGAGKTWTSRCLMKFYAVVAASPTSweshkiaERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 232 IIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEgvnDRAEMveTQKTFT 311
Cdd:cd14880 162 MTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNLEE---DCFEV--TREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 312 LLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSS---VSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVV-- 386
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQVfk 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 387 KPMTRPQAVNARDALAKKIYAHLFDFIVERINQAL-QFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNM 465
Cdd:cd14880 317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSIcADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 466 HVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMS-N 543
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSpISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKLSrE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 544 TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTppspfgsmitvKSAKQVIKPNSKHFRTT 623
Cdd:cd14880 477 PSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPE-----------EKTQEEPSGQSRAPVLT 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 624 VGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILM 703
Cdd:cd14880 546 VVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLR 625
|
650 660 670
....*....|....*....|....*....|....*.
gi 294862453 704 TKQELSFSDKKEVCKVVLHrliqdSNQYQFGKTKIF 739
Cdd:cd14880 626 RLRPHTSSGPHSPYPAKGL-----SEPVHCGRTKVF 656
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
82-741 |
6.61e-138 |
|
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: 444.12 E-value: 6.61e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd15896 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 162 ESGAGKTVSARYAMRYFATVSKS-----------GSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQN 230
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 231 QIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLgsaEEFNYTRM--GGNTVIEGVNDRAEMVETQK 308
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLL---ENYNNYRFlsNGNVTIPGQQDKDLFTETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 309 TFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKP 388
Cdd:cd15896 238 AFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 389 MTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHV 467
Cdd:cd15896 318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 468 FKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIE---AKMGILELLDEECLLPHGTDENWLQKLYNNfVNRNPLFEKPR--M 541
Cdd:cd15896 398 FILEQEEYQREGIEWSFIDFgLDLQPCIDLIEkpaSPPGILALLDEECWFPKATDKSFVEKVLQE-QGTHPKFFKPKklK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 542 SNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSpFGSMITVKSAKQVIKPNSKHFR 621
Cdd:cd15896 477 DEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVG-LDKVSGMSEMPGAFKTRKGMFR 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 622 tTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGI 701
Cdd:cd15896 556 -TVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 634
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 294862453 702 LMTKQ-ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd15896 635 LTPNAiPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
81-739 |
2.74e-136 |
|
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: 438.65 E-value: 2.74e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSG-QNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14876 1 PCVLDFLKHRYLKNQ-IYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 160 SGESGAGKTVSARYAMRYFATVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMST 239
Cdd:cd14876 80 SGESGAGKTEATKQIMRYFASAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYtrMGGNTV-IEGVNDRAEMVETQKTFTLLGFKED 318
Cdd:cd14876 160 FLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKF--LNPKCLdVPGIDDVADFEEVLESLKSMGLTEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 319 FQMDVFKILAAILHLGNVQITA-----VGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14876 238 QIDTVFSIVSGVLLLGNVKITGkteqgVDDAAAISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 394 AVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQE 473
Cdd:cd14876 318 AEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERESK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 474 EYMKEDIPWTLIDFYDNQPVID-LIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSNTSFVIQHFA 552
Cdd:cd14876 398 LYKDEGIPTAELEYTSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVDSNINFIVVHTI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 553 DKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPtppspfgsMITVKSAK-QVIkpnskhfrttvGSKFRSS 631
Cdd:cd14876 478 GDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVV--------VEKGKIAKgSLI-----------GSQFLKQ 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 632 LYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGIL-MTKQELSF 710
Cdd:cd14876 539 LESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLdLGIANDKS 618
|
650 660
....*....|....*....|....*....
gi 294862453 711 SDKKEVCKVVLHRLIQDSNQYQFGKTKIF 739
Cdd:cd14876 619 LDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
83-741 |
1.14e-131 |
|
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: 425.84 E-value: 1.14e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMG-----DMDPHIFAVAEEAYKQMARNNRNQS 156
Cdd:cd14886 3 VIDILRDRFAKDK-IYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 157 IIVSGESGAGKTVSARYAMRYFATVSKSGSNAhVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGAN 236
Cdd:cd14886 82 CIVSGESGAGKTETAKQLMNFFAYGHSTSSTD-VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 237 MSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFK 316
Cdd:cd14886 161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKLFSK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 317 EDFQmDVFKILAAILHLGNVQ---ITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14886 241 NEID-SFYKCISGILLAGNIEfseEGDMGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 394 AVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQE 473
Cdd:cd14886 320 AEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEIQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 474 EYMKEDIPWTLIDFYDNQPVIDLIEA-KMGILELLDEECLLPHGTDENWLQKLYNNFvnRNPLFEKPRMSNTSFVIQHFA 552
Cdd:cd14886 400 EYEIEGIDHSMITFTDNSNVLAVFDKpNLSIFSFLEEQCLIQTGSSEKFTSSCKSKI--KNNSFIPGKGSQCNFTIVHTA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 553 DKVEYKCEGFLEKNRDTVYDMLVEILRASKFHlcanffqenptppspfgsmITVKSAKQVIKPNSKHFRTTVGSKFRSSL 632
Cdd:cd14886 478 ATVTYNTEEFVDKNKHKLSVDILELLMGSTNP-------------------IVNKAFSDIPNEDGNMKGKFLGSTFQLSI 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 633 YLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSF-- 710
Cdd:cd14886 539 DQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILISHNSSSQna 618
|
650 660 670
....*....|....*....|....*....|..
gi 294862453 711 -SDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14886 619 gEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
83-702 |
2.04e-130 |
|
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: 421.64 E-value: 2.04e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAY---------SGQNMGD--MDPHIFAVAEEAYKQMAR 150
Cdd:cd14900 3 ILSALETRFYAQK-IYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssSTRNKGSdpMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 151 --NNR--NQSIIVSGESGAGKTVSARYAMRYFA---------TVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSR 217
Cdd:cd14900 82 glNGVmsDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaaSVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 218 FGKYTEISFDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKhlklgsaeEFNYTRMggntviegv 297
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK--------RDMYRRV--------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 298 ndraemvetQKTFTLLGFKEDFQMDVFKILAAILHLGNVQItAVGNERSSVSEDDSHLKVFCE--------LLGLESGRV 369
Cdd:cd14900 225 ---------MDAMDIIGFTPHERAGIFDLLAALLHIGNLTF-EHDENSDRLGQLKSDLAPSSIwsrdaaatLLSVDATKL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 370 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQF--SGKQHT---FIGVLDIYGFETFDV 444
Cdd:cd14900 295 EKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMddSSKSHGglhFIGILDIFGFEVFPK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 445 NSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQ 523
Cdd:cd14900 375 NSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRpTGILSLIDEECVMPKGSDTTLAS 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 524 KLYNNFVNrNPLFEKPRMSNTS--FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAskfhlcanffqenptppspfg 601
Cdd:cd14900 455 KLYRACGS-HPRFSASRIQRARglFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVY--------------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 602 smitvksakqvikpnskhfrttvGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRI 681
Cdd:cd14900 513 -----------------------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRV 569
|
650 660
....*....|....*....|.
gi 294862453 682 SAQSYPSRWTYIEFYSRYGIL 702
Cdd:cd14900 570 ARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
81-741 |
1.36e-128 |
|
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: 417.26 E-value: 1.36e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14896 1 SSVLLCLKKRF-HLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 161 GESGAGKTVSARYAMRYFATVSKSGSNAHVE--DKVLasnPITEAVGNAKTTRNDNSSRFGKYTEISFdEQNQIIGANMS 238
Cdd:cd14896 80 GHSGSGKTEAAKKIVQFLSSLYQDQTEDRLRqpEDVL---PILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 239 TYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKED 318
Cdd:cd14896 156 HYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 319 FQMDVFKILAAILHLGNVQITAVGNERSSVSE--DDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVN 396
Cdd:cd14896 236 ELTAIWAVLAAILQLGNICFSSSERESQEVAAvsSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 397 ARDALAKKIYAHLFDFIVERINQALQFSGKQHTF--IGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEE 474
Cdd:cd14896 316 ARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEEE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 475 YMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNrNPLFEKPRMSNTSFVIQHFAD 553
Cdd:cd14896 396 CQRELLPWVPIPQPPRESCLDLLVDQpHSLLSILDDQTWLSQATDHTFLQKCHYHHGD-HPSYAKPQLPLPVFTVRHYAG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 554 KVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQEnptppspfgsmitvKSAKQVIKPNskhfRTTVGSKFRSSLY 633
Cdd:cd14896 475 TVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQE--------------AEPQYGLGQG----KPTLASRFQQSLG 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 634 LLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDK 713
Cdd:cd14896 537 DLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEALSDR 616
|
650 660
....*....|....*....|....*...
gi 294862453 714 KEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14896 617 ERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
83-734 |
9.97e-127 |
|
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: 414.76 E-value: 9.97e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 83 VLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQN-MGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14906 3 ILNNLGKRY-KSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINqNKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 161 GESGAGKTVSARYAMRYFATVSKSGS---------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQ 231
Cdd:cd14906 82 GESGSGKTEASKTILQYLINTSSSNQqqnnnnnnnNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSDG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 232 II-GANMSTYLLEKSRVVFQSENER-NYHIFYQLCASAQQSEFKHLKLGS-AEEFNY-------------TRMGGNTVIE 295
Cdd:cd14906 162 KIdGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNdPSKYRYldarddvissfksQSSNKNSNHN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 296 GVNDRAEMVE--TQKTFTLLGFKEDFQmDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVF---CELLGLESGRVA 370
Cdd:cd14906 242 NKTESIESFQllKQSMESMSINKEQCD-AIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLesvSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 371 QWLCNRKIVTSSETVV--KPMTRPQAVNARDALAKKIYAHLFDFIVERINQ-----------ALQFSGKQHTFIGVLDIY 437
Cdd:cd14906 321 QALLNRNLKAGGRGSVycRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRkfnqntqsndlAGGSNKKNNLFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 438 GFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHG 516
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKsDGILSLLDDECIMPKG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 517 TDENWLQKLYNNFVNRNPLFEKPrMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTP 596
Cdd:cd14906 481 SEQSLLEKYNKQYHNTNQYYQRT-LAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQITS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 597 PSPfgsmiTVKSAKQVIkpnskhfrtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVL 676
Cdd:cd14906 560 TTN-----TTKKQTQSN---------TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVL 625
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 294862453 677 ETIRISAQSYPSRWTYIEFYSRYGILMTKQELSfSDKKEVCKVVLHRLIQDSNQYQFG 734
Cdd:cd14906 626 NTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRK-NNNNPKLASQLILQNIQSKLKTMG 682
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
82-699 |
4.69e-116 |
|
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: 384.83 E-value: 4.69e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYS---GQNMGDM-------DPHIFAVAEEAYKQMAR 150
Cdd:cd14899 2 SILNALRLRY-ERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhNSQFGDRvtstdprEPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 151 NNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSG----------------SNAHVEDKVLASNPITEAVGNAKTTRNDN 214
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGnnnltnsesisppaspSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 215 SSRFGKYTEISF-DEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQL------CASAQQSEFKHLKLGSAEEFNYTR 287
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELlsadnnCVSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 288 MGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNER------------SSVSEDDSHL 355
Cdd:cd14899 241 SLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKGddtvfadearvmSSTTGAFDHF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 356 KVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGK--------- 426
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 427 ------QHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK 500
Cdd:cd14899 401 vddeedATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 501 -MGILELLDEECLLPHGTDENWLQKLYNNFVNR--NPLFEKPRM--SNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLV 575
Cdd:cd14899 481 pIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKnsHPHFRSAPLiqRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 576 EILRASKFHLCANFFQENPTPPSPFGSMITVKSAKQVIKPNSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDE 655
Cdd:cd14899 561 QLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 294862453 656 KLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRY 699
Cdd:cd14899 641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
83-741 |
1.95e-111 |
|
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: 369.91 E-value: 1.95e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 83 VLHNLRIRFAESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAY-SGQNMGDMDPHIFAVAEEAYKQM-ARNNRNQSIIVS 160
Cdd:cd14875 3 LLHCIKERFEKLHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 161 GESGAGKTVSARYAMRYFATVS----KSGSNAHVEDKVLA----SNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQI 232
Cdd:cd14875 83 GESGSGKTENAKMLIAYLGQLSymhsSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPTSGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 233 -IGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHL-KLGSAEEFNYTRmGGNTVI------EGVNDRAEMV 304
Cdd:cd14875 163 mVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLN-GGNTFVrrgvdgKTLDDAHEFQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 305 ETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVsEDDSHLKVFCELLGLESGRVAQWLcnrkIVTSSET 384
Cdd:cd14875 242 NVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQI-ADETPFLTACRLLQLDPAKLRECF----LVKSKTS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 385 VVKPMTRPQ-AVNARDALAKKIYAHLFDFIVERINQAL--QFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQ 461
Cdd:cd14875 317 LVTILANKTeAEGFRNAFCKAIYVGLFDRLVEFVNASItpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 462 QFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPR 540
Cdd:cd14875 397 HYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKrTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPYFVLPK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 541 MS-NTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKfhlcANFFQenptppspfgsmiTVKSAKQVikpnSKH 619
Cdd:cd14875 477 STiPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNST----DEFIR-------------TLLSTEKG----LAR 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 620 FRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRY 699
Cdd:cd14875 536 RKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYF 615
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 294862453 700 GILMTKQELSF---SDKKEVCKVVL---HRLIQ-DSNQYQFGKTKIFFR 741
Cdd:cd14875 616 YLIMPRSTASLfkqEKYSEAAKDFLayyQRLYGwAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
82-740 |
2.76e-107 |
|
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: 357.63 E-value: 2.76e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 82 AVLHNLRIRFAESkLIYTY-SGIILVAMNPYKQLPIYGDAIIHAY-------SGQNMGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14879 5 AITSHLASRFRSD-LPYTRlGSSALVAVNPYKYLSSNSDASLGEYgseyydtTSGSKEPLPPHAYDLAARAYLRMRRRSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 154 NQSIIVSGESGAGKTVSARYAMRYFATVSKSGSNAH-VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQI 232
Cdd:cd14879 84 DQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKKGTkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 233 IGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYT-RMGGNTVIEGV--NDRAEMVETQKT 309
Cdd:cd14879 164 IGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLaSYGCHPLPLGPgsDDAEGFQELKTA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 310 FTLLGFKEDFQMDVFKILAAILHLGNVQIT--AVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNR-KIVtSSEtVV 386
Cdd:cd14879 244 LKTLGFKRKHVAQICQLLAAILHLGNLEFTydHEGGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTYKtKLV-RKE-LC 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 387 KPMTRP-QAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFD---VNSFEQFCINYANEKLQQ 461
Cdd:cd14879 322 TVFLDPeGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDDfATFISLLDFPGFQNRSstgGNSLDQFCVNFANERLHN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 462 QFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMG--ILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKP 539
Cdd:cd14879 402 YVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGglLGILDDQTRRMPKKTDEQMLEALRKRFGNHSSFIAVG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 540 RMSNTS----FVIQHFADKVEYKCEGFLEKNRDtvydmlveilraskfHLCANFfqenptppspfgsMITVKSAKQvikp 615
Cdd:cd14879 482 NFATRSgsasFTVNHYAGEVTYSVEGFLERNGD---------------VLSPDF-------------VNLLRGATQ---- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 616 nskhfrttvgskFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEF 695
Cdd:cd14879 530 ------------LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEF 597
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 294862453 696 YSRYGILMTKQELSFSDKKevckvVLHRLIQDSNQYQFGKTKIFF 740
Cdd:cd14879 598 CERYKSTLRGSAAERIRQC-----ARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
82-702 |
6.18e-106 |
|
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: 351.12 E-value: 6.18e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQlpIYGDAIIHAYSgQNMGDMDPHIFAVAEEAYKQMARNNrNQSIIVSG 161
Cdd:cd14898 2 ATLEILEKRYASGK-IYTKSGLVFLALNPYET--IYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVHG-NQTIVISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 162 ESGAGKTVSARYAMRYFatVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDeqNQIIGANMSTYL 241
Cdd:cd14898 77 ESGSGKTENAKLVIKYL--VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 242 LEKSRVVFQSENERNYHIFYQLCASaqqsefKHLKLGSaEEFNYTRMGGNT-VIEGVNDRAEMVETQ-KTFTLLGFKEdf 319
Cdd:cd14898 153 LEKSRVTHHEKGERNFHIFYQFCAS------KRLNIKN-DFIDTSSTAGNKeSIVQLSEKYKMTCSAmKSLGIANFKS-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 320 qmdVFKILAAILHLGNVQITavgNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARD 399
Cdd:cd14898 224 ---IEDCLLGILYLGSIQFV---NDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIRN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 400 ALAKKIYAHLFDFIVERINQALQFSGKQHtfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKED 479
Cdd:cd14898 298 SMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 480 IPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKL--YNN-FVNRNplfekprmSNTSFVIQHFADKVE 556
Cdd:cd14898 376 IEWPDVEFFDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIkkYLNgFINTK--------ARDKIKVSHYAGDVE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 557 YKCEGFLEKNRDtvydmlveilrasKFHLcanffqenptppSPFGSMITVKSAKqvikpnskhfRTTVGSKFRSSLYLLM 636
Cdd:cd14898 448 YDLRDFLDKNRE-------------KGQL------------LIFKNLLINDEGS----------KEDLVKYFKDSMNKLL 492
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294862453 637 ETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGIL 702
Cdd:cd14898 493 NSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRIL 558
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
81-741 |
9.00e-101 |
|
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: 341.24 E-value: 9.00e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFAES-------KLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14887 1 PNLLENLYQRYNKAyinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 154 NQSIIVSGESGAGKTVSARYAMRYFATVS---KSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQN 230
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSdrrHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 231 QIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSefKHLKLGSAEEFNYTrmggntviegvndrAEMVETQKTF 310
Cdd:cd14887 161 KLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAA--ATQKSSAGEGDPES--------------TDLRRITAAM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 311 TLLGFKEDFQMDVFKILAAILHLGNVQIT----------------AVGNE-----RSSVSE-------------DDSHLK 356
Cdd:cd14887 225 KTVGIGGGEQADIFKLLAAILHLGNVEFTtdqepetskkrkltsvSVGCEetaadRSHSSEvkclssglkvteaSRKHLK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 357 VFCELLGLESGRVAQWLCNRKIVTSS--ETVvKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGK-------- 426
Cdd:cd14887 305 TVARLLGLPPGVEGEEMLRLALVSRSvrETR-SFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsde 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 427 ------QHTFIGVLDIYGFETF---DVNSFEQFCINYANEKLqqqfnmHVFKLEQ----EE--YMKEDIPWTLIDFYDNQ 491
Cdd:cd14887 384 dtpsttGTQTIGILDLFGFEDLrnhSKNRLEQLCINYANERL------HCFLLEQlilnEHmlYTQEGVFQNQDCSAFPF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 492 P-------------VIDLI-EAKMGILELLDEECLLPH----------GTDENW------------LQKLYNNFVNRNPL 535
Cdd:cd14887 458 SfplastltsspssTSPFSpTPSFRSSSAFATSPSLPSslsslssslsSSPPVWegrdnsdlfyekLNKNIINSAKYKNI 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 536 FEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAskfhlCANFFQENPTPPSPFGSMITVKsakqvikp 615
Cdd:cd14887 538 TPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLA-----CSTYTRLVGSKKNSGVRAISSR-------- 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 616 nskhfRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEF 695
Cdd:cd14887 605 -----RSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVEL 679
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 294862453 696 YSRYGILMTKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14887 680 WRRYETKLPMALREALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
82-741 |
3.22e-94 |
|
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: 320.22 E-value: 3.22e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAY---SGQNMGDMDPHIFAVAEEAYKQMARNNRNQSII 158
Cdd:cd14878 2 SLLYEIQKRFGNNQ-IYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 159 VSGESGAGKTVSARYAMRYFATVSKSgSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISF-DEQNQIIGANM 237
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASS-SRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 238 STYLLEKSRVVFQSENERNYHIFYQLC--ASAQQSEFKHLKLGSAEEF-NYTRMGGNTVIEGVNDRAEMVETQKTFTLLG 314
Cdd:cd14878 160 YTYMLEKSRLVSQPPGQSNFLIFYLLMdgLSAEEKYGLHLNNLCAHRYlNQTMREDVSTAERSLNREKLAVLKQALNVVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 315 FKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14878 240 FSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 395 VNARDALAKKIYAHLFDFIVERINQALQ----FSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKL 470
Cdd:cd14878 320 EFYRDLLAKSLYSRLFSFLVNTVNCCLQsqdeQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 471 EQEEYMKEDIPWTLIDFYDNQP-VIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYN-------NFV-------NRNP 534
Cdd:cd14878 400 EQTECVQEGVTMETAYSPGNQTgVLDFFFQKpSGFLSLLDEESQMIWSVEPNLPKKLQSllessntNAVyspmkdgNGNV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 535 lfeKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQenptppspfgsmitvksakqvik 614
Cdd:cd14878 480 ---ALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ----------------------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 615 pnSKhfRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIE 694
Cdd:cd14878 534 --SK--LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSD 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 294862453 695 FYSRYG-----ILMTKQELSfsdKKEVCKVVLHRLIQDSnqYQFGKTKIFFR 741
Cdd:cd14878 610 FLSRYKpladtLLGEKKKQS---AEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
83-741 |
5.82e-93 |
|
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: 316.19 E-value: 5.82e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 83 VLHNLRIRFaESKLIYTYSGIILVAMNPYKQLpiygDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd14937 3 VLNMLALRY-KKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 163 SGAGKTVSARYAMRYFatVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYLL 242
Cdd:cd14937 78 SGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 243 EKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTrMGGNTVIEGVNDRAEMVETQKTFTLLGFkEDFQMD 322
Cdd:cd14937 156 ENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYI-VNKNVVIPEIDDAKDFGNLMISFDKMNM-HDMKDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 323 VFKILAAILHLGNVQITAV-GNERSSVSE-DDSHLKVFCE---LLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNA 397
Cdd:cd14937 234 LFLTLSGLLLLGNVEYQEIeKGGKTNCSElDKNNLELVNEisnLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 398 RDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 477
Cdd:cd14937 314 CKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYKA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSNTSFVIQHFADKVEY 557
Cdd:cd14937 394 EDILIESVKYTTNESIIDLLRGKTSIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINKNFVIKHTVSDVTY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 558 KCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQEnptppspfgsmitVKSAKQVIKPNSKHFrttvgsKFRSSLYLLME 637
Cdd:cd14937 474 TITNFISKNKDILPSNIVRLLKVSNNKLVRSLYED-------------VEVSESLGRKNLITF------KYLKNLNNIIS 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 638 TLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAqSYPSRWTYIEFYSRYGIL--MTKQELSFSDKKE 715
Cdd:cd14937 535 YLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNISF-FFQYKYTFDVFLSYFEYLdySTSKDSSLTDKEK 613
|
650 660
....*....|....*....|....*.
gi 294862453 716 VCKVVLHRLiqDSNQYQFGKTKIFFR 741
Cdd:cd14937 614 VSMILQNTV--DPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
82-740 |
7.25e-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: 312.82 E-value: 7.25e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 82 AVLHNLRIRFAESKLiYTYSGIILVAMNPYKQLPiygdAIIHAYSGQNMGDMdPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14881 2 AVMKCLQARFYAKEF-FTNVGPILLSVNPYRDVG----NPLTLTSTRSSPLA-PQLLKVVQEAVRQQSETGYPQAIILSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 162 ESGAGKTVSARYAMRYFATVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEqnqiiGANMST-- 239
Cdd:cd14881 76 TSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-----GALYRTki 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 240 --YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKT-FTLLGFK 316
Cdd:cd14881 151 hcYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKAcLGILGIP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 317 edFqMDVFKILAAILHLGNVQITAvGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVN 396
Cdd:cd14881 231 --F-LDVVRVLAAVLLLGNVQFID-GGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKSVCDANMSNM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 397 ARDALAKKIYAHLFDFIVERINQALQFSGKQHT-----FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLE 471
Cdd:cd14881 307 TRDALAKALYCRTVATIVRRANSLKRLGSTLGThatdgFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTHIFKSS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 472 QEEYMKEDIPWTL-IDFYDNQPVIDLIEA-KMGILELLDEECLlPHGTDENWLQKLYNNFVNRNPLFEKPRMSNTSFVIQ 549
Cdd:cd14881 387 IESCRDEGIQCEVeVDYVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAKPQDDRMFGIR 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 550 HFADKVEYKCEGFLEKNRDTVYDMLVEILRAskfHLCAnffqenptppspFGsmitvksakqvikpnskhFRTTVgSKFR 629
Cdd:cd14881 466 HFAGRVVYDASDFLDTNRDVVPDDLVAVFYK---QNCN------------FG------------------FATHT-QDFH 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 630 SSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELS 709
Cdd:cd14881 512 TRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLR 591
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 294862453 710 FSDKKEV--CKVVL-----HRLIQDSN---QYQFGKTKIFF 740
Cdd:cd14881 592 RVEEKALedCALILqfleaQPPSKLSSvstSWALGKRHIFL 632
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
81-732 |
1.15e-84 |
|
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: 293.35 E-value: 1.15e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYS-------GQNMGDMDPHIFAVAEEAYKQMARNN 152
Cdd:cd14884 1 PNVLQNLKNRYLKNK-IYTFHASLLLALNPYKPLKeLYDQDVMNVYLhkksnsaASAAPFPKAHIYDIANMAYKNMRGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 153 RNQSIIVSGESGAGKTVSARYAMRYFATVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQI 232
Cdd:cd14884 80 KRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVENT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 233 I---------GANMSTYLLEKSRVVFQSENERNYHIFYQL---CASAQQSE------FKHLKLGSAEEFNYTRMGGNTVI 294
Cdd:cd14884 160 QknmfngcfrNIKIKILLLEINRCIAHNFGERNFHVFYQVlrgLSDEDLARrnlvrnCGVYGLLNPDESHQKRSVKGTLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 295 EGVN----DRAEMVETQKTFTLL-------GFKEDFQMDVFKILAAILHLGNvqitavgnerssvseddSHLKVFCELLG 363
Cdd:cd14884 240 LGSDsldpSEEEKAKDEKNFVALlhglhyiKYDERQINEFFDIIAGILHLGN-----------------RAYKAAAECLQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 364 LESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQAL------------QFSGKQHTFI 431
Cdd:cd14884 303 IEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdesdneDIYSINEAII 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 432 GVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEEC 511
Cdd:cd14884 383 SILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAKIFRRLDDITKLK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 512 LLPHG-TDENWLQKLYNN-------------FVN---RNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDML 574
Cdd:cd14884 463 NQGQKkTDDHFFRYLLNNerqqqlegkvsygFVLnhdADGTAKKQNIKKNIFFIRHYAGLVTYRINNWIDKNSDKIETSI 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 575 VEILRASKFHlcanFFQENptppspfgsmitvksakqVIKPNSKHFrTTVGSKFRSSLYLLMETLNATTPHYVRCIKPND 654
Cdd:cd14884 543 ETLISCSSNR----FLREA------------------NNGGNKGNF-LSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNA 599
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 294862453 655 EKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRwtyiefysrygilMTKQELSFSDKKEVCKVVLHRLIQDSNQYQ 732
Cdd:cd14884 600 KMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHK-------------IPKKETAAALKEQIAKELEKCNSNTDIEYQ 664
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
83-741 |
1.48e-84 |
|
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: 293.06 E-value: 1.48e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 83 VLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd01386 3 VLHTLRQRYG-ANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 163 SGAGKTVSARYAMRYFATVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYLL 242
Cdd:cd01386 82 SGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 243 EKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRA-EMVETQKTFTLLGFKEDFQM 321
Cdd:cd01386 162 ERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKAAaAFSKLQAAMKTLGISEEEQR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 322 DVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLE-------------SGRVAQWLCNRkivTSSETVVKP 388
Cdd:cd01386 242 AIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTleelssaifkhhlSGGPQQSTTSS---GQESPARSS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 389 MTRPQ--AVNARDALAKKIYAHLFDFIVERINQALqfSGKQHTF--IGVLDIYGFEtfdvN----------SFEQFCINY 454
Cdd:cd01386 319 SGGPKltGVEALEGFAAGLYSELFAAVVSLINRSL--SSSHHSTssITIVDTPGFQ----NpahsgsqrgaTFEDLCHNY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 455 ANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDN-QPVIDLI---------------EAKMGILELLDEECLLPHGTD 518
Cdd:cd01386 393 AQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSpGALVALIdqapqqalvrsdlrdEDRRGLLWLLDEEALYPGSSD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 519 ENWLQKLYNNF----VNRNPLFEKPRMSNTSFVIQHF--ADKVEYKCEGFLeknrdtvydmlveilRASKfhlcanffqE 592
Cdd:cd01386 473 DTFLERLFSHYgdkeGGKGHSLLRRSEGPLQFVLGHLlgTNPVEYDVSGWL---------------KAAK---------E 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 593 NPTPpspfgsmitvKSAKQVIKPNSKHF----RTTVGSKFRSSLYLLMETLNATTPHYVRCIKPN------DEKLPFEFD 662
Cdd:cd01386 529 NPSA----------QNATQLLQESQKETaavkRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkdERSTSSPAA 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 663 SKRIVQ------QLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKEVC--KVVLHRLIQ----DSNQ 730
Cdd:cd01386 599 GDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLNSEVAdeRKAVEELLEeldlEKSS 678
|
730
....*....|.
gi 294862453 731 YQFGKTKIFFR 741
Cdd:cd01386 679 YRIGLSQVFFR 689
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
93-741 |
4.51e-82 |
|
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: 285.45 E-value: 4.51e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 93 ESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSgQNMGdMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTVSA 171
Cdd:cd14905 12 KKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN-QRRG-LPPHLFALAAKAISDMQDFRRDQLIFIGGESGSGKSENT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 172 RYAMRYFATVSKSGSNaHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYLLEKSRVVFQS 251
Cdd:cd14905 90 KIIIQYLLTTDLSRSK-YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 252 ENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAIL 331
Cdd:cd14905 169 KGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFII 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 332 HLGNVQITAvGNERSSVsEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSEtvvkpmtrpqAVNARDALAKKIYAHLFD 411
Cdd:cd14905 249 ILGNVTFFQ-KNGKTEV-KDRTLIESLSHNITFDSTKLENILISDRSMPVNE----------AVENRDSLARSLYSALFH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 412 FIVERINQALQFSGKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPW-TLIDFYDN 490
Cdd:cd14905 317 WIIDFLNSKLKPTQYSHT-LGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWmTPISFKDN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 491 QPVIDLIEAKMGILELLDEECllpHGTDENWLQKLyNNFVNRNPLF-EKPrmsnTSFVIQHFADKVEYKCEGFLEKNRDT 569
Cdd:cd14905 396 EESVEMMEKIINLLDQESKNI---NSSDQIFLEKL-QNFLSRHHLFgKKP----NKFGIEHYFGQFYYDVRGFIIKNRDE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 570 VY--------DMLVEIL--RASKFHLCAN-------FFQENPTPPSPFgSMITV------KSAKQVIKPNSKH------F 620
Cdd:cd14905 468 ILqrtnvlhkNSITKYLfsRDGVFNINATvaelnqmFDAKNTAKKSPL-SIVKVllscgsNNPNNVNNPNNNSggggggG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 621 RTTVGSKFRSSLYLLMETLNATTP------HYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIE 694
Cdd:cd14905 547 NSGGGSGSGGSTYTTYSSTNKAINnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKI 626
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 294862453 695 FYSRYGILMTKQElSFSDKKEvcKVVLHRLIQDS---NQYQFGKTKIFFR 741
Cdd:cd14905 627 FFDRFSFFFQNQR-NFQNLFE--KLKENDINIDSilpPPIQVGNTKIFLR 673
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
83-741 |
4.88e-78 |
|
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: 272.77 E-value: 4.88e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 83 VLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd14882 3 ILEELRHRY-LMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 163 SGAGKTVSARYAMRYFATVSKsgSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYLL 242
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGD--GNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 243 EKSRVVFQSENERNYHIFYQLCASAQQSE-FKHLKLGSAEEFNYTRMGGNTVIEGV----NDRAEMVETQKTFT----LL 313
Cdd:cd14882 160 EKLRVSTTDGNQSNFHIFYYFYDFIEAQNrLKEYNLKAGRNYRYLRIPPEVPPSKLkyrrDDPEGNVERYKEFEeilkDL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 314 GFKEDFQMDVFKILAAILHLGNVQItaVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14882 240 DFNEEQLETVRKVLAAILNLGEIRF--RQNGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHTTEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 394 AVNARDALAKKIYAHLFDFIVERINQALQFS----GKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFK 469
Cdd:cd14882 318 ARDARDVLASTLYSRLVDWIINRINMKMSFPravfGDKYS-ISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYNQRIFI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 470 LEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKmgilelldeecllPHG----TDENWLQKLYNNFV------NRNPlFEKP 539
Cdd:cd14882 397 SEMLEMEEEDIPTINLRFYDNKTAVDQLMTK-------------PDGlfyiIDDASRSCQDQNYImdrikeKHSQ-FVKK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 540 rMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASkfhlcanffqenptppspfgsmiTVKSAKQVIKPNSKH 619
Cdd:cd14882 463 -HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSS-----------------------LDESVKLMFTNSQVR 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 620 FRTTVGSKFRSSLYLLMETL----NATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEF 695
Cdd:cd14882 519 NMRTLAATFRATSLELLKMLsigaNSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEF 598
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 294862453 696 YSRYGILMTKQELSFSDKKEVCKVVLHRLIQDSnqYQFGKTKIFFR 741
Cdd:cd14882 599 LRRYQFLAFDFDETVEMTKDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
82-741 |
2.54e-75 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 264.43 E-value: 2.54e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYsgqnmgdmdpHIFAVAEEAYKQMARNNRN-QSIIVS 160
Cdd:cd14874 2 GIAQNLHERF-KKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 161 GESGAGKTVSARYAMRYFATVSKSG-SNAHVEdkvlASNPITEAVGNAKTTRNDNSSRFGKYTEISFdEQNQIIGANMS- 238
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKvTTKHSS----AIESVFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLNLKy 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 239 TYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNT--VIEGVNDRAEMVETQKTftlLGFK 316
Cdd:cd14874 146 TVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTenIQSDVNHFKHLEDALHV---LGFS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 317 EDFQMDVFKILAAILHLGNVQITAVGNerSSVSED------DSHLKVFCELLGLEsgrVAQWLcnrKIVTSSETVVKPMT 390
Cdd:cd14874 223 DDHCISIYKIISTILHIGNIYFRTKRN--PNVEQDvveignMSEVKWVAFLLEVD---FDQLV---NFLLPKSEDGTTID 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 391 RPQAVNARDALAKKIYAHLFDFIVERINQALQFSgKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKL 470
Cdd:cd14874 295 LNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCP-LHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 471 EQEEYMKEDIPwtlIDF-----YDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSNT 544
Cdd:cd14874 374 QLVDYAKDGIS---VDYkvpnsIENGKTVELLFKKpYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARNKERL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 545 SFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENptppSPFGSMITVKSAKQVIKpnskhfrttv 624
Cdd:cd14874 451 EFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESY----SSNTSDMIVSQAQFILR---------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 625 GSKfrsslyLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMT 704
Cdd:cd14874 517 GAQ------EIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLP 590
|
650 660 670
....*....|....*....|....*....|....*...
gi 294862453 705 KQELSFSDKKEVCKVVLH-RLIQDSNQYQFGKTKIFFR 741
Cdd:cd14874 591 GDIAMCQNEKEIIQDILQgQGVKYENDFKIGTEYVFLR 628
|
|
| Myo5-like_CBD |
cd14945 |
Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied ... |
1369-1695 |
7.11e-70 |
|
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: 236.53 E-value: 7.11e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1369 EDEAKLIQNLILDLKPRGVVVnmiPGLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSNT 1448
Cdd:cd14945 1 SEEDSLLRGIVTDFEPSSGDH---KLTPAYILYLCIRHAASNGLTGQSTSLLNKVLKTIQQVVQQHNDDMQLLAFWLSNA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1449 CHFLNCLKQYSGEEEFMKHNSPQQNKNCLNNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPiivpgmleyeslqgisgl 1528
Cdd:cd14945 78 SELLYFLKQDSKLYGAAGEAPQKEEEQKLTVSDLNELKQDLEAVSIKIYQQALKYLNKNLQP------------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1529 kptgfrkrsssiddtdgyTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRC 1608
Cdd:cd14945 140 ------------------KIRDIVKFLNSFLDLLKSFHVHPEIRSQVFTQLFSFINARLFNQLITKKDALSWSRGMQIRA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1609 NISYLEEWLKDKNLqNSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPIDDFEKRVTPSFV 1688
Cdd:cd14945 202 NISRLEEWCEGRGL-EHLAVDFLSKLIQAVQLLQLKKYTQEDIEILCELCPSLNPAQLQAILTQYQPANYGESPVPKEIL 280
|
....*..
gi 294862453 1689 RKVQALL 1695
Cdd:cd14945 281 RTLAAEV 287
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
84-699 |
1.59e-61 |
|
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: 226.01 E-value: 1.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 84 LHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQN----------MGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14893 4 LYTLRARYRMEQ-VYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSReqtplyekdtVNDAPPHVFALAQNALRCMQDAGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 154 NQSIIVSGESGAGKTVSARYAMRYFATV-----------SKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYT 222
Cdd:cd14893 83 DQAVILLGGMGAGKSEAAKLIVQYLCEIgdeteprpdseGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 223 EISFDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQ--SEFKHLKLG-SAEEFNYTRMGGNTVIEGVND 299
Cdd:cd14893 163 SVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdpTLRDSLEMNkCVNEFVMLKQADPLATNFALD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 300 RAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQI---------------TAVGNERSSVSEDDSHLKVFCELLGL 364
Cdd:cd14893 243 ARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvggansTTVSDAQSCALKDPAQILLAAKLLEV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 365 ESGRVAQWLCNRKIVT--SSETV--VKPMTRPQAVNARDALAKKIYAHLFDFIVERINQAL-----QFSGK----QHTFI 431
Cdd:cd14893 323 EPVVLDNYFRTRQFFSkdGNKTVssLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdRYEKSniviNSQGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 432 GVLDIYGFETFD--VNSFEQFCINYANEK-----LQQQFNMHVFKLEQEEYMKED--IPWTLIDF-YDNQPVIDLIEAK- 500
Cdd:cd14893 403 HVLDMVGFENLTpsQNSFDQLCFNYWSEKvhhfyVQNTLAINFSFLEDESQQVENrlTVNSNVDItSEQEKCLQLFEDKp 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 501 MGILELLDEECLLPHGTDENWLQKLYN-------------NFVNRNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNR 567
Cdd:cd14893 483 FGIFDLLTENCKVRLPNDEDFVNKLFSgneavgglsrpnmGADTTNEYLAPSKDWRLLFIVQHHCGKVTYNGKGLSSKNM 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 568 DTVYDMLVEILRASKFHLCanffqeNPTPPSPFGSMITVKSAKQVIKPNSKH--FRTTVGSKFRSS---------LY--- 633
Cdd:cd14893 563 LSISSTCAAIMQSSKNAVL------HAVGAAQMAAASSEKAAKQTEERGSTSskFRKSASSARESKnitdsaatdVYnqa 636
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 294862453 634 -LLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRY 699
Cdd:cd14893 637 dALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY 703
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
104-227 |
3.70e-44 |
|
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: 158.28 E-value: 3.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 104 ILVAMNPYKQLPIYGDA-IIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTVSARYAMRYFATVS 182
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 294862453 183 KSGSNA--------------HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFD 227
Cdd:cd01363 81 FNGINKgetegwvylteitvTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLD 139
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
81-739 |
2.72e-42 |
|
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: 167.32 E-value: 2.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQN-MGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14938 1 PSVLYHLKERF-KNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDcIEDLSLNEYHVVHNALKNLNELKRNQSIII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 160 SGESGAGKTVSARYAMRYFATVSK------SGSNAHVEDKVLAS----------------NPITEAVGNAKTTRNDNSSR 217
Cdd:cd14938 80 SGESGSGKSEIAKNIINFIAYQVKgsrrlpTNLNDQEEDNIHNEentdyqfnmsemlkhvNVVMEAFGNAKTVKNNNSSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 218 FGKYTEISFDEQnQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGv 297
Cdd:cd14938 160 FSKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFS- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 298 NDRAEMVETQKTFTLLgFKEDFQMD-VFKILAAILHLGNVQITAV---------------------------GNERSSVS 349
Cdd:cd14938 238 DYSGKILELLKSLNYI-FDDDKEIDfIFSVLSALLLLGNTEIVKAfrkksllmgknqcgqninyetilseleNSEDIGLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 350 EDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSeTVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQ---ALQFSGK 426
Cdd:cd14938 317 ENVKNLLLACKLLSFDIETFVKYFTTNYIFNDS-ILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEkctQLQNINI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 427 QHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTL-IDFYDNQPVID-LIEAKMGIL 504
Cdd:cd14938 396 NTNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNlLVGPTEGSL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 505 ELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPR---MSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAS 581
Cdd:cd14938 476 FSLLENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDditGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 582 K----FHLCANFFQENPTPPSPFGSMITVKSAKQVIKPNSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEK- 656
Cdd:cd14938 556 EneymRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESKr 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 657 LPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSrygILMTKQElsfsDKKEVCKVVLHRLIQDSNQYQFGKT 736
Cdd:cd14938 636 ELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLS---IFDIKNE----DLKEKVEALIKSYQISNYEWMIGNN 708
|
...
gi 294862453 737 KIF 739
Cdd:cd14938 709 MIF 711
|
|
| DIL |
pfam01843 |
DIL domain; The DIL domain has no known function. |
1574-1675 |
3.98e-34 |
|
DIL domain; The DIL domain has no known function.
Pssm-ID: 460359 [Multi-domain] Cd Length: 103 Bit Score: 126.94 E-value: 3.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1574 QAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRCNISYLEEWLKDKNLQnSLAKETLEPLSQAAWLLQVKKTTDSDAKE 1653
Cdd:pfam01843 1 QLFSQLFYFINAELFNRLLLRKKYCSWSKGMQIRYNLSRLEEWARSNGLE-SEARDHLAPLIQAAQLLQLRKSTLEDLDS 79
|
90 100
....*....|....*....|..
gi 294862453 1654 IYERCTSLSAVQIIKILNSYTP 1675
Cdd:pfam01843 80 ILQVCPALNPLQLHRLLTLYQP 101
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
187-703 |
5.57e-33 |
|
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: 139.11 E-value: 5.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 187 NAHVEDK---VLASNPITEAVGNAKTTRNDNSSRFGKYT--EISFDE---QNQIIGANMSTYLLEKSRVVFQ------SE 252
Cdd:cd14894 239 NPHAAKKlsiVLDSNIVLEAFGHATTSMNLNSSRFGKMTtlQVAFGLhpwEFQICGCHISPFLLEKSRVTSErgresgDQ 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 253 NERNYHIFYQLCASAQQSEF-----KHLKLGSAEEFNYTRMG-GNTVIEGV--------NDRAEMVETQKTFTLLGFKED 318
Cdd:cd14894 319 NELNFHILYAMVAGVNAFPFmrllaKELHLDGIDCSALTYLGrSDHKLAGFvskedtwkKDVERWQQVIDGLDELNVSPD 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 319 FQMDVFKILAAILHLGNVQIT--AVGNE--RSSVSEDDSHLKVfCELLGLESGRVAQWLCNRKIVT---SSETVVKPMTR 391
Cdd:cd14894 399 EQKTIFKVLSAVLWLGNIELDyrEVSGKlvMSSTGALNAPQKV-VELLELGSVEKLERMLMTKSVSlqsTSETFEVTLEK 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 392 PQAVNARDALAKKIYAHLFDFIVERINQALQFS-----GKQH------------TFIGVLDIYGFETFDVNSFEQFCINY 454
Cdd:cd14894 478 GQVNHVRDTLARLLYQLAFNYVVFVMNEATKMSalstdGNKHqmdsnasapeavSLLKIVDVFGFEDLTHNSLDQLCINY 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 455 ANEKLQQqfnmhvfKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQ-----KLY-NN 528
Cdd:cd14894 558 LSEKLYA-------REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENMNAQQeekrnKLFvRN 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 529 FVNRNP--LFEKPR-MSNTS-----------FVIQHFADKVEYKCEGFLEKNRDTVY-DMLVEILRASKFHLCANFFQEN 593
Cdd:cd14894 631 IYDRNSsrLPEPPRvLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYaNLLVGLKTSNSSHFCRMLNESS 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 594 PTPPSPFGSMITVKSAKQVIKpNSKHFrttVGsKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRAC 673
Cdd:cd14894 711 QLGWSPNTNRSMLGSAESRLS-GTKSF---VG-QFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQ 785
|
570 580 590
....*....|....*....|....*....|....
gi 294862453 674 GV---LETIRISAQSYPS-RWTYIEFYSRYGILM 703
Cdd:cd14894 786 RLirqMEICRNSSSSYSAiDISKSTLLTRYGSLL 819
|
|
| Myo5p-like_CBD_DIL_ANK |
cd15473 |
cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ... |
1369-1729 |
3.04e-24 |
|
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: 105.33 E-value: 3.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1369 EDEAKLIQNLILDLKPRGVVVNMIPgLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSNT 1448
Cdd:cd15473 7 EDELPRILDLLITNMTPQRSPSQRP-VPANLLFLCARYAHYHCSPELLEDLLLGALDRIEDVVEANPWDMTLLAFWLSNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1449 C---HFLNCLKQYsgeeefmkhnspqqnknclnNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPIIVPGMLEYESLqgi 1525
Cdd:cd15473 86 TlllHYLKKDAGL--------------------VEATPEFQQELAELINEIFVLIIRDAERRIDKLLDASPRNITSL--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1526 sglkptgfrkrsssiddtdgytMTSVLQQLSYFYttmcqngLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQ 1605
Cdd:cd15473 143 ----------------------LSSTLYVLELYD-------VHPAIIIQALSQLFYWLGCELFNRILTNKKYLCRSKAMQ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1606 IRCNISYLEEWLKDKNLQ-------NSLAKETLEPLSQAAWLLQVKKT-TDSDA-KEIYERCTSLSAVQIIKILNSYTPi 1676
Cdd:cd15473 194 IRMNLSALEDWARSNNLQpekgespPRIARSHLAPVIQLLQWLQCLSSlDDFESlIATIQQLDALNPLQLLRAVKDYRY- 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 294862453 1677 DDFEKRVTPSFVRKVQALLNSRedssqlmLDTKYLFQVTFPFTPsphalEMIQ 1729
Cdd:cd15473 273 EVNEGRMPEECVKYLAQLQKDW-------LDSRYMLPFSLPTDT-----EMLV 313
|
|
| fMyo2p_CBD |
cd15480 |
cargo binding domain of fungal myosin 2; Yeast myosin V travels along actin cables, actin ... |
1396-1706 |
2.06e-23 |
|
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: 104.20 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1396 PAHILFMCvryadsLNDanMLK--------SLMNSTINGIKQVVKEhLEDFEMLS---FWLSNTcHFLNCLKQYSgEEEF 1464
Cdd:cd15480 48 PAHLIILI------LSE--MWRlgltkeseRFLANVMQTIQQHVMS-LKGEDAIVpgaFWLSNV-HELLSFVCLA-ESDI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1465 MKHNSPqqnKNCLNNFDLSEYRQILSDV-------AIRIYHQFIIIMEKNIQPiivpgmleyeslqgisglkptgfrkrs 1537
Cdd:cd15480 117 LQGIGP---GKDMREEEWEEYERLVTVVkhdleslEYNIYHTWMKELKKRLEK--------------------------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1538 ssiddtdgyTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRCNISYLEEWL 1617
Cdd:cd15480 167 ---------TMDDILNFFNKVYKSMKSYYIEESVIRQVVTELLKLIGVTAFNDLLMRRNFLSWKRGLQINYNITRLEEWC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1618 K-----DKNLQnslaketLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTpIDDFEKRVTPSFVRKVQ 1692
Cdd:cd15480 238 KshdipEGTLQ-------LEHLMQATKLLQLKKATLEDIEIIYDVCWILTPAQIQKLISQYY-VADYENPISPEILKAVA 309
|
330
....*....|....
gi 294862453 1693 ALLNSREDSSQLML 1706
Cdd:cd15480 310 ARVKPEDKSDHLLL 323
|
|
| Myo5p-like_CBD_fungal |
cd15474 |
cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin ... |
1396-1694 |
3.29e-22 |
|
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: 100.19 E-value: 3.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1396 PAHILFMC---VRYADSLNDANMLKSLmNSTINGIKQVVKEHLEDFEMLS--FWLSNTcH----FLNCLKQ---YSGEEE 1463
Cdd:cd15474 34 LGHVNFLIysqMWKSLLELLTQSERFL-SHVLSYIASIVDSLPKKETIPDgaFWLANL-HelrsFVVYLLSlieHSSSDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1464 FMKHNSPQQNKNclnnfdLSEYRQILSdvaiRIYHQFIIIMEKNIQPIIVPGMLEYESLQGISGlkptgFRKRSSSIDDT 1543
Cdd:cd15474 112 FSKESEEYWNTL------FDKTLKHLS----NIYSTWIDKLNKHLSPKIEGAVLVLLTSLDLSE-----LIDLNKEFFNK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1544 DGYTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRCNISYLEEWLKDKNLq 1623
Cdd:cd15474 177 PKKKMADLITFLNEVYDLLQSFSVQPELLNAIVSSTLQYINVEAFNSLITKRSALSWKRGSQISYNVSRLKEWCHQHGL- 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294862453 1624 nSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPiDDFEKRVTPSFVRKVQAL 1694
Cdd:cd15474 256 -SDANLQLEPLIQASKLLQLRKDDENDFKIILSVCYALNPAQIQKLLDKYQP-ANYEAPVPKEFLNALEKL 324
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
886-1356 |
2.91e-19 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 95.12 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 886 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAV---EEKLAKLQ 962
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVaqlELQIASLN 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 963 KHNSELETQKEQIQ----------------------LKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSfELKTQ 1020
Cdd:TIGR02168 400 NEIERLEARLERLEdrrerlqqeieellkkleeaelKELQAELEELEEELEELQEELERLEEALEELREELEEA-EQALD 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1021 DYEKQIQSLKEEIKALKDekMQLQHLVEGEHVT-----SDGLKAEVARLSKQVKTISEFEKEIEL-------------LQ 1082
Cdd:TIGR02168 479 AAERELAQLQARLDSLER--LQENLEGFSEGVKallknQSGLSGILGVLSELISVDEGYEAAIEAalggrlqavvvenLN 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1083 AQKIDVE--------------------KHVQSQKREMREKMSEITKQL--LESYDIE---DVRSRLS----VEDLEHLNE 1133
Cdd:TIGR02168 557 AAKKAIAflkqnelgrvtflpldsikgTEIQGNDREILKNIEGFLGVAkdLVKFDPKlrkALSYLLGgvlvVDDLDNALE 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1134 --------------DGEL----WFAYEGLKKATRVLESHFQSQKDCyEKEIEALNFKVVHLSQEINHLQKLFREendINE 1195
Cdd:TIGR02168 637 lakklrpgyrivtlDGDLvrpgGVITGGSAKTNSSILERRREIEEL-EEKIEELEEKIAELEKALAELRKELEE---LEE 712
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1196 SIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLnEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAqneihtkEK 1275
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI-AQLSKELTELEAEIEELEERLEEAEEELAEAEA-------EI 784
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1276 EKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVHSSS 1355
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
.
gi 294862453 1356 G 1356
Cdd:TIGR02168 865 E 865
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
813-1383 |
6.53e-18 |
|
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: 90.56 E-value: 6.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 813 IIQKHCRGYLVRSLYQLIRMATITMQAYSRGFLARRRYRKMLEE-HKAVILqkyARAWLARRRFQSIRRFVLNIQLTYRV 891
Cdd:pfam15921 303 IIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEElEKQLVL---ANSELTEARTERDQFSQESGNLDDQL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 892 QRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKaathrRNYEekgkryrdaVEEKLAKLQKHNSELETQ 971
Cdd:pfam15921 380 QKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDD-----RNME---------VQRLEALLKAMKSECQGQ 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 972 KEQIQLKLQEKTEELkEKMDNLTKQLFDD-------VQKEERQRMLLEKS------FELKTQDYEKQIQSLKEEIKALK- 1037
Cdd:pfam15921 446 MERQMAAIQGKNESL-EKVSSLTAQLESTkemlrkvVEELTAKKMTLESSertvsdLTASLQEKERAIEATNAEITKLRs 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1038 --DEKMQ-LQHL-VEGEHVTSDGLKAEVARLSkqvktISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEitKQLLES 1113
Cdd:pfam15921 525 rvDLKLQeLQHLkNEGDHLRNVQTECEALKLQ-----MAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVE--KAQLEK 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1114 yDIEDvrSRLSVEDLEHLNEdgelwfayeglKKATRVLESHFQSQkdcyekEIEALNFKVVHLSQEINHLQKLFREEND- 1192
Cdd:pfam15921 598 -EIND--RRLELQEFKILKD-----------KKDAKIRELEARVS------DLELEKVKLVNAGSERLRAVKDIKQERDq 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1193 -INE--SIRHEVTRLTSE-NMMIPDFKQQISELEKQKQDLEIRLneqaEKMKGKLEELSNQLHRSQEEEGTQRK-ALEAQ 1267
Cdd:pfam15921 658 lLNEvkTSRNELNSLSEDyEVLKRNFRNKSEEMETTTNKLKMQL----KSAQSELEQTRNTLKSMEGSDGHAMKvAMGMQ 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1268 NEIHTK--EKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTI 1345
Cdd:pfam15921 734 KQITAKrgQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
|
570 580 590
....*....|....*....|....*....|....*...
gi 294862453 1346 GKAndvhsSSGPKEYLGMLQYKREDEAKLIQNLILDLK 1383
Cdd:pfam15921 814 DKA-----SLQFAECQDIIQRQEQESVRLKLQHTLDVK 846
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
890-1344 |
7.15e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 90.12 E-value: 7.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 890 RVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLE---AELEKAATHRRNYEEKGKRYRDaVEEKLAKLQKHNS 966
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvKELKELKEKAEEYIKLSEFYEE-YLDELREIEKRLS 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 967 ELETQKEQIQLKLQE------KTEELKEKMDNLTKQ---LFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALK 1037
Cdd:PRK03918 318 RLEEEINGIEERIKEleekeeRLEELKKKLKELEKRleeLEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1038 DEKMQLQHLVEGEHVTSDGLKAEVARLSKQV-----------------------KTISEFEKEIELLQAQKIDVEKHVQS 1094
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERK 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1095 QKREMREKMSEITKQ-----LLESYD-IEDVRSRLSVEDLEHLNEDGELwfaYEGLKKATRVLESHFQSQKD------CY 1162
Cdd:PRK03918 478 LRKELRELEKVLKKEselikLKELAEqLKELEEKLKKYNLEELEKKAEE---YEKLKEKLIKLKGEIKSLKKelekleEL 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1163 EKEIEALNFKVVHLSQEINHLQKLFREENdiNESIRHEVTRLTSenmMIPDFKQQIsELEKQKQDLEIRLNEQaEKMKGK 1242
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKELEELG--FESVEELEERLKE---LEPFYNEYL-ELKDAEKELEREEKEL-KKLEEE 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1243 LEELSNQLHRSQEEEGTQRKALEAQNEIHTKEK-EKLIDKIQEMQEASDHLKKQFETESEVkcnfRQEASRlTLEnrDLE 1321
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKR----REEIKK-TLE--KLK 700
|
490 500
....*....|....*....|...
gi 294862453 1322 EELDMKDRVIKKLQDQVKTLSKT 1344
Cdd:PRK03918 701 EELEEREKAKKELEKLEKALERV 723
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
886-1349 |
2.31e-17 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 88.54 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 886 QLTYRVQRLQKKLEdqNKENhglveKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHN 965
Cdd:TIGR04523 37 QLEKKLKTIKNELK--NKEK-----ELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 966 SELETQKEQIqLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFElKTQDYEKQIQSLKEEIKALKDEKMQLQH 1045
Cdd:TIGR04523 110 SEIKNDKEQK-NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNN-KYNDLKKQKEELENELNLLEKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1046 LVegehvtsDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSV 1125
Cdd:TIGR04523 188 NI-------DKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1126 EDLEHLNEDGELWFAYEGLKKATRVLESHFQSqkdcYEKEIEALNfkvvhlSQEINHLQKLFREE-NDINESIRHEVTRL 1204
Cdd:TIGR04523 261 EQNKIKKQLSEKQKELEQNNKKIKELEKQLNQ----LKSEISDLN------NQKEQDWNKELKSElKNQEKKLEEIQNQI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1205 TSENMMIPDFKQQISELEKQKQDLE---IRLNEQAEKMKGKLEELSNQLHRSQEEE---GTQRKALEAQNEIHTKEKEKL 1278
Cdd:TIGR04523 331 SQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEKQNEIEKLKKENQSYKQEIknlESQINDLESKIQNQEKLNQQK 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294862453 1279 IDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKAN 1349
Cdd:TIGR04523 411 DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
890-1349 |
8.07e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 86.66 E-value: 8.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 890 RVQRLQKKLEDQNKENHGLVEKLTSLAALRagdvEKIQKLEAELEKAATHRRNYEEKGKRyrdaVEEKLAKLQKHNSELE 969
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKELEELK----EEIEELEKELESLEGSKRKLEEKIRE----LEERIEELKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 970 TQKEQIQlKLQEKTEE---LKEKMDNLTKQLFDdVQKE----ERQRMLLEKSFElKTQDYEKQIQSLKEEIKALKDEKMQ 1042
Cdd:PRK03918 280 EKVKELK-ELKEKAEEyikLSEFYEEYLDELRE-IEKRlsrlEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1043 LQHLVEgEHVTSDGLKAEVARLSKQVK--TISEFEKEIELLQAQKIDVEKHVqsqkREMREKMSEITkqllesydiedvr 1120
Cdd:PRK03918 357 LEERHE-LYEEAKAKKEELERLKKRLTglTPEKLEKELEELEKAKEEIEEEI----SKITARIGELK------------- 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1121 srlsvedlehlNEDGELWFAYEGLKKATRVL--------ESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREEnd 1192
Cdd:PRK03918 419 -----------KEIKELKKAIEELKKAKGKCpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL-- 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1193 inESIRHEVTRLTSENMMIPDFKQQISELEK-QKQDLEiRLNEQAEKMKGKLEELSNQLhRSQEEEGTQRKALEaqneih 1271
Cdd:PRK03918 486 --EKVLKKESELIKLKELAEQLKELEEKLKKyNLEELE-KKAEEYEKLKEKLIKLKGEI-KSLKKELEKLEELK------ 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1272 tKEKEKLIDKIQEMQEASDHLKKQ-----FETESEVKCNFR--QEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKT 1344
Cdd:PRK03918 556 -KKLAELEKKLDELEEELAELLKEleelgFESVEELEERLKelEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEE 634
|
....*
gi 294862453 1345 IGKAN 1349
Cdd:PRK03918 635 LAETE 639
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
886-1350 |
1.04e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 86.65 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 886 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHN 965
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 966 SELETQKEQIQLkLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEkSFELKTQDYEKQIQSLKEEIKALKDEKMQLQH 1045
Cdd:TIGR02168 337 EELAELEEKLEE-LKEELESLEAELEELEAELEELESRLEELEEQLE-TLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1046 LVEGEH--VTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKqllESYDIEDVRSRL 1123
Cdd:TIGR02168 415 RRERLQqeIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA---AERELAQLQARL 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1124 -SVEDLEHLNED-----GELWFAYEGLKKATRVLESHFQSQKDcYEKEIEA-----LNFKVVHLSQE----INHLQK--- 1185
Cdd:TIGR02168 492 dSLERLQENLEGfsegvKALLKNQSGLSGILGVLSELISVDEG-YEAAIEAalggrLQAVVVENLNAakkaIAFLKQnel 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1186 ---LFREENDINESIRHEVTRLTSENmmIPDFKQQISELEKQKQDLEIRLN------------EQAEKMKGKLEEL---- 1246
Cdd:TIGR02168 571 grvTFLPLDSIKGTEIQGNDREILKN--IEGFLGVAKDLVKFDPKLRKALSyllggvlvvddlDNALELAKKLRPGyriv 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1247 ---------------------SNQLHRSQE--EEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVK 1303
Cdd:TIGR02168 649 tldgdlvrpggvitggsaktnSSILERRREieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI 728
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 294862453 1304 CNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKAND 1350
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
890-1343 |
1.01e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.65 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 890 RVQRLQKKLEDQNKenhglVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELE 969
Cdd:PTZ00121 1303 KADEAKKKAEEAKK-----ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 970 TQKEQIQLKLQE--KTEELKEKMDNLTKQLfDDVQKEERQRmllEKSFELKTQDYEK----QIQSLKEEIKALKDEKMQL 1043
Cdd:PTZ00121 1378 KKADAAKKKAEEkkKADEAKKKAEEDKKKA-DELKKAAAAK---KKADEAKKKAEEKkkadEAKKKAEEAKKADEAKKKA 1453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1044 QHLVEGEHVTSdglKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHV-QSQKREMREKMSEITKQLLESYDIEDVRSR 1122
Cdd:PTZ00121 1454 EEAKKAEEAKK---KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAdEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1123 LSVEDLEHLNEDGELWFAYEgLKKATRVLESHFQSQKDCYEKEIEALNF---KVVHLSQ----EINHLQKLFREENDIN- 1194
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADE-LKKAEELKKAEEKKKAEEAKKAEEDKNMalrKAEEAKKaeeaRIEEVMKLYEEEKKMKa 1609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1195 -ESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEgtQRKALEAQNEIHTK 1273
Cdd:PTZ00121 1610 eEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED--KKKAEEAKKAEEDE 1687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1274 EK--EKLIDKIQEMQEASDHLKK---------QFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLS 1342
Cdd:PTZ00121 1688 KKaaEALKKEAEEAKKAEELKKKeaeekkkaeELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
.
gi 294862453 1343 K 1343
Cdd:PTZ00121 1768 K 1768
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
854-1285 |
4.73e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.88 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 854 LEEHKAVILQKYARAWLARRRFQSIRrfvlniQLTYRVQRLQKKLEDQNKENhgLVEKLTSLAalragdvEKIQKLEAEL 933
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEEAK------AKKEELERLKKRLTGLTPEK--LEKELEELE-------KAKEEIEEEI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 934 EKAATHRRNYEEKGKRYRDAVEE-KLAKLQ--KHNSEL-ETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRM 1009
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEElKKAKGKcpVCGRELtEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1010 LLEKSFEL-KTQDYEKQIQSLKEEIKALKDEKM-QLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLqaqkid 1087
Cdd:PRK03918 488 VLKKESELiKLKELAEQLKELEEKLKKYNLEELeKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL------ 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1088 vekhvQSQKREMREKMSEITKQLLES--YDIEDVRSRLsvEDLEhlnedgELWFAYEGLKKATRVLESHFQSQKDCYE-- 1163
Cdd:PRK03918 562 -----EKKLDELEEELAELLKELEELgfESVEELEERL--KELE------PFYNEYLELKDAEKELEREEKELKKLEEel 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1164 ----KEIEALNFKVVHLSQEINHLQKLFREENdiNESIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEirlnEQAEKM 1239
Cdd:PRK03918 629 dkafEELAETEKRLEELRKELEELEKKYSEEE--YEELREEYLELSRE---LAGLRAELEELEKRREEIK----KTLEKL 699
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 294862453 1240 KGKLEELSnqlhRSQEEEGTQRKALEAQNEIHTK-------EKEKLIDKIQEM 1285
Cdd:PRK03918 700 KEELEERE----KAKKELEKLEKALERVEELREKvkkykalLKERALSKVGEI 748
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
924-1287 |
1.42e-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: 79.73 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 924 EKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKEKMDNLtkqlfdDVQK 1003
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE-KLKERLEELEEDLSSL------EQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1004 EERQRMLleKSFELKTQDYEKQIQSLKEEIKALKDekMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQA 1083
Cdd:TIGR02169 754 ENVKSEL--KELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1084 QKIDVEKHVQSQKREMREKMSEITKQLLESY-DIEDVRSRLSvedlEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCY 1162
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNgKKEELEEELE----ELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1163 EKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTrLTSENMMIPDFKQQISELEKqkqdlEIRlneqaekmkgK 1242
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE-IPEEELSLEDVQAELQRVEE-----EIR----------A 969
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 294862453 1243 LEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQE 1287
Cdd:TIGR02169 970 LEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
895-1325 |
1.45e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.31 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 895 QKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYR------DAVEEKLAKLQKHNSEL 968
Cdd:PRK02224 191 QLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEerreelETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 969 ETQKEQIQLKLQEKTEELKEKMDNLTKQL----FDDV--------------QKEERQRMLLEKSfeLKTQDYEKQIQSLK 1030
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDLLaeagLDDAdaeavearreeledRDEELRDRLEECR--VAAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1031 EEIKALKDEKMQLQHlvEGEHVTSDGLKAEVArLSKQVKTISEFEKEIELLQAQKIDVE---KHVQSQKREMREKMSEIT 1107
Cdd:PRK02224 349 EDADDLEERAEELRE--EAAELESELEEAREA-VEDRREEIEELEEEIEELRERFGDAPvdlGNAEDFLEELREERDELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1108 KQLLE-SYDIEDVRSRlsVEDLEHLNEDG---ELWFAYEGLKKATRVLEShfQSQKDCYEKEIEALNFKVVHLSQEINHL 1183
Cdd:PRK02224 426 EREAElEATLRTARER--VEEAEALLEAGkcpECGQPVEGSPHVETIEED--RERVEELEAELEDLEEEVEEVEERLERA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1184 QKLFREENDIN--ESIRHEVTRLTSENMMIPDFKQ-QISELEKQKQDLEirlNEQAEKmkgklEELSNQLHRSQEEEGTQ 1260
Cdd:PRK02224 502 EDLVEAEDRIErlEERREDLEELIAERRETIEEKReRAEELRERAAELE---AEAEEK-----REAAAEAEEEAEEAREE 573
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 294862453 1261 RKALEAQNEIHTKEKEKLiDKIQEMQEASDHLKKQFETESEVKCNF--RQEASRLTLEN-----RDLEEELD 1325
Cdd:PRK02224 574 VAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALaeLNDERRERLAEkrerkRELEAEFD 644
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
890-1337 |
3.85e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.64 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 890 RVQRLQKKLEDQNKenhglVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKR---YRDAVEEKLAKLQKHNS 966
Cdd:PTZ00121 1379 KADAAKKKAEEKKK-----ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAdeaKKKAEEAKKADEAKKKA 1453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 967 ELETQKEQIQLKLQE--KTEELKEKMDNLTKQlfDDVQKEERQRMllEKSFELKTQDYEKQiqslKEEIKALKDEKMQLQ 1044
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEakKADEAKKKAEEAKKA--DEAKKKAEEAK--KKADEAKKAAEAKK----KADEAKKAEEAKKAD 1525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1045 HLVEGEhvtsDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDV--EKHVQSQKREMREKMSEITKQLlESYDIEDVRSR 1122
Cdd:PTZ00121 1526 EAKKAE----EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKaeEAKKAEEDKNMALRKAEEAKKA-EEARIEEVMKL 1600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1123 LSVEDL---EHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDinesirh 1199
Cdd:PTZ00121 1601 YEEEKKmkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED------- 1673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1200 evtrltsenmmipdfKQQISELEKQKQDLeiRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLI 1279
Cdd:PTZ00121 1674 ---------------KKKAEEAKKAEEDE--KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 294862453 1280 DKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRD----LEEELDMKDRVIKKLQDQ 1337
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEkeavIEEELDEEDEKRRMEVDK 1798
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
894-1347 |
1.31e-13 |
|
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: 76.21 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 894 LQKKLEDQNKENHGLVEKLTSLAalragdvEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKE 973
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQ-------QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 974 QIQlKLQEKTEELK-EKMDNLTKQLFDDVQKEERQRMLLEKsfelKTQDYEKQIQSLKEEIKALKDEKMQLQHlvegehv 1052
Cdd:TIGR04523 289 QLN-QLKSEISDLNnQKEQDWNKELKSELKNQEKKLEEIQN----QISQNNKIISQLNEQISQLKKELTNSES------- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1053 TSDGLKAEVARLSKQVKTI----SEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVE-- 1126
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLkkenQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETii 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1127 -------DLEhlNEDGELWFAYEGLKKATRVLESHFQSQKDCY-----------------EKEIEALNFKVVHLSQEINH 1182
Cdd:TIGR04523 437 knnseikDLT--NQDSVKELIIKNLDNTRESLETQLKVLSRSInkikqnleqkqkelkskEKELKKLNEEKKELEEKVKD 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1183 L-----------QKLFREEN-------DINESIRHEVTRLTSENM--MIPDFKQQISELeKQKQDLEIRLNEQAEKMKGK 1242
Cdd:TIGR04523 515 LtkkisslkekiEKLESEKKekeskisDLEDELNKDDFELKKENLekEIDEKNKEIEEL-KQTQKSLKKKQEEKQELIDQ 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1243 LEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEE 1322
Cdd:TIGR04523 594 KEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKT 673
|
490 500
....*....|....*....|....*
gi 294862453 1323 ELdmkDRVIKKLQDQVKTLSKTIGK 1347
Cdd:TIGR04523 674 KI---DDIIELMKDWLKELSLHYKK 695
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
681-1378 |
2.48e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 75.54 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 681 ISAQSYPSRWTYIEFYSRYGILMT--KQELSFSDKKEVCKVV---------LHRLIQDSNQYQfGKTKIFFRAG------ 743
Cdd:pfam15921 39 IENTSSTGTFTQIPIFPKYEVELDspRKIIAYPGKEHIERVLeeyshqvkdLQRRLNESNELH-EKQKFYLRQSvidlqt 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 744 --QVAYLEKLRLDKLRQSCVMVQKHMRGWLQRKkfLRERRAALIIQQYFRGQ-----QTVRKAITAV--ALKEAWAAIII 814
Cdd:pfam15921 118 klQEMQMERDAMADIRRRESQSQEDLRNQLQNT--VHELEAAKCLKEDMLEDsntqiEQLRKMMLSHegVLQEIRSILVD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 815 QKHCRGylvRSLYQLIRMATITMQAYSRGFlarrryRKMLEEHKAVILQKYARAWLARRRFQSIRRFVLN---IQLTYRV 891
Cdd:pfam15921 196 FEEASG---KKIYEHDSMSTMHFRSLGSAI------SKILRELDTEISYLKGRIFPVEDQLEALKSESQNkieLLLQQHQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 892 QRLQKKLEDQNKENHGLVEKLTSLAAlragdveKIQKLEAELEKAATHRRNYEEKGKRyrdaveeKLAKLQKHNSELETQ 971
Cdd:pfam15921 267 DRIEQLISEHEVEITGLTEKASSARS-------QANSIQSQLEIIQEQARNQNSMYMR-------QLSDLESTVSQLRSE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 972 KEQIQLKLQEKTEELKEK------------------------MDNLTKQLFDDVQKEERQrMLLEKS------------- 1014
Cdd:pfam15921 333 LREAKRMYEDKIEELEKQlvlanseltearterdqfsqesgnLDDQLQKLLADLHKREKE-LSLEKEqnkrlwdrdtgns 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1015 -----FELKTQDYEKQIQSLKEEIKALKDE-KMQLQHLVEGEHVTSDGLKaEVARLSKQVKTISE-FEKEIELLQAQKI- 1086
Cdd:pfam15921 412 itidhLRRELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEmLRKVVEELTAKKMt 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1087 ---------DVEKHVQSQKREMREKMSEITKqllesydiedVRSR--LSVEDLEHLNEDGElwfayeglkkatrvlesHF 1155
Cdd:pfam15921 491 lessertvsDLTASLQEKERAIEATNAEITK----------LRSRvdLKLQELQHLKNEGD-----------------HL 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1156 QS-QKDCYEKEIE-ALNFKVVH-LSQEINHLQKLFREENDINESIRHEVTRLTSE----NMMIPDFK-------QQISEL 1221
Cdd:pfam15921 544 RNvQTECEALKLQmAEKDKVIEiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEindrRLELQEFKilkdkkdAKIREL 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1222 EKQKQDLEIR----LNEQAEKMKGkLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFE 1297
Cdd:pfam15921 624 EARVSDLELEkvklVNAGSERLRA-VKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLK 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1298 T-ESEVkcnfrqEASRLTLENRD------------LEEELDMKDRVIKKLQDQVKTLSKTIGKANDvhsssgPKEYLgml 1364
Cdd:pfam15921 703 SaQSEL------EQTRNTLKSMEgsdghamkvamgMQKQITAKRGQIDALQSKIQFLEEAMTNANK------EKHFL--- 767
|
810
....*....|....
gi 294862453 1365 qykREDEAKLIQNL 1378
Cdd:pfam15921 768 ---KEEKNKLSQEL 778
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
922-1352 |
3.36e-13 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 74.76 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 922 DVEKIQKLEAELEKAAThrrNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTE-------ELKEKMDNLT 994
Cdd:pfam05483 220 DHEKIQHLEEEYKKEIN---DKEKQVSLLLIQITEKENKMKDLTFLLEESRDKAN-QLEEKTKlqdenlkELIEKKDHLT 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 995 KQLfDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDE--KMQLQH-LVEGEHVTS-----DGLKAEVARLSK 1066
Cdd:pfam05483 296 KEL-EDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEElnKAKAAHsFVVTEFEATtcsleELLRTEQQRLEK 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1067 ---QVKTIS-EFEKEI-ELLQAQKIDVEKHVQSQkrEMREKMSEITKQLLESYDIEDVRSRLSvedlehlNEDGELWFAY 1141
Cdd:pfam05483 375 nedQLKIITmELQKKSsELEEMTKFKNNKEVELE--ELKKILAEDEKLLDEKKQFEKIAEELK-------GKEQELIFLL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1142 EGLKK----------ATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHL----QKLFREENDINESIRHEVTRLTSE 1207
Cdd:pfam05483 446 QAREKeihdleiqltAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLllenKELTQEASDMTLELKKHQEDIINC 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1208 NMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEeegtqrKALEAQNEIHTKEKEKLIdkiqeMQE 1287
Cdd:pfam05483 526 KKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEE------NARSIEYEVLKKEKQMKI-----LEN 594
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 294862453 1288 ASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVH 1352
Cdd:pfam05483 595 KCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNY 659
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
886-1284 |
4.10e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.09 E-value: 4.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 886 QLTYRVQRLQKKLEDQNKEnhgLVEKLTSLAALRAgDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHN 965
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKA---LAELRKELEELEE-ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 966 SELETQKEQIQLKLQEKTEELKEKMDNLTKQlfddvqkeerqrmlleksfELKTQDYEKQIQSLKEEIKALKDEKMQLQh 1045
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEEL-------------------EAQIEQLKEELKALREALDELRAELTLLN- 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1046 lvEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEkHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSV 1125
Cdd:TIGR02168 817 --EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA-AEIEELEELIEELESELEALLNERASLEEALALLR 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1126 EDLEHLNEDgelwfayeglkkaTRVLESHFQSQKDCYE---KEIEALNFKVVHLSQEINHLQKLFREENDIN--ESIRHE 1200
Cdd:TIGR02168 894 SELEELSEE-------------LRELESKRSELRRELEelrEKLAQLELRLEGLEVRIDNLQERLSEEYSLTleEAEALE 960
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1201 VTRLTSENmmipDFKQQISELEKQKQDL-EIRLN--EQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEK 1277
Cdd:TIGR02168 961 NKIEDDEE----EARRRLKRLENKIKELgPVNLAaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKD 1036
|
....*..
gi 294862453 1278 LIDKIQE 1284
Cdd:TIGR02168 1037 TFDQVNE 1043
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
891-1341 |
1.30e-12 |
|
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: 73.29 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 891 VQRLQKKLEdQNKENHGLVEKltSLAALRAGDVEkiqkLEAELEKAATHRRNYEEKGKRyrdaVEEKLAKLQKHNSELET 970
Cdd:pfam01576 358 LEELTEQLE-QAKRNKANLEK--AKQALESENAE----LQAELRTLQQAKQDSEHKRKK----LEGQLQELQARLSESER 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 971 QKEQiqlkLQEKTEELKEKMDNLTKQLfddvQKEERQRMLLEK---SFELKTQDYEKQIQ-------SLKEEIKALKDEK 1040
Cdd:pfam01576 427 QRAE----LAEKLSKLQSELESVSSLL----NEAEGKNIKLSKdvsSLESQLQDTQELLQeetrqklNLSTRLRQLEDER 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1041 MQLQHLVEGEHVTSDGLKAEVARLSKQV----KTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITK-------- 1108
Cdd:pfam01576 499 NSLQEQLEEEEEAKRNVERQLSTLQAQLsdmkKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKlektknrl 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1109 -QLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKAtRVLESHFQSQKDCYEKEIEALNfkvvhLSQEINHLQKLF 1187
Cdd:pfam01576 579 qQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISA-RYAEERDRAEAEAREKETRALS-----LARALEEALEAK 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1188 REENDINESIRHEVTRLTSENmmiPDFKQQISELEKQKQDLEirlnEQAEKMKGKLEELSNQLHRSQE-----EEGTQrk 1262
Cdd:pfam01576 653 EELERTNKQLRAEMEDLVSSK---DDVGKNVHELERSKRALE----QQVEEMKTQLEELEDELQATEDaklrlEVNMQ-- 723
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1263 ALEAQNE--IHTKE------KEKLIDKIQEMQEASDHLKKQFETESEVKcnfrqeaSRLTLENRDLEEELDM----KDRV 1330
Cdd:pfam01576 724 ALKAQFErdLQARDeqgeekRRQLVKQVRELEAELEDERKQRAQAVAAK-------KKLELDLKELEAQIDAankgREEA 796
|
490
....*....|....
gi 294862453 1331 IK---KLQDQVKTL 1341
Cdd:pfam01576 797 VKqlkKLQAQMKDL 810
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
879-1288 |
2.01e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.11 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 879 RRFVLNIQltyRVQRLQKKLEDQNKENHGLVEKLTSLAALRagdvEKIQKLEAELEKAATHRRNYEEKGKRYRDAveEKL 958
Cdd:COG4717 64 RKPELNLK---ELKELEEELKEAEEKEEEYAELQEELEELE----EELEELEAELEELREELEKLEKLLQLLPLY--QEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 959 AKLQKHNSELETQKEQIQLKLQEkTEELKEKMDNLTKQLfddvQKEERQrmlLEKSFELKTQDYEKQIQSLKEEIKALKD 1038
Cdd:COG4717 135 EALEAELAELPERLEELEERLEE-LRELEEELEELEAEL----AELQEE---LEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1039 EKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEK-------------------------------------EIELL 1081
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaallallglggsllsliltiagvlflVLGLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1082 QAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHF-QSQKD 1160
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEeELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1161 CYEKEIEAL-NFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENmmiPDFKQQISELEKQkqdleiRLNEQAEKM 1239
Cdd:COG4717 367 ELEQEIAALlAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELL---GELEELLEALDEE------ELEEELEEL 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 294862453 1240 KGKLEELSNQLHRSQEEEGT---QRKALEAQNEIHTK--EKEKLIDKIQEMQEA 1288
Cdd:COG4717 438 EEELEELEEELEELREELAEleaELEQLEEDGELAELlqELEELKAELRELAEE 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
914-1287 |
2.36e-12 |
|
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: 72.40 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 914 SLAALRAGDVEKI-----QKLEAELEKAA---THRRNYEEKGKRYRDAvEEKLAKLQKHNSELETQKEQIQL------KL 979
Cdd:TIGR02168 137 SYSIIEQGKISEIieakpEERRAIFEEAAgisKYKERRKETERKLERT-RENLDRLEDILNELERQLKSLERqaekaeRY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 980 QEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKA 1059
Cdd:TIGR02168 216 KELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1060 EVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLE-SYDIEDVRSRLSVedlehlnedgelw 1138
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElKEELESLEAELEE------------- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1139 fayegLKKATRVLESHFQSQkdcyEKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSEnmmIPDFKQQI 1218
Cdd:TIGR02168 363 -----LEAELEELESRLEEL----EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE---IEELLKKL 430
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294862453 1219 SELEKQKQDLEI-RLNEQAEKMKGKLEELSNQLHRSQEE-EGTQRKALEAQNEIHTKEKEklIDKIQEMQE 1287
Cdd:TIGR02168 431 EEAELKELQAELeELEEELEELQEELERLEEALEELREElEEAEQALDAAERELAQLQAR--LDSLERLQE 499
|
|
| Myo5p-like_CBD_afadin |
cd15471 |
cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and ... |
1396-1702 |
2.56e-12 |
|
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: 70.03 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1396 PAHILFMCVRYADSLND---------ANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSNTCHFLNCLKQysgeeefmk 1466
Cdd:cd15471 25 PAYTLYLAARYRLSTHYrpeltpterAHKLTAFLNKIASLIQQVIQEQRNIAGALAFWMANASELLNFLKQ--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1467 hnspqqnknclnNFDLSEYR----QILSDVAIRIYHQFIIIMEKNIQPIIVPGMLEYESLQGISGlkptgfrkrsssIDD 1542
Cdd:cd15471 96 ------------DRDLSAFSvqaqDVLAEAVQSAFSYLVRCLQEELERSLPAFLDSLVSLDDEPA------------IGD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1543 tdgytmtsVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKD--MCSCRKGMQIRCNISYLEEWLKDK 1620
Cdd:cd15471 152 --------VLHTLSSAMRLLRRCRVNAALTIQLFSQLFHFINAWLFNSLVSNPDsgLCTRYWGKRLRQRLAHVEAWAERQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1621 NLQnsLAKET-LEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPiDDFEKRVTPSFVRKVQALLNSRE 1699
Cdd:cd15471 224 GLE--LAADChLDRIVQAANLLTAPKYSAEDVANLSSTCFKLNSLQLRALLSHYQP-PPGEPPIPPDLIERVVRLAESQA 300
|
...
gi 294862453 1700 DSS 1702
Cdd:cd15471 301 DEL 303
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
875-1296 |
5.86e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 5.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 875 FQSIRRFVLNIQLTYRVQRLQKK-----------LEDQNKENHGLVEKLTSLAALRagdvEKIQKLEAELEKAATHRRNY 943
Cdd:COG4717 39 LLAFIRAMLLERLEKEADELFKPqgrkpelnlkeLKELEEELKEAEEKEEEYAELQ----EELEELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 944 EEKGKRYRDAVE--EKLAKLQKHNSELETQKEQIQlKLQEKTEELKEKMDNLtKQLFDDVQKEERQrmlLEKSFELKTQD 1021
Cdd:COG4717 115 REELEKLEKLLQllPLYQELEALEAELAELPERLE-ELEERLEELRELEEEL-EELEAELAELQEE---LEELLEQLSLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1022 YEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEK------------------------- 1076
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaallallglggsll 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1077 ------------EIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGL 1144
Cdd:COG4717 270 sliltiagvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1145 KKATRVLESHF-QSQKDCYEKEIEAL-NFKVVHLSQEINHLQKLFREENDINE---SIRHEVTRLTSENMMIPDF----- 1214
Cdd:COG4717 350 QELLREAEELEeELQLEELEQEIAALlAEAGVEDEEELRAALEQAEEYQELKEeleELEEQLEELLGELEELLEAldeee 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1215 -KQQISELEKQKQDLEIRLNEQAEKmKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQE--MQEASDH 1291
Cdd:COG4717 430 lEEELEELEEELEELEEELEELREE-LAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALelLEEAREE 508
|
....*
gi 294862453 1292 LKKQF 1296
Cdd:COG4717 509 YREER 513
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
892-1378 |
1.05e-11 |
|
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: 70.38 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 892 QRLQKKLEDQNKENHGLVEKLTSLaalragdvEKIQKLEAELEKAaTHRRNYEEKGKRY---RDAVEEKLAKLQKHNSEL 968
Cdd:TIGR00618 246 TQKREAQEEQLKKQQLLKQLRARI--------EELRAQEAVLEET-QERINRARKAAPLaahIKAVTQIEQQAQRIHTEL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 969 ETQKEQIQLKLQEKTEELKEKMD-----NLTKQLF---------DDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIK 1034
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKQQSSieeqrRLLQTLHsqeihirdaHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQ 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1035 ALKDEKMQL---QHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLL 1111
Cdd:TIGR00618 397 SLCKELDILqreQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1112 ESYDIEDVRSRLSVEDLEHLNEDGELwfaYEGLKKATRVLESHFQ----SQKDC---------YEKEIEALNFKVVHLSQ 1178
Cdd:TIGR00618 477 TKEQIHLQETRKKAVVLARLLELQEE---PCPLCGSCIHPNPARQdidnPGPLTrrmqrgeqtYAQLETSEEDVYHQLTS 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1179 EINHLQKLFREEndinESIRHEVTRLTSenmMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEG 1258
Cdd:TIGR00618 554 ERKQRASLKEQM----QEIQQSFSILTQ---CDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1259 TQRKALEAQNEIHTKEKEKL------IDKIQEMQEASDHLKKQFETES-EVKCNFRQEASRLTLENRDLEEELDMKDRVI 1331
Cdd:TIGR00618 627 LQDVRLHLQQCSQELALKLTalhalqLTLTQERVREHALSIRVLPKELlASRQLALQKMQSEKEQLTYWKEMLAQCQTLL 706
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 294862453 1332 KKLQDQVKTLSKTIGKANDVHSSSGPKeylgmLQYKREDEAKLIQNL 1378
Cdd:TIGR00618 707 RELETHIEEYDREFNEIENASSSLGSD-----LAAREDALNQSLKEL 748
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
962-1350 |
2.41e-11 |
|
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: 68.93 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 962 QKHNSELETQKEQiqLKLQEKTEELKEKMDNLTKQLfDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKM 1041
Cdd:TIGR02168 667 KTNSSILERRREI--EELEEKIEELEEKIAELEKAL-AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1042 QLQHLVEGEHVTSDGLKAEV----ARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITkqlLESYDIE 1117
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIeeleERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT---LLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1118 DVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLEShfqsqkdcYEKEIEALNFKVVHLSQEINHLQKLFREENDINESI 1197
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIES--------LAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1198 RHEVTRLTSEnmmipdfkqqISELEKQKQDLE---IRLNEQAEKMKGKLEELSNQLhRSQEEEGTQRKALEAqnEIHTKE 1274
Cdd:TIGR02168 893 RSELEELSEE----------LRELESKRSELRrelEELREKLAQLELRLEGLEVRI-DNLQERLSEEYSLTL--EEAEAL 959
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294862453 1275 KEKLIDKIQEMQEASDHLKKQFETESEVkcNFRQEAsrltlENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKAND 1350
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRLENKIKELGPV--NLAAIE-----EYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
772-1350 |
3.30e-11 |
|
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: 68.54 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 772 QRKKFLRERRAALIIQQYFRG---QQTVRKAITAVALKEAWAAIIIQkhcrgylVRSLYQLIRMATITMQAYSRGFLARR 848
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEaqlEELESKLDELAEELAELEEKLEE-------LKEELESLEAELEELEAELEELESRL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 849 R-YRKMLEEHKAVILQKYARAWLARRRFQSIRRfvlniqltyRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGdvEKIQ 927
Cdd:TIGR02168 375 EeLEEQLETLRSKVAQLELQIASLNNEIERLEA---------RLERLEDRRERLQQEIEELLKKLEEAELKELQ--AELE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 928 KLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQK------EQIQLKLQEKTEELKEKMDN------LTK 995
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslERLQENLEGFSEGVKALLKNqsglsgILG 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 996 QLFDDVQKEERQRMLLEKSFELKTQDYE-KQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAE-----------VAR 1063
Cdd:TIGR02168 524 VLSELISVDEGYEAAIEAALGGRLQAVVvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNdreilkniegfLGV 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1064 LSKQVKTISEFEKEIELLQAQKIDVE--KHVQSQKREMREKMSEITKqllesyDIEDVRSRLSV------EDLEHLNEDG 1135
Cdd:TIGR02168 604 AKDLVKFDPKLRKALSYLLGGVLVVDdlDNALELAKKLRPGYRIVTL------DGDLVRPGGVItggsakTNSSILERRR 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1136 ELwfayEGLKKATRVLESHFQSQK---DCYEKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSenmMIP 1212
Cdd:TIGR02168 678 EI----EELEEKIEELEEKIAELEkalAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE---RIA 750
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1213 DFKQQISELEKQKQDLEIRLNEQAEKMK---GKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLID---KIQEMQ 1286
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAeaeAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANlreRLESLE 830
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 294862453 1287 EASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKAND 1350
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
873-1137 |
4.82e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 4.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 873 RRFQSIRRFVLNIQLTYRVQRLQKKLEDQNKENhglvEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRD 952
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELE----AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 953 AVEEKLAKLQKHNSELETQKEQIQ------LKLQEKTEELKEKMDNLTKQL---FDDVQKEERQRMLLEKSFELKTQDYE 1023
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRReleerlEELEEELAELEEELEELEEELeelEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1024 KQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKM 1103
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270
....*....|....*....|....*....|....
gi 294862453 1104 SEITKQLLESYDIEDVRSRLSVEDLEHLNEDGEL 1137
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
847-1345 |
7.95e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 847 RRRYRKMLEEHKAVILQKYARAWLARRRFQSIRRFVLNIQLtyRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKI 926
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELEL--ELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 927 QKLEAELEKAATHRRNYEEKgkryRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLtkqlfDDVQKEER 1006
Cdd:COG1196 319 EELEEELAELEEELEELEEE----LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL-----EELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1007 QRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKI 1086
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1087 DVEKHVQSQKREMREKMSE------ITKQLLESYD--IEDVRSRLSVEDLEHLNEDGELW----FAYEGL---------- 1144
Cdd:COG1196 470 EEAALLEAALAELLEELAEaaarllLLLEAEADYEgfLEGVKAALLLAGLRGLAGAVAVLigveAAYEAAleaalaaalq 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1145 -------------------KKATRV----LESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEV 1201
Cdd:COG1196 550 nivveddevaaaaieylkaAKAGRAtflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1202 TRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEiHTKEKEKLIDK 1281
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE-ALLAEEEEERE 708
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 294862453 1282 IQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDR----VIKKLQDQVKTLSKTI 1345
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELpeppDLEELERELERLEREI 776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
849-1185 |
1.36e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.63 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 849 RYRKMLEEhkaviLQKYaRAWLARRRFQSIRRfvlniqltyRVQRLQKKLEDQNKEnhglVEKLTslaalragdvEKIQK 928
Cdd:TIGR02169 212 RYQALLKE-----KREY-EGYELLKEKEALER---------QKEAIERQLASLEEE----LEKLT----------EEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 929 LEAELEKAathRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELkEKMDNLTKQLFddvqkEERQR 1008
Cdd:TIGR02169 263 LEKRLEEI---EQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL-EDAEERLAKLE-----AEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1009 MLLEK-SFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKID 1087
Cdd:TIGR02169 334 LLAEIeELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1088 VEKHVQSQKREMREKMSEITKQLLEsydiedVRSRLSVEDLEhlnedgelwfayegLKKATRVLEShFQSQKDCYEKEIE 1167
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINE------LEEEKEDKALE--------------IKKQEWKLEQ-LAADLSKYEQELY 472
|
330
....*....|....*...
gi 294862453 1168 ALNFKVVHLSQEINHLQK 1185
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQR 490
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
966-1345 |
1.40e-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: 66.53 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 966 SELETQKEQIQLKLQEKTEELKEKMDNLTkqlfddvqKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEkmQLQH 1045
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLE--------ELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD--YLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1046 LVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLEsYDIEDVRSRLSV 1125
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE-LLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1126 EDLEHLNEDGELwfaYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQ--------EINHLQKLFREENDINESI 1197
Cdd:pfam02463 314 EKLKESEKEKKK---AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKlqekleqlEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1198 rhevtRLTSENMMIPDFKQQISELEKQ--KQDLEIRLNEQAEKMKGKLEELSnqlhrsqEEEGTQRKALEAQNEIHTKEK 1275
Cdd:pfam02463 391 -----KLKEEELELKSEEEKEAQLLLElaRQLEDLLKEEKKEELEILEEEEE-------SIELKQGKLTEEKEELEKQEL 458
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1276 EKLIDKIQEMQEASDHLKKQfETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTI 1345
Cdd:pfam02463 459 KLLKDELELKKSEDLLKETQ-LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISA 527
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
888-1253 |
1.43e-10 |
|
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: 66.03 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 888 TYRVQRLQKKLEDqnkenhglVEKLTSLAAlraGDVEKIQK-LEAELEKAATHRRNYEEKGKRYR--------------- 951
Cdd:pfam06160 78 KYRFKKAKKALDE--------IEELLDDIE---EDIKQILEeLDELLESEEKNREEVEELKDKYRelrktllanrfsygp 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 952 --DAVEEKLAKLQKHNSELETQKEQ--------IQLKLQEKTEELKEKMDNLtKQLFDDVQKE---------ERQRMLLE 1012
Cdd:pfam06160 147 aiDELEKQLAEIEEEFSQFEELTESgdyleareVLEKLEEETDALEELMEDI-PPLYEELKTElpdqleelkEGYREMEE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1013 KSFELKTQDYEKQIQSLKEEIKALkdekmqLQHLVEGEhvtSDGLKAEVARLSKQVKTISE-FEKEIEllqaQKIDVEKH 1091
Cdd:pfam06160 226 EGYALEHLNVDKEIQQLEEQLEEN------LALLENLE---LDEAEEALEEIEERIDQLYDlLEKEVD----AKKYVEKN 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1092 vQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHlnedgelwfayeglkkaTRVLESHFQSQKDCYEKEIEALNF 1171
Cdd:pfam06160 293 -LPEIEDYLEHAEEQNKELKEELERVQQSYTLNENELER-----------------VRGLEKQLEELEKRYDEIVERLEE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1172 KVVHLSQEINHLQKLFREENDINEsiRHEvtrltsenmmipDFKQQISELEKQkqdlEIRLNEQAEKMKGKLEELSNQLH 1251
Cdd:pfam06160 355 KEVAYSELQEELEEILEQLEEIEE--EQE------------EFKESLQSLRKD----ELEAREKLDEFKLELREIKRLVE 416
|
..
gi 294862453 1252 RS 1253
Cdd:pfam06160 417 KS 418
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
891-1265 |
2.89e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 65.76 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 891 VQRLQKKLEDQNKEnhgLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELET 970
Cdd:pfam02463 164 GSRLKRKKKEALKK---LIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 971 QKEQIQLKLQEKTEELKEKMDNlTKQLFDDVQKEERQrmlleksfelktqdyEKQIQSLKEEIKALKD-----EKMQLQH 1045
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEK-EEEKLAQVLKENKE---------------EEKEKKLQEEELKLLAkeeeeLKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1046 LVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSv 1125
Cdd:pfam02463 305 LERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1126 edlehlnedgelwfayeglkkatrvleSHFQSQKDCYEKEIEALNFKVvhlsQEINHLQKLFREENDINESIRHEVTRLT 1205
Cdd:pfam02463 384 ---------------------------ERLSSAAKLKEEELELKSEEE----KEAQLLLELARQLEDLLKEEKKEELEIL 432
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 294862453 1206 SENMMIPDFKQQISELEKQKQDL----EIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALE 1265
Cdd:pfam02463 433 EEEEESIELKQGKLTEEKEELEKqelkLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
988-1347 |
3.36e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 988 EKMDNLTKQL--FDDVQKEERQRMLLEKSFELKTQDYEKQIQS---LKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVA 1062
Cdd:PRK03918 145 ESREKVVRQIlgLDDYENAYKNLGEVIKEIKRRIERLEKFIKRtenIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1063 RLSKQVKTISEFEKEIELLQAQKIDVEKHvqsqKREMREKMSEITKQLLES-YDIEDVRSRlsVEDLEHLNEDGELWFAY 1141
Cdd:PRK03918 225 KLEKEVKELEELKEEIEELEKELESLEGS----KRKLEEKIRELEERIEELkKEIEELEEK--VKELKELKEKAEEYIKL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1142 EGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREEndinESIRHEVTRLTSENMMIPDFKQQISEL 1221
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL----KELEKRLEELEERHELYEEAKAKKEEL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1222 EKQKQDLEirlNEQAEKMKGKLEELSNqlhrsqeeegtqrkaleAQNEIhTKEKEKLIDKIQEMQEASDHLKKQFE--TE 1299
Cdd:PRK03918 375 ERLKKRLT---GLTPEKLEKELEELEK-----------------AKEEI-EEEISKITARIGELKKEIKELKKAIEelKK 433
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 294862453 1300 SEVKC---------NFRQE-ASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGK 1347
Cdd:PRK03918 434 AKGKCpvcgrelteEHRKElLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
924-1345 |
3.69e-10 |
|
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: 65.20 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 924 EKIQKLEAEL--EKAATHRRNYEE-----KGKRyrdaVEEKLAKLQKHNSELETQKEQIQLKLQEKTEEL---KEKMDNL 993
Cdd:pfam01576 103 QHIQDLEEQLdeEEAARQKLQLEKvtteaKIKK----LEEDILLLEDQNSKLSKERKLLEERISEFTSNLaeeEEKAKSL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 994 TK----------QLFDDVQKEERQRMLLEKS---FELKTQDYEKQIQSLKEEIKALKdekMQLQHlvegehvTSDGLKAE 1060
Cdd:pfam01576 179 SKlknkheamisDLEERLKKEEKGRQELEKAkrkLEGESTDLQEQIAELQAQIAELR---AQLAK-------KEEELQAA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1061 VARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQkREMREKMSEITKQLLEsyDIEDVRSRLsvED-LEHLNEDGELWF 1139
Cdd:pfam01576 249 LARLEEETAQKNNALKKIRELEAQISELQEDLESE-RAARNKAEKQRRDLGE--ELEALKTEL--EDtLDTTAAQQELRS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1140 AYEG----LKKA----TRVLESHFQSQKDCYEKEIEALN--------FKVV------HLSQEINHLQKLFREENDINESI 1197
Cdd:pfam01576 324 KREQevteLKKAleeeTRSHEAQLQEMRQKHTQALEELTeqleqakrNKANlekakqALESENAELQAELRTLQQAKQDS 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1198 RHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNE---QAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEI---H 1271
Cdd:pfam01576 404 EHKRKKLEGQ---LQELQARLSESERQRAELAEKLSKlqsELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELlqeE 480
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 294862453 1272 TKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTI 1345
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL 554
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
955-1294 |
5.98e-10 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 64.58 E-value: 5.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 955 EEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLfddvqkeeRQRML-LEKS---FELKTQDYEKQIQSLK 1030
Cdd:pfam15818 27 EEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAVFKKQL--------QMKMCaLEEEkgkYQLATEIKEKEIEGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1031 EEIKALKDEKMQLQhlvegehvtsdglkaevarlskqvKTISEFEKEIELLQAQKIDVEKhvqsQKREMREKMSEITKQL 1110
Cdd:pfam15818 99 ETLKALQVSKYSLQ------------------------KKVSEMEQKLQLHLLAKEDHHK----QLNEIEKYYATITGQF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1111 ---------LESYDIEDVR--SRLSVedlehLNE--DGELWFAYEGLKKATRVL-ESHFQSQkdcYEKEIEALNFKVVHl 1176
Cdd:pfam15818 151 glvkenhgkLEQNVQEAIQlnKRLSA-----LNKkqESEICSLKKELKKVTSDLiKSKVTCQ---YKMGEENINLTIKE- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1177 sQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQ--AEKMKGKLEELSNQLHRSQ 1254
Cdd:pfam15818 222 -QKFQELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAElkALKENNQTLERDNELQREK 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 294862453 1255 EEEgTQRKALEAQNEiHTK-------EKEKLIDKIQEMQEASDHLKK 1294
Cdd:pfam15818 301 VKE-NEEKFLNLQNE-HEKalgtwkkHVEELNGEINEIKNELSSLKE 345
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
928-1383 |
6.25e-10 |
|
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: 64.37 E-value: 6.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 928 KLEAELEkaaTHRRNYEEKGKRYRDAVEEKLA--------KLQKHNSELETQK---EQIQLKLQEKTEELKEKMDNLTkq 996
Cdd:pfam15921 56 KYEVELD---SPRKIIAYPGKEHIERVLEEYShqvkdlqrRLNESNELHEKQKfylRQSVIDLQTKLQEMQMERDAMA-- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 997 lfdDVQKEERQrmlleksfelKTQDYEKQIQSLKEEIKA---LKDE-------------KMQLQH---LVEGEHVTSDGL 1057
Cdd:pfam15921 131 ---DIRRRESQ----------SQEDLRNQLQNTVHELEAakcLKEDmledsntqieqlrKMMLSHegvLQEIRSILVDFE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1058 KAEVARLSKQ---------------VKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQ-------LLESYD 1115
Cdd:pfam15921 198 EASGKKIYEHdsmstmhfrslgsaiSKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQhqdrieqLISEHE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1116 IE----------------DVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVV----- 1174
Cdd:pfam15921 278 VEitgltekassarsqanSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVlanse 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1175 ---------HLSQEI----NHLQKLF-------------REEN------DINESIR--HEVTRLTSENMMIP-------- 1212
Cdd:pfam15921 358 ltearterdQFSQESgnldDQLQKLLadlhkrekelsleKEQNkrlwdrDTGNSITidHLRRELDDRNMEVQrleallka 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1213 -------DFKQQISELEKQKQDLE------IRLNEQAEKMKGKLEELSNQLHRSQEEEGT----------QRKALEAQNE 1269
Cdd:pfam15921 438 mksecqgQMERQMAAIQGKNESLEkvssltAQLESTKEMLRKVVEELTAKKMTLESSERTvsdltaslqeKERAIEATNA 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1270 IHTKEKEKLIDKIQEMQeasdHLKkqfeTESEVKCNFRQEASRLTLenrdleeELDMKDRVIKKLQDQVKTLSKTIGKan 1349
Cdd:pfam15921 518 EITKLRSRVDLKLQELQ----HLK----NEGDHLRNVQTECEALKL-------QMAEKDKVIEILRQQIENMTQLVGQ-- 580
|
570 580 590
....*....|....*....|....*....|....
gi 294862453 1350 dvHSSSGpkeylGMLQYKREDEAKLIQNLILDLK 1383
Cdd:pfam15921 581 --HGRTA-----GAMQVEKAQLEKEINDRRLELQ 607
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1012-1357 |
1.02e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1012 EKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQvktISEFEKEIELLQAQkidvekh 1091
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK---IGEIEKEIEQLEQE------- 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1092 vqsqkremREKMSEItkqllesydIEDVRSRLSVEDLEHLNEDGELwfayeglkkatrvleshfqsqkDCYEKEIEALNF 1171
Cdd:TIGR02169 732 --------EEKLKER---------LEELEEDLSSLEQEIENVKSEL----------------------KELEARIEELEE 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1172 KVVHLSQEINHLqklfreENDINESIRHEVTRLTSEnmmipdFKQQISELEKQKQDLEIRLNEQAEKmKGKLEELSNQLH 1251
Cdd:TIGR02169 773 DLHKLEEALNDL------EARLSHSRIPEIQAELSK------LEEEVSRIEARLREIEQKLNRLTLE-KEYLEKEIQELQ 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1252 RSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFEtesevkcNFRQEASRLTLENRDLEEELDMKDRVI 1331
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG-------DLKKERDELEAQLRELERKIEELEAQI 912
|
330 340
....*....|....*....|....*.
gi 294862453 1332 KKLQDQVKTLSKTIGKANDVHSSSGP 1357
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSEIED 938
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
953-1322 |
1.32e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 63.45 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 953 AVEEKLAKLQKHNSE------LETQKEQIQLkLQEKTEELKEKMDNLTK---------QLFDDVQKEERQRMLLEKSFEL 1017
Cdd:TIGR00618 127 ETEEVIHDLLKLDYKtftrvvLLPQGEFAQF-LKAKSKEKKELLMNLFPldqytqlalMEFAKKKSLHGKAELLTLRSQL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1018 KTQDYEKQIQSLKEEIKALKDEKMQL----QHLVEGEHVTSDGLKAEVARLSKQvKTISEFEKEIELLQAQKIDVEKhvQ 1093
Cdd:TIGR00618 206 LTLCTPCMPDTYHERKQVLEKELKHLrealQQTQQSHAYLTQKREAQEEQLKKQ-QLLKQLRARIEELRAQEAVLEE--T 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1094 SQKREMREKMSEITkqllesydiedvrsrLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKV 1173
Cdd:TIGR00618 283 QERINRARKAAPLA---------------AHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1174 VHLSQEINHlqklFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQ----KQDLEIRLNEQAEKMKGKLEE--LS 1247
Cdd:TIGR00618 348 QTLHSQEIH----IRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKlqslCKELDILQREQATIDTRTSAFrdLQ 423
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 294862453 1248 NQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEE 1322
Cdd:TIGR00618 424 GQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLE 498
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
911-1343 |
1.48e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 911 KLTSLAALRAGDVEKIQKLEAELEKAA--THRRNYEEkgkryRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKE 988
Cdd:COG4717 36 KSTLLAFIRAMLLERLEKEADELFKPQgrKPELNLKE-----LKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 989 KMDNLTKQLfDDVQKEERQRMLLEKSFELKTQ--DYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSK 1066
Cdd:COG4717 110 ELEELREEL-EKLEKLLQLLPLYQELEALEAElaELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1067 QV-KTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEI--TKQLLESYDIEDVRSRLSV----------------ED 1127
Cdd:COG4717 189 ATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELeqLENELEAAALEERLKEARLllliaaallallglggSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1128 LEHLNEDGELWFAYEGLkkaTRVLESHFQSQKDCYEKEIEALNfKVVHLSQEINHLQKLFREENDINESIrhEVTRLTSE 1207
Cdd:COG4717 269 LSLILTIAGVLFLVLGL---LALLFLLLAREKASLGKEAEELQ-ALPALEELEEEELEELLAALGLPPDL--SPEELLEL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1208 NMMIPDFKQQISELEKQKQDLEIRLNEQaekmkgKLEELSNQLHRSQEEEgtQRKALEAQNEIHtKEKEKLIDKIQEMQE 1287
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELEQ------EIAALLAEAGVEDEEE--LRAALEQAEEYQ-ELKEELEELEEQLEE 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 294862453 1288 ASDHLKKQFETESEVKCnfRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSK 1343
Cdd:COG4717 414 LLGELEELLEALDEEEL--EEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
966-1348 |
1.78e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 966 SELETQKEQIQLKLqEKTEElkekmdNLTKqlFDDVQKE--------ERQRMLLEKSFELKTQDYEKQIQSLKEEIKALK 1037
Cdd:COG1196 168 SKYKERKEEAERKL-EATEE------NLER--LEDILGElerqleplERQAEKAERYRELKEELKELEAELLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1038 DEKMQLQHLVEGEHVTSDGLKAEVARLskqvktisefEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQllesydie 1117
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAEL----------EAELEELRLELEELELELEEAQAEEYELLAELARL-------- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1118 dvrsrlsVEDLEHLNEDgelwfayeglkkatrvlESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINESI 1197
Cdd:COG1196 301 -------EQDIARLEER-----------------RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1198 RhevtrltsenmmipdfkQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEgTQRKALEAQNEIHTKEKEK 1277
Cdd:COG1196 357 E-----------------AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA-AQLEELEEAEEALLERLER 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294862453 1278 LIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKA 1348
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
873-1329 |
1.93e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 873 RRFQSIRRFVLNIQL-----TYRVQRLQKKLEDQNKENHGLVEKLTS--------LAAL--RAGDVEKIQKLEaELE--- 934
Cdd:COG4913 496 EHYAAALRWVNRLHLrgrlvYERVRTGLPDPERPRLDPDSLAGKLDFkphpfrawLEAElgRRFDYVCVDSPE-ELRrhp 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 935 KAAT------HRRNYEEKGKRYRDA--------VEEKLAKLQKhnsELETQKEQIQlKLQEKTEELKEKMDNLTKQLfdd 1000
Cdd:COG4913 575 RAITragqvkGNGTRHEKDDRRRIRsryvlgfdNRAKLAALEA---ELAELEEELA-EAEERLEALEAELDALQERR--- 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1001 vqkeERQRMLLEKSF-ELKTQDYEKQIQSLKEEIKALKDEKMQLQHLvegehvtsdglkaevarlskqvktisefEKEIE 1079
Cdd:COG4913 648 ----EALQRLAEYSWdEIDVASAEREIAELEAELERLDASSDDLAAL----------------------------EEQLE 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1080 LLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQK 1159
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERI 775
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1160 DCYEKEIEALNFKVVHLSQEINHLQKLFREENDI----NESIRHEVTRLTSENmmIPDFKQQISELEKQ-----KQDLEI 1230
Cdd:COG4913 776 DALRARLNRAEEELERAMRAFNREWPAETADLDAdlesLPEYLALLDRLEEDG--LPEYEERFKELLNEnsiefVADLLS 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1231 RLNEQAEKMKGKLEELSNQLHRSQEEEGTqRKALEAQNEIHTKEKEKLidkiQEMQEASDHLKKQFETESEVKCNFRQEA 1310
Cdd:COG4913 854 KLRRAIREIKERIDPLNDSLKRIPFGPGR-YLRLEARPRPDPEVREFR----QELRAVTSGASLFDEELSEARFAALKRL 928
|
490 500
....*....|....*....|
gi 294862453 1311 -SRLtlenRDLEEELDMKDR 1329
Cdd:COG4913 929 iERL----RSEEEESDRRWR 944
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
892-1314 |
2.38e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 62.43 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 892 QRLQKKlEDQNK-------ENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKH 964
Cdd:pfam05483 370 QRLEKN-EDQLKiitmelqKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAR 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 965 NSE---LETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELkTQDYEKQIQSLKEEIKALKDEKM 1041
Cdd:pfam05483 449 EKEihdLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKEL-TQEASDMTLELKKHQEDIINCKK 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1042 QLQHLVegehvtsdglkaevarlskqvktisefeKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESydiEDVRS 1121
Cdd:pfam05483 528 QEERML----------------------------KQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKS---EENAR 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1122 RLSVEDLEHLNEDGELWFAYEGLKK----ATRVLESHFQSQK------DCYEKEIEALNFKVVHLSQEINHLQKLFREEN 1191
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKqienKNKNIEELHQENKalkkkgSAENKQLNAYEIKVNKLELELASAKQKFEEII 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1192 DiNESIRHEVTRLTSENMM--IPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNE 1269
Cdd:pfam05483 657 D-NYQKEIEDKKISEEKLLeeVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQ 735
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 294862453 1270 IHTKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLT 1314
Cdd:pfam05483 736 EQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
851-1286 |
4.06e-09 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 61.69 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 851 RKMLEEHKavilqkyarawlaRRRFQSIRRFVLNiQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVE------ 924
Cdd:pfam07111 131 RKNLEEGS-------------QRELEEIQRLHQE-QLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKqlaeaq 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 925 --------KIQKLEAELEKAAT-----------------HRRNYEEKGKRYRDAVEEklakLQKHNSELETQKEQIQLKL 979
Cdd:pfam07111 197 keaellrkQLSKTQEELEAQVTlveslrkyvgeqvppevHSQTWELERQELLDTMQH----LQEDRADLQATVELLQVRV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 980 QEKTEELKEKMDNLTK--QLFDDVQKE--ERQRMLL----EKSF----ELKTQDYEK---------QIQSLKEEIKALKD 1038
Cdd:pfam07111 273 QSLTHMLALQEEELTRkiQPSDSLEPEfpKKCRSLLnrwrEKVFalmvQLKAQDLEHrdsvkqlrgQVAELQEQVTSQSQ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1039 EKMQLQHL-------VEGEHVTSDGLKAEVARLS----KQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEI- 1106
Cdd:pfam07111 353 EQAILQRAlqdkaaeVEVERMSAKGLQMELSRAQearrRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIp 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1107 --TKQLleSYDIEDVRS------------RLSVE-----------------DLEHLNEDGELWFAYegLKKATRVLESHF 1155
Cdd:pfam07111 433 slSNRL--SYAVRKVHTikglmarkvalaQLRQEscpppppappvdadlslELEQLREERNRLDAE--LQLSAHLIQQEV 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1156 QSQKDCYEKEIEALNFKVVHLSQEINHLQKLF--------------REENDINESIRHEVTRltSENMMIPDFKQQISEL 1221
Cdd:pfam07111 509 GRAREQGEAERQQLSEVAQQLEQELQRAQESLasvgqqlevarqgqQESTEEAASLRQELTQ--QQEIYGQALQEKVAEV 586
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 294862453 1222 E----KQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQ 1286
Cdd:pfam07111 587 EtrlrEQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKEEGQRLARRVQELE 655
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
979-1337 |
4.69e-09 |
|
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: 61.06 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 979 LQEKTEE-LKEKMDNLTKQLFDDVQKE-ERQRMLLEK-SFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSD 1055
Cdd:pfam07888 32 LQNRLEEcLQERAELLQAQEAANRQREkEKERYKRDReQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1056 GLKAEVARLSKQ----VKTISEFEKEIELLQAQKIDVEkhvqSQKREMREKMSEITKQLLESY-DIEDVRSRL--SVEDL 1128
Cdd:pfam07888 112 ELSEEKDALLAQraahEARIRELEEDIKTLTQRVLERE----TELERMKERAKKAGAQRKEEEaERKQLQAKLqqTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1129 EHLNEDgelwfaYEGLKKATRVLESHFQSQKDcyekeiealnfKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSEN 1208
Cdd:pfam07888 188 RSLSKE------FQELRNSLAQRDTQVLQLQD-----------TITTLTQKLTTAHRKEAENEALLEELRSLQERLNASE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1209 MMIPDFKQQISELEKQKQDLEIRLNE---QAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEM 1285
Cdd:pfam07888 251 RKVEGLGEELSSMAAQRDRTQAELHQarlQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRL 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 294862453 1286 QEA-----SDHLKKQFETESEVKCNFRQEAsrltlENRDLEEELDMKDRVIKKLQDQ 1337
Cdd:pfam07888 331 EERlqeerMEREKLEVELGREKDCNRVQLS-----ESRRELQELKASLRVAQKEKEQ 382
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
983-1388 |
6.19e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 61.39 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 983 TEELKEKMDNLTKQLFDDVQKEERQrmllEKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHL-VEGEHVTSDGLKAEV 1061
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQAAA----EEQLVQANGELEKASREETFARTALKNARLDLRRLfDEKQSEKDKKNKALA 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1062 ARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSrlsvedlehlneDGELWFAY 1141
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALL------------KAAIAARR 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1142 EGLKKATRVLESHfqsqkdcYEKEIEALNF---KVVHLSQEINHL-QKLFREENDinesiRHEVTRLTsenmmipDFKQQ 1217
Cdd:pfam12128 743 SGAKAELKALETW-------YKRDLASLGVdpdVIAKLKREIRTLeRKIERIAVR-----RQEVLRYF-------DWYQE 803
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1218 ISELEKQkqdleiRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQneihTKEKEKLIDKIQEMQEASDHLKKQFE 1297
Cdd:pfam12128 804 TWLQRRP------RLATQLSNIERAISELQQQLARLIADTKLRRAKLEME----RKASEKQQVRLSENLRGLRCEMSKLA 873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1298 TESEvKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKandvHSSSGPKEYlgmLQYKREDEAKLIQN 1377
Cdd:pfam12128 874 TLKE-DANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIAD----HSGSGLAET---WESLREEDHYQNDK 945
|
410
....*....|.
gi 294862453 1378 LILDLKPRGVV 1388
Cdd:pfam12128 946 GIRLLDYRKLV 956
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1017-1350 |
8.42e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1017 LKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQK 1096
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1097 rEMREKMSEITKQLlesydiedvrsrLSVE-DLEHLNED-GELWFAYEGLKKATRVLESHfqsqkdcyEKEIEALNFKVv 1174
Cdd:PRK03918 235 -ELKEEIEELEKEL------------ESLEgSKRKLEEKiRELEERIEELKKEIEELEEK--------VKELKELKEKA- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1175 hlsQEINHLQKLFREENDINESIRHEVTRLTsenmmipdfkQQISELEKQKQDLEiRLNEQAEKMKGKLEELSNQLHRSQ 1254
Cdd:PRK03918 293 ---EEYIKLSEFYEEYLDELREIEKRLSRLE----------EEINGIEERIKELE-EKEERLEELKKKLKELEKRLEELE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1255 EEEGTQRKALEAQNEIHT-------KEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLE----------- 1316
Cdd:PRK03918 359 ERHELYEEAKAKKEELERlkkrltgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAieelkkakgkc 438
|
330 340 350
....*....|....*....|....*....|....*..
gi 294862453 1317 ---NRDLEEEldMKDRVIKKLQDQVKTLSKTIGKAND 1350
Cdd:PRK03918 439 pvcGRELTEE--HRKELLEEYTAELKRIEKELKEIEE 473
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
879-1248 |
1.07e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.36 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 879 RRFVLNIQLTYRvQRLQKKLEDQNKENHGLVEKLTSLAALragdVEKIQKLEAELEKAATHR------RNYEEKGKRYRD 952
Cdd:PRK04863 281 RRVHLEEALELR-RELYTSRRQLAAEQYRLVEMARELAEL----NEAESDLEQDYQAASDHLnlvqtaLRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 953 AVEEKLAKLQKHNSELETQKEQiQLKLQEKTEELKEKMDNLTKQLFDDVQK-EERQRMLLEksfelktqdYEKQIQSLkE 1031
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEADEQ-QEENEARAEAAEEEVDELKSQLADYQQAlDVQQTRAIQ---------YQQAVQAL-E 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1032 EIKALKD---------EKMQLQHLVEGEHVTSDGLKAEvARLSKQVKTISEFEKEIELLQAQKIDVE------------- 1089
Cdd:PRK04863 425 RAKQLCGlpdltadnaEDWLEEFQAKEQEATEELLSLE-QKLSVAQAAHSQFEQAYQLVRKIAGEVSrseawdvarellr 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1090 -----KHVQSQKREMREKMSEITKQLLESYDIEDVRSRL---------SVEDLEHLNEDGElwfayeglkkatRVLESHF 1155
Cdd:PRK04863 504 rlreqRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFckrlgknldDEDELEQLQEELE------------ARLESLS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1156 QSQKDCYEKEIEaLNFKVVHLSQEINHLQKL---FREENDINESIRHEV--TRLTSENMMipDFKQQISELEKQKQDLEI 1230
Cdd:PRK04863 572 ESVSEARERRMA-LRQQLEQLQARIQRLAARapaWLAAQDALARLREQSgeEFEDSQDVT--EYMQQLLERERELTVERD 648
|
410
....*....|....*...
gi 294862453 1231 RLNEQAEKMKGKLEELSN 1248
Cdd:PRK04863 649 ELAARKQALDEEIERLSQ 666
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
921-1347 |
2.52e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 59.14 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 921 GDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLqekteelkekmdnltkqlfdd 1000
Cdd:PRK01156 360 GYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKL--------------------- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1001 vqkeerqrmlleksfelktQDYEKQIQSLKEEIKALKDEKMQLQHLVE-----------GEHVTSDGLKAEVARLSKQVK 1069
Cdd:PRK01156 419 -------------------QDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcGTTLGEEKSNHIINHYNEKKS 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1070 TISEFEKEIElLQAQKIDvEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSvEDLEHLNEDGELWFAYEGLKKATR 1149
Cdd:PRK01156 480 RLEEKIREIE-IEVKDID-EKIVDLKKRKEYLESEEINKSINEYNKIESARADLE-DIKIKINELKDKHDKYEEIKNRYK 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1150 VLEshfqsQKDCYEKEIEALNFKVVHLSQEINHLQKLFreeNDINESIRHEVTRLTSENMMIPDFK----QQISELEKQK 1225
Cdd:PRK01156 557 SLK-----LEDLDSKRTSWLNALAVISLIDIETNRSRS---NEIKKQLNDLESRLQEIEIGFPDDKsyidKSIREIENEA 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1226 QDLEIRLNE------QAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHT--KEKEKLIDKIqemqeasdhLKKQFE 1297
Cdd:PRK01156 629 NNLNNKYNEiqenkiLIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDnlKKSRKALDDA---------KANRAR 699
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 294862453 1298 TESEVKCNfRQEASRLTLENRDLEEELDMKDRVIKKLQDqVKTLSKTIGK 1347
Cdd:PRK01156 700 LESTIEIL-RTRINELSDRINDINETLESMKKIKKAIGD-LKRLREAFDK 747
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
823-1238 |
4.52e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 823 VRSLYQLIRMATITMQAYSRGFLARRRYRKMLEEHKAVILQkyarawlARRRFQSIRRFVLNIQLTYRVQRLQKKLEDQN 902
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE-------LREELEKLEKLLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 903 KENHGLVEKLTSLAALRagdvEKIQKLEAELEKAATHRRNYEEK-GKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQE 981
Cdd:COG4717 146 ERLEELEERLEELRELE----EELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELE-EAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 982 KTEELKEKMDNLTKQLFDDVQKEERQRMLLEK-------SFELKTQDYEKQIQSLKEEIKA---------LKDEKMQLQH 1045
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLliaaallALLGLGGSLLSLILTIAGVLFLvlgllallfLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1046 LVEGEHVTSDGLKAEVARLS-KQVKTISEFEKEIELLQAQK-IDVEKHVQSQKREMREKMSEITKQLLESyDIEDVRSRL 1123
Cdd:COG4717 301 GKEAEELQALPALEELEEEElEELLAALGLPPDLSPEELLElLDRIEELQELLREAEELEEELQLEELEQ-EIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1124 SVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKvvHLSQEINHLQ-KLFREENDINEsIRHEVT 1202
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEeELEELEEELEE-LREELA 456
|
410 420 430
....*....|....*....|....*....|....*.
gi 294862453 1203 RLTSENMMIPDfKQQISELEKQKQDLEIRLNEQAEK 1238
Cdd:COG4717 457 ELEAELEQLEE-DGELAELLQELEELKAELRELAEE 491
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
890-1359 |
4.56e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.37 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 890 RVQRLQKKLEDQNKENHGLVEKLTSLAALragdVEKIQKLEAELEKAATHRRNYEEKGKRYRDaVEEKLAKLQkhNSELE 969
Cdd:PRK01156 219 EIERLSIEYNNAMDDYNNLKSALNELSSL----EDMKNRYESEIKTAESDLSMELEKNNYYKE-LEERHMKII--NDPVY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 970 TQKEQIQ--LKLQEKTEELKEKMDNLTKQL--FDDVQKEERQrmlLEKSFElktqDYEKQiQSLKEEIKALKDEkmqlqh 1045
Cdd:PRK01156 292 KNRNYINdyFKYKNDIENKKQILSNIDAEInkYHAIIKKLSV---LQKDYN----DYIKK-KSRYDDLNNQILE------ 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1046 lVEGEHVTSDGLKAEVARLSKQvktISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLE-SYDIE--DVRSR 1122
Cdd:PRK01156 358 -LEGYEMDYNSYLKSIESLKKK---IEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDiSSKVSslNQRIR 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1123 LSVEDLEHLNEDGELWFAYE---------GLKKATRVLEsHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKL--FREEN 1191
Cdd:PRK01156 434 ALRENLDELSRNMEMLNGQSvcpvcgttlGEEKSNHIIN-HYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRkeYLESE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1192 DINESIrhevtrlTSENmmipdfkqQISELEKQKQDLEIRLNEQAEKmKGKLEELSNQlHRSQEEEGTQRKALEAQNEIH 1271
Cdd:PRK01156 513 EINKSI-------NEYN--------KIESARADLEDIKIKINELKDK-HDKYEEIKNR-YKSLKLEDLDSKRTSWLNALA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1272 TKEkekLIDkIQEMQEASDHLKKQF-ETES---EVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGK 1347
Cdd:PRK01156 576 VIS---LID-IETNRSRSNEIKKQLnDLESrlqEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGK 651
|
490
....*....|..
gi 294862453 1348 ANDVHSSSGPKE 1359
Cdd:PRK01156 652 IDNYKKQIAEID 663
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
886-1230 |
5.15e-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: 57.83 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 886 QLTYRVQRLQKKLEDQNKENHGLVEKltslaalragdvEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHN 965
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQ------------ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 966 S-ELETQKEQIQLKLQEKTEELK-----------EKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQ--IQSLKE 1031
Cdd:pfam17380 341 RmAMERERELERIRQEERKRELErirqeeiameiSRMRELERLQMERQQKNERVRQELEAARKVKILEEERQrkIQQQKV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1032 EIKALKDEKmqlqhlvegehvtSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVekhVQSQKREMREKMSEITKQLL 1111
Cdd:pfam17380 421 EMEQIRAEQ-------------EEARQREVRRLEEERAREMERVRLEEQERQQQVER---LRQQEEERKRKKLELEKEKR 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1112 ESYDIEDVRSRLSVEDLEHLNEdgelwfAYEGLKKATRVLESHFQS-QKDCYEKEIEalnfkvvHLSQEINHLQKLFREE 1190
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQ------AMIEEERKRKLLEKEMEErQKAIYEEERR-------REAEEERRKQQEMEER 551
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 294862453 1191 NDINESIR---HEVTRLTS---ENMMIpdfkQQISELEKQKQDLEI 1230
Cdd:pfam17380 552 RRIQEQMRkatEERSRLEAmerEREMM----RQIVESEKARAEYEA 593
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
846-1373 |
5.80e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 846 ARR--RYRKMLEEHKAVILQKY--ARAWLARRRFQSIRRF--VLNIQLTYRVQRLQKKLEDQNKenhglvekltslaALR 919
Cdd:PTZ00121 1181 ARKaeEVRKAEELRKAEDARKAeaARKAEEERKAEEARKAedAKKAEAVKKAEEAKKDAEEAKK-------------AEE 1247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 920 AGDVEKIQKLEaELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQiqlklqEKTEELKEKMDNLTKQlfD 999
Cdd:PTZ00121 1248 ERNNEEIRKFE-EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEK------KKADEAKKKAEEAKKA--D 1318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1000 DVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHlvegehvtsdglKAEVARLSKqvktiSEFEKEIE 1079
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE------------KAEAAEKKK-----EEAKKKAD 1381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1080 LLQAQKIDVEKHVQSQKR--EMREKMSEITKQLLESYDIEDVRSRLSvedlehlnedgELWFAYEGLKKATRVLESHFQS 1157
Cdd:PTZ00121 1382 AAKKKAEEKKKADEAKKKaeEDKKKADELKKAAAAKKKADEAKKKAE-----------EKKKADEAKKKAEEAKKADEAK 1450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1158 QKDCYEKEIEALNfKVVHLSQEINHLQKLFREENDINESIR--HEVTRLTSENMMIPDFKQQISEL----EKQKQDlEIR 1231
Cdd:PTZ00121 1451 KKAEEAKKAEEAK-KKAEEAKKADEAKKKAEEAKKADEAKKkaEEAKKKADEAKKAAEAKKKADEAkkaeEAKKAD-EAK 1528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1232 LNEQAEKM--------KGKLEELSNQLHRSQEEEgtQRKALEAQNEihTKEKEKLIDKIQEMQEASDHLKKQFETESEVK 1303
Cdd:PTZ00121 1529 KAEEAKKAdeakkaeeKKKADELKKAEELKKAEE--KKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1304 CNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVHSSSGPKEYLGMLQYKREDEAK 1373
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1071-1353 |
6.70e-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: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1071 ISEFEKEIELLQA------QKIDVEKHVQSQKREMREKMsEITKQLLESYDieDVRSRL-SVEDLEHLNEdgelwfayeg 1143
Cdd:TIGR02169 165 VAEFDRKKEKALEeleeveENIERLDLIIDEKRQQLERL-RREREKAERYQ--ALLKEKrEYEGYELLKE---------- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1144 lKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREEN-DINE-------SIRHEVTRLTSE----NMMI 1211
Cdd:TIGR02169 232 -KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNkKIKDlgeeeqlRVKEKIGELEAEiaslERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1212 PDFKQQISELEKQKQDLEIRLNEQAEKM----------KGKLEELSNQLHRSQEEEGTQRKALEAQNEIHT--------- 1272
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIeelereieeeRKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdelkdy 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1273 -KEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDV 1351
Cdd:TIGR02169 391 rEKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
..
gi 294862453 1352 HS 1353
Cdd:TIGR02169 471 LY 472
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
908-1354 |
9.51e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 9.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 908 LVEKLTSLAALRAgDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEK-LAKLQKHNSELETQKEQIQlKLQEKTEEL 986
Cdd:COG4913 230 LVEHFDDLERAHE-ALEDAREQIELLEPIRELAERYAAARERLAELEYLRaALRLWFAQRRLELLEAELE-ELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 987 KEKMDNLTKQLfDDVQKEERQrmlLEKsfELKTQDYEkQIQSLKEEIKALKDEK-------MQLQHLVEGEHVTSDGLKA 1059
Cdd:COG4913 308 EAELERLEARL-DALREELDE---LEA--QIRGNGGD-RLEQLEREIERLERELeererrrARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1060 EVARLSKQVKTISEFEKEI-ELLQAQKIDVEKHVQSQKREMREKMSEItkQLLES------YDIEDVRSRLSvedlEHLN 1132
Cdd:COG4913 381 EFAALRAEAAALLEALEEElEALEEALAEAEAALRDLRRELRELEAEI--ASLERrksnipARLLALRDALA----EALG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1133 ED-GELWF----------------AYEGL---------------KKATRVLESHFQSQKDCYEKeIEALNFKVVHLSQEI 1180
Cdd:COG4913 455 LDeAELPFvgelievrpeeerwrgAIERVlggfaltllvppehyAAALRWVNRLHLRGRLVYER-VRTGLPDPERPRLDP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1181 NHL-QKLFREENDINESIRHEVTR-------------------LTSENMM--------------IP-------DFKQQIS 1219
Cdd:COG4913 534 DSLaGKLDFKPHPFRAWLEAELGRrfdyvcvdspeelrrhpraITRAGQVkgngtrhekddrrrIRsryvlgfDNRAKLA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1220 ELEKQKQDLEIRLNE---QAEKMKGKLEELSNQ---LHRSQEEEGTQRKALEAQNEIHTKEKEklidkIQEMQEASDHLK 1293
Cdd:COG4913 614 ALEAELAELEEELAEaeeRLEALEAELDALQERreaLQRLAEYSWDEIDVASAEREIAELEAE-----LERLDASSDDLA 688
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294862453 1294 KQfetesevkcnfRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVHSS 1354
Cdd:COG4913 689 AL-----------EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
890-1043 |
1.07e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.55 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 890 RVQRLQKKLEDQNKEnhgLVEKLTSLAALRAgdveKIQKLEAELEKAATHRRNYEEKGKRYRDAVEekLAKLQKhnsELE 969
Cdd:COG1579 32 ELAELEDELAALEAR---LEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQLGNVRNNKE--YEALQK---EIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 294862453 970 TQKEQIQlKLQEKTEELKEKMDNLTKQLfddvQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQL 1043
Cdd:COG1579 100 SLKRRIS-DLEDEILELMERIEELEEEL----AELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
966-1345 |
1.36e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.57 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 966 SELETQKEQIQLKLQEKTEELKekmdNLTKQLFDDVQKeerqrmllEKSFELKTQDYEKQIQSLKeeiKALKDEKMQLqh 1045
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELK----NLDKNLNKDEEK--------INNSNNKIKILEQQIKDLN---DKLKKNKDKI-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1046 lvegehvtsDGLKAEVARLSKQVKT----ISEFEKEIELLQAQKIDVEKHV----------QSQKREMREKMSEITKQLL 1111
Cdd:TIGR04523 99 ---------NKLNSDLSKINSEIKNdkeqKNKLEVELNKLEKQKKENKKNIdkflteikkkEKELEKLNNKYNDLKKQKE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1112 E--------SYDIEDVRSRLSVEDLEHLNEDGELwFAYEGLKKATRVLES---HFQSQKDCYEKEIEALNFKVVHLSQEI 1180
Cdd:TIGR04523 170 ElenelnllEKEKLNIQKNIDKIKNKLLKLELLL-SNLKKKIQKNKSLESqisELKKQNNQLKDNIEKKQQEINEKTTEI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1181 N----HLQKLFREENDINESIRHEVTRLTSENMMIPD-------FKQQISELEKQK-QDLEIRLNEQAEKMKGKLEELSN 1248
Cdd:TIGR04523 249 SntqtQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKElekqlnqLKSEISDLNNQKeQDWNKELKSELKNQEKKLEEIQN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1249 QLHRSQE---EEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELD 1325
Cdd:TIGR04523 329 QISQNNKiisQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ 408
|
410 420
....*....|....*....|
gi 294862453 1326 MKDRVIKKLQDQVKTLSKTI 1345
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEI 428
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
890-1270 |
1.50e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 890 RVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAElEKAATHRRNYEEKGKRYRDAVEEKLaKLQKHNSELE 969
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE-EVMKLYEEEKKMKAEEAKKAEEAKI-KAEELKKAEE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 970 TQKEQIQLKLQE-----KTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEkmQLQ 1044
Cdd:PTZ00121 1631 EKKKVEQLKKKEaeekkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE--ELK 1708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1045 HLVEGEHVTSDGL-KAEVARLSKQVKTISEFEKEIELLQAQKIDVE--KHVQSQKREMREKMSEITKQ----LLESYDIE 1117
Cdd:PTZ00121 1709 KKEAEEKKKAEELkKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekKKIAHLKKEEEKKAEEIRKEkeavIEEELDEE 1788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1118 DVRSRLSVE-DLEHLNEDGELwfAYEGLKKATRVLeshfQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINES 1196
Cdd:PTZ00121 1789 DEKRRMEVDkKIKDIFDNFAN--IIEGGKEGNLVI----NDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGE 1862
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 294862453 1197 IRHEVTRLTSENMMIPDFKQQISELEKQKQ----DLEIRLNEQaeKMKGKLEELSNQlhRSQEEEGTQRKALEAQNEI 1270
Cdd:PTZ00121 1863 DGNKEADFNKEKDLKEDDEEEIEEADEIEKidkdDIEREIPNN--NMAGKNNDIIDD--KLDKDEYIKRDAEETREEI 1936
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
891-1342 |
1.74e-07 |
|
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: 56.34 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 891 VQRLQKKLEDQNKEnhgLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYR---DAVEEKLAKLQKHNSE 967
Cdd:pfam01576 403 SEHKRKKLEGQLQE---LQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSkdvSSLESQLQDTQELLQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 968 LETQK----------EQIQLKLQEKTEELKEKMDNLTK-------QLFDDVQKEERQRMLLEKSFELK---TQDYEKQIQ 1027
Cdd:pfam01576 480 ETRQKlnlstrlrqlEDERNSLQEQLEEEEEAKRNVERqlstlqaQLSDMKKKLEEDAGTLEALEEGKkrlQRELEALTQ 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1028 SLKEEIKA---LKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMS 1104
Cdd:pfam01576 560 QLEEKAAAydkLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRAL 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1105 EITKQLLESYD----IEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQS---QKDCYEKEIEA-----LNFK 1172
Cdd:pfam01576 640 SLARALEEALEakeeLERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEmktQLEELEDELQAtedakLRLE 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1173 VVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNE-----------------Q 1235
Cdd:pfam01576 720 VNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKEleaqidaankgreeavkQ 799
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1236 AEKMKGKLEELSNQL---HRSQEEEGTQRKaleaQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETE-----SEVKCN-- 1305
Cdd:pfam01576 800 LKKLQAQMKDLQRELeeaRASRDEILAQSK----ESEKKLKNLEAELLQLQEDLAASERARRQAQQErdelaDEIASGas 875
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 294862453 1306 ----FRQEASRLTLENRDLEEELD--------MKDRViKKLQDQVKTLS 1342
Cdd:pfam01576 876 gksaLQDEKRRLEARIAQLEEELEeeqsntelLNDRL-RKSTLQVEQLT 923
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
924-1324 |
3.25e-07 |
|
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: 55.57 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 924 EKIQKLEAELEKAathrrnyeekgKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKT------EELKEKMDNlTKQL 997
Cdd:pfam01576 5 EEMQAKEEELQKV-----------KERQQKAESELKELEKKHQQLCEEKNALQEQLQAETelcaeaEEMRARLAA-RKQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 998 FDDV---------QKEER-QRMLLEKsfelktQDYEKQIQSLKEEIKALKDEKMQLQHlvegEHVTSDGlkaevarlskq 1067
Cdd:pfam01576 73 LEEIlhelesrleEEEERsQQLQNEK------KKMQQHIQDLEEQLDEEEAARQKLQL----EKVTTEA----------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1068 vkTISEFEKEIELLQAQKIDVEKhvqsQKREMREKMSEITKQLLESYDIEDVRSRLS------VEDLE-HLNEDGELWFA 1140
Cdd:pfam01576 132 --KIKKLEEDILLLEDQNSKLSK----ERKLLEERISEFTSNLAEEEEKAKSLSKLKnkheamISDLEeRLKKEEKGRQE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1141 YEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREE----NDINESIRHEVTRLTSENMMIPDFKQ 1216
Cdd:pfam01576 206 LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEEtaqkNNALKKIRELEAQISELQEDLESERA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1217 QISELEKQKQDLEirlnEQAEKMKGKLEEL-----SNQLHRSQ-EEEGTQ-RKALEAQNEIHTKEkeklidkIQEMQE-- 1287
Cdd:pfam01576 286 ARNKAEKQRRDLG----EELEALKTELEDTldttaAQQELRSKrEQEVTElKKALEEETRSHEAQ-------LQEMRQkh 354
|
410 420 430
....*....|....*....|....*....|....*....
gi 294862453 1288 --ASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEEL 1324
Cdd:pfam01576 355 tqALEELTEQLEQAKRNKANLEKAKQALESENAELQAEL 393
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
895-1185 |
3.29e-07 |
|
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: 54.43 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 895 QKKLEDQNKenHGLVEKLTSLAALRAGDVEK-IQKLEAELEK------AAThrrnyeekgkRYRDAVEEKLAKLQKHNSE 967
Cdd:pfam15905 66 QKNLKESKD--QKELEKEIRALVQERGEQDKrLQALEEELEKveaklnAAV----------REKTSLSASVASLEKQLLE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 968 LETQKEQIQLKLQEKTEelKEKMDNLTKQLF---DDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQ 1044
Cdd:pfam15905 134 LTRVNELLKAKFSEDGT--QKKMSSLSMELMklrNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1045 HLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQllesydIEDVRSRLS 1124
Cdd:pfam15905 212 KEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQ------IKDLNEKCK 285
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294862453 1125 VedLEHLNEDgelwfayeglkkatrvLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQK 1185
Cdd:pfam15905 286 L--LESEKEE----------------LLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
955-1373 |
3.86e-07 |
|
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: 55.44 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 955 EEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNL------------TKQLFDDVQKEERQRMLLEKsfelKTQDY 1022
Cdd:TIGR00606 590 RDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsqdeesdLERLKEEIEKSSKQRAMLAG----ATAVY 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1023 EKQIQSLKEEI--------------KALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEF----EKEIELLQAQ 1084
Cdd:TIGR00606 666 SQFITQLTDENqsccpvcqrvfqteAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLapgrQSIIDLKEKE 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1085 KIDVEKHVQSQKREMREKMSEITKQ--LLESYDIEDVRSRLSVED------LEHLNEDGELWFAYEGLKKATRVLESHFQ 1156
Cdd:TIGR00606 746 IPELRNKLQKVNRDIQRLKNDIEEQetLLGTIMPEEESAKVCLTDvtimerFQMELKDVERKIAQQAAKLQGSDLDRTVQ 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1157 SQKdcyeKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQA 1236
Cdd:TIGR00606 826 QVN----QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLI 901
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1237 EKMKGKLEELsnqlhrSQEEEGTQRKALEAQNEIHTKEKEKLI--DKIQEM------------------QEASDHLKKQF 1296
Cdd:TIGR00606 902 REIKDAKEQD------SPLETFLEKDQQEKEELISSKETSNKKaqDKVNDIkekvknihgymkdienkiQDGKDDYLKQK 975
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1297 ETE------SEVKCNFRQEasRLTLENRDLEEELDMKDRVIKKLQDQVkTLSKTIGKANDVHSSsgPKEYLGMLQYKRED 1370
Cdd:TIGR00606 976 ETElntvnaQLEECEKHQE--KINEDMRLMRQDIDTQKIQERWLQDNL-TLRKRENELKEVEEE--LKQHLKEMGQMQVL 1050
|
...
gi 294862453 1371 EAK 1373
Cdd:TIGR00606 1051 QMK 1053
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
894-1324 |
4.53e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 55.34 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 894 LQKKLEDQNKENHGLVEKLTSLAALRAGDVEkiqkLEAELEKAATHRR------NYEEKGKRYRDAVEEKLAKLQKHNSE 967
Cdd:COG3096 294 LFGARRQLAEEQYRLVEMARELEELSARESD----LEQDYQAASDHLNlvqtalRQQEKIERYQEDLEELTERLEEQEEV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 968 LETQKEQiQLKLQEKTEELKEKMDNLTKQLfDDVQK--EERQRMLLEksfelktqdYEKQIQSLKEEikalkdekmqlQH 1045
Cdd:COG3096 370 VEEAAEQ-LAEAEARLEAAEEEVDSLKSQL-ADYQQalDVQQTRAIQ---------YQQAVQALEKA-----------RA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1046 LVEGEHVTSDGLKAEVARLSKQVKTISEfekeiELLQA-QKIDVEkhvQSQKREMREKMseitkQLLESYDIEDVRSRls 1124
Cdd:COG3096 428 LCGLPDLTPENAEDYLAAFRAKEQQATE-----EVLELeQKLSVA---DAARRQFEKAY-----ELVCKIAGEVERSQ-- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1125 vedlehlnedgelwfAYEglkKATRVLESHfQSQKDCYEKEiEALNFKVVHLSQEINHLQKLFREENDINESIRHEVtrl 1204
Cdd:COG3096 493 ---------------AWQ---TARELLRRY-RSQQALAQRL-QQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQL--- 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1205 tSENMMIPDFKqqiSELEKQKQDLEIRLNEQAEKmkgkleelSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLiDKIQE 1284
Cdd:COG3096 550 -DAAEELEELL---AELEAQLEELEEQAAEAVEQ--------RSELRQQLEQLRARIKELAARAPAWLAAQDAL-ERLRE 616
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 294862453 1285 M--------QEASDHLKKQFETESEVKcnfrQEASRLTLENRDLEEEL 1324
Cdd:COG3096 617 QsgealadsQEVTAAMQQLLEREREAT----VERDELAARKQALESQI 660
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
923-1265 |
6.02e-07 |
|
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: 54.19 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 923 VEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQ 1002
Cdd:COG5185 235 LKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1003 KEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKdekmqlqhlvegehvtsDGLKAEVARLSKQVKTISEfEKEIELLQ 1082
Cdd:COG5185 315 EEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQ-----------------ESLTENLEAIKEEIENIVG-EVELSKSS 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1083 AQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDgelwfayegLKKATRVLEShFQSQKDCY 1162
Cdd:COG5185 377 EELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQ---------IEQATSSNEE-VSKLLNEL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1163 EKEIEalnfKVVHLSQEiNHLQKLFREENDINESIRHEVTRLTSENMMIpdfKQQISELEKQKQDLEIRLNEQAEKMKGK 1242
Cdd:COG5185 447 ISELN----KVMREADE-ESQSRLEEAYDEINRSVRSKKEDLNEELTQI---ESRVSTLKATLEKLRAKLERQLEGVRSK 518
|
330 340
....*....|....*....|...
gi 294862453 1243 LEELSNQLHRSQEEEGTQRKALE 1265
Cdd:COG5185 519 LDQVAESLKDFMRARGYAHILAL 541
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
704-1273 |
7.21e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.20 E-value: 7.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 704 TKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIffragQVAYLEKLRLDKLrQSCVMVQKHMRGWLQRKkfLRERRAA 783
Cdd:TIGR00618 361 HEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKL-----QSLCKELDILQRE-QATIDTRTSAFRDLQGQ--LAHAKKQ 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 784 LIIQQYFRGQQtvRKAITAVAlKEAWAAIIIQKHCRGYLVRSLYQLIRMATITMQaYSRgflarrryRKMLEEHKAVILQ 863
Cdd:TIGR00618 433 QELQQRYAELC--AAAITCTA-QCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQ-ETR--------KKAVVLARLLELQ 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 864 KYARAWLARRRFQSIRRFVLNIQ--LTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRR 941
Cdd:TIGR00618 501 EEPCPLCGSCIHPNPARQDIDNPgpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDN 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 942 NYEEKGKRYRDAVEEklakLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQD 1021
Cdd:TIGR00618 581 RSKEDIPNLQNITVR----LQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLT 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1022 YEKQIQSLK--EEIKALKDEKMQ-----LQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQ----AQKIDVEK 1090
Cdd:TIGR00618 657 QERVREHALsiRVLPKELLASRQlalqkMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIEnassSLGSDLAA 736
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1091 HVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNE----DGELWF---AYEGLKKATRVLESHFQSQKDCYE 1163
Cdd:TIGR00618 737 REDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAElshlAAEIQFfnrLREEDTHLLKTLEAEIGQEIPSDE 816
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1164 keiEALNFKVVHLSQEINHLQKLFREendiNESIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLeIRLNEQAEKMKGKL 1243
Cdd:TIGR00618 817 ---DILNLQCETLVQEEEQFLSRLEE----KSATLGEITHQLLK---YEECSKQLAQLTQEQAKI-IQLSDKLNGINQIK 885
|
570 580 590
....*....|....*....|....*....|
gi 294862453 1244 EELSNQLHRSQEEEGTQRKALEAQNEIHTK 1273
Cdd:TIGR00618 886 IQFDGDALIKFLHEITLYANVRLANQSEGR 915
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
973-1320 |
7.96e-07 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 53.99 E-value: 7.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 973 EQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERqrmlleKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHV 1052
Cdd:pfam09731 44 EEVVLYALGEDPPLAPKPKTFRPLQPSVVSAVTG------ESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1053 TSDglKAEVARLSKQVKTISEFEKEIELLQAQ--------KIDVEKHVQSQKREM------REKMSEITKQLLESYDIED 1118
Cdd:pfam09731 118 QLP--KSEQEKEKALEEVLKEAISKAESATAVakeakddaIQAVKAHTDSLKEASdtaeisREKATDSALQKAEALAEKL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1119 VRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINESIR 1198
Cdd:pfam09731 196 KEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1199 HEVTRLTSE-NMMIPDFKQQISELEKQKQDL----EIRLNEQAEKMKGKLEELSNQL------HRSQEEEGTQRKALEAQ 1267
Cdd:pfam09731 276 EDNLLSNDDlNSLIAHAHREIDQLSKKLAELkkreEKHIERALEKQKEELDKLAEELsarleeVRAADEAQLRLEFERER 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 294862453 1268 NEIHTKEKEKLIDKIQEMQEA-SDHLKKQFET-ESEVKCNFRQEASRLTLENRDL 1320
Cdd:pfam09731 356 EEIRESYEEKLRTELERQAEAhEEHLKDVLVEqEIELQREFLQDIKEKVEEERAG 410
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
892-1257 |
8.06e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 54.29 E-value: 8.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 892 QRLQKKLEDQNKENHGLVEKLTSLAALRagDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVE--EKLAKLQKHNSELE 969
Cdd:TIGR01612 1325 KELQKNLLDAQKHNSDINLYLNEIANIY--NILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDksEKLIKKIKDDINLE 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 970 TQKEQIQLKLQE-------------KTEELKEKMDNLTkqLFDDVQKEERQRMLLEKSFEL---KTQ------------D 1021
Cdd:TIGR01612 1403 ECKSKIESTLDDkdidecikkikelKNHILSEESNIDT--YFKNADENNENVLLLFKNIEMadnKSQhilkikkdnatnD 1480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1022 YEKQIQSLKEEI---KALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQV------KTISEFEKEIELLQAQKIDVEKHV 1092
Cdd:TIGR01612 1481 HDFNINELKEHIdksKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYsalaikNKFAKTKKDSEIIIKEIKDAHKKF 1560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1093 QSQKREMREKMSEITKqllESYDIEDvrsrlsveDLEHLNEDGElwfAYEGLKKATRVLESHF-------QSQKDCYeKE 1165
Cdd:TIGR01612 1561 ILEAEKSEQKIKEIKK---EKFRIED--------DAAKNDKSNK---AAIDIQLSLENFENKFlkisdikKKINDCL-KE 1625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1166 IEALNFKVVHLSqeINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEE 1245
Cdd:TIGR01612 1626 TESIEKKISSFS--IDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIE 1703
|
410
....*....|..
gi 294862453 1246 LSNQLHRSQEEE 1257
Cdd:TIGR01612 1704 KIKEIAIANKEE 1715
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
912-1109 |
9.15e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 9.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 912 LTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKEKMD 991
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID-KLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 992 NLTKQLFD---DVQKEERQRMLLE-----KSFE--LKTQDYEKQI----QSLKEEIKALKDEKMQLQHLVEGEHVTSDGL 1057
Cdd:COG3883 83 ERREELGErarALYRSGGSVSYLDvllgsESFSdfLDRLSALSKIadadADLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 294862453 1058 KAEVARLSKQV-KTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQ 1109
Cdd:COG3883 163 KAELEAAKAELeAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
896-1373 |
1.01e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 896 KKLEDQNKENHGLVEKLTSL--AALRAGDVEKIQKLE--AELEKAATHRRNYEEK----GKRYRDAVEEKLAKLQKHNSE 967
Cdd:PTZ00121 1098 GKAEEAKKTETGKAEEARKAeeAKKKAEDARKAEEARkaEDARKAEEARKAEDAKrveiARKAEDARKAEEARKAEDAKK 1177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 968 LETQKEQIQLKlqeKTEELKEKmdnltkqlfDDVQKEERQRMLLE--KSFELKTQDYEKQIQSLKEEIKALKDE----KM 1041
Cdd:PTZ00121 1178 AEAARKAEEVR---KAEELRKA---------EDARKAEAARKAEEerKAEEARKAEDAKKAEAVKKAEEAKKDAeeakKA 1245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1042 QLQHLVEGEHVTSDGLKAEVARLSKQVKTiSEFEKEIELLQAQkiDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRS 1121
Cdd:PTZ00121 1246 EEERNNEEIRKFEEARMAHFARRQAAIKA-EEARKADELKKAE--EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK 1322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1122 RLSvedlEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKeiealnfkvvhlSQEINHLQKLFREEndinESIRHEV 1201
Cdd:PTZ00121 1323 KAE----EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA------------AEEKAEAAEKKKEE----AKKKADA 1382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1202 TRLTSEnmmipdfkqqiselEKQKQDleiRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDK 1281
Cdd:PTZ00121 1383 AKKKAE--------------EKKKAD---EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1282 IQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVHSSSGPK--- 1358
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKkad 1525
|
490
....*....|....*
gi 294862453 1359 EYLGMLQYKREDEAK 1373
Cdd:PTZ00121 1526 EAKKAEEAKKADEAK 1540
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
943-1278 |
1.21e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.22 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 943 YEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKEKMDNLtkqlfddvqKEERQRMLleksfelktqdy 1022
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRD-ELNAQVKELREEAQEL---------REKRDELN------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1023 eKQIQSLKEEIKALKDEKMQLQHLVegehvtsDGLKAEVARLSKQVKTISEFEKEIELLQaQKIDVEKHVQSQKREMREK 1102
Cdd:COG1340 71 -EKVKELKEERDELNEKLNELREEL-------DELRKELAELNKAGGSIDKLRKEIERLE-WRQQTEVLSPEEEKELVEK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1103 MSEITKQLlesydiedvrsrlsvEDLEHLNEdgelwfayegLKKATRVLESHFQSQKdcyeKEIEALNFKVVHLSQEINH 1182
Cdd:COG1340 142 IKELEKEL---------------EKAKKALE----------KNEKLKELRAELKELR----KEAEEIHKKIKELAEEAQE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1183 L----QKLFREEndinESIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNqLHRSQEEEG 1258
Cdd:COG1340 193 LheemIELYKEA----DELRKEADELHKE---IVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRA-LKREKEKEE 264
|
330 340
....*....|....*....|
gi 294862453 1259 TQRKALEAQNEIhtKEKEKL 1278
Cdd:COG1340 265 LEEKAEEIFEKL--KKGEKL 282
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
955-1302 |
1.32e-06 |
|
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: 53.15 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 955 EEKLAKLQKHNSELETQKEqiqlKLQEKTEELKE----------KMDNLTKQLfdDVQKEERQRmlLEKS---FELKTQD 1021
Cdd:pfam05622 20 DQQVSLLQEEKNSLQQENK----KLQERLDQLESgddsgtpggkKYLLLQKQL--EQLQEENFR--LETArddYRIKCEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1022 YEKQI----------QSLKEEIKALKDEKMQLQHlvegehvTSDGLK---AEVARLSKQVKTISEFEKEIELLQ------ 1082
Cdd:pfam05622 92 LEKEVlelqhrneelTSLAEEAQALKDEMDILRE-------SSDKVKkleATVETYKKKLEDLGDLRRQVKLLEernaey 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1083 -AQKIDVEK----------HVQSQKREMRE---KMSEIT----------KQLLESYD-IEDVRSRLSVE--DLEHLNEDG 1135
Cdd:pfam05622 165 mQRTLQLEEelkkanalrgQLETYKRQVQElhgKLSEESkkadklefeyKKLEEKLEaLQKEKERLIIErdTLRETNEEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1136 ELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNF-----------KVVHLSQEINHLQKLFREENDINESIRhEVTRL 1204
Cdd:pfam05622 245 RCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIreklirlqhenKMLRLGQEGSYRERLTELQQLLEDANR-RKNEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1205 TSENMMIpdfKQQISELEKQKQDLEIRLNEQAEK------MKGKLEELSNQLHRSQEEEGTQRKALE-----AQNEIHTK 1273
Cdd:pfam05622 324 ETQNRLA---NQRILELQQQVEELQKALQEQGSKaedsslLKQKLEEHLEKLHEAQSELQKKKEQIEelepkQDSNLAQK 400
|
410 420 430
....*....|....*....|....*....|..
gi 294862453 1274 E---KEKLIDKIQEMQEASDHLKKQFETESEV 1302
Cdd:pfam05622 401 IdelQEALRKKDEDMKAMEERYKKYVEKAKSV 432
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
890-1133 |
1.36e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 890 RVQRLQKKLEDQNKENHGLVEKLTSL----AALRAGDVEKIQKLEAELEKAatHRRNYEEKGKRYRdaVEEKLAKLQKHN 965
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELAELlkelEELGFESVEELEERLKELEPF--YNEYLELKDAEKE--LEREEKELKKLE 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 966 SELETQKEQIQLKLQEkTEELKEKMDNLtKQLFDDVQKEERQRMLLEKSFELKtqdyekqiqSLKEEIKALKDEKmqlqh 1045
Cdd:PRK03918 626 EELDKAFEELAETEKR-LEELRKELEEL-EKKYSEEEYEELREEYLELSRELA---------GLRAELEELEKRR----- 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1046 lvegehvtsDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEkhvqsqkrEMREKMSEItKQLLESYDIEDVrSRLSV 1125
Cdd:PRK03918 690 ---------EEIKKTLEKLKEELEEREKAKKELEKLEKALERVE--------ELREKVKKY-KALLKERALSKV-GEIAS 750
|
....*...
gi 294862453 1126 EDLEHLNE 1133
Cdd:PRK03918 751 EIFEELTE 758
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
959-1169 |
1.75e-06 |
|
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: 52.84 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 959 AKLQKHNSELETQKEQIQLKLQEKTEELKEKmdnltkqlFDDVQKEERQRMLLEKSFELKtqDYEKQIQSLKEEIKALKD 1038
Cdd:pfam09731 294 REIDQLSKKLAELKKREEKHIERALEKQKEE--------LDKLAEELSARLEEVRAADEA--QLRLEFEREREEIRESYE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1039 EKMQLQhLVEGEHVTSDGLKAEVArlskqvktisefEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLEsydIED 1118
Cdd:pfam09731 364 EKLRTE-LERQAEAHEEHLKDVLV------------EQEIELQREFLQDIKEKVEEERAGRLLKLNELLANLKG---LEK 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 294862453 1119 VRSRLSVEDLEHLNEDgELWFAYEGLKKATRvlESHFQSQKDCYEKEIEAL 1169
Cdd:pfam09731 428 ATSSHSEVEDENRKAQ-QLWLAVEALRSTLE--DGSADSRPRPLVRELKAL 475
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
890-1051 |
2.14e-06 |
|
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: 52.38 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 890 RVQRLQKKLEDQNKENHGLVEKLtSLAALRAGDVEkiQKLEaELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELE 969
Cdd:pfam05622 305 RLTELQQLLEDANRRKNELETQN-RLANQRILELQ--QQVE-ELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 970 TQKEQI-------QLKLQEKTEELKEkmdNLTKQLFDDVQKEERQRMLLEKSFE-LKTQDyEKQIQSLKEEIKALKD--- 1038
Cdd:pfam05622 381 KKKEQIeelepkqDSNLAQKIDELQE---ALRKKDEDMKAMEERYKKYVEKAKSvIKTLD-PKQNPASPPEIQALKNqll 456
|
170
....*....|...
gi 294862453 1039 EKMQLQHLVEGEH 1051
Cdd:pfam05622 457 EKDKKIEHLERDF 469
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1021-1289 |
2.31e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.45 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1021 DYEKQIQSLKEEIKALKDEKMQLQHLVEgehvtsdGLKAEVARLSKQVKTISEfekeiellQAQKIdvekhvQSQKREMR 1100
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELK-------ELAEKRDELNAQVKELRE--------EAQEL------REKRDELN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1101 EKMSEITKQLLESYD-IEDVRSRLSV--EDLEHLNEDGElwfAYEGLKKATRVLESHFQSQKDCYEKEIEALNfKVVHLS 1177
Cdd:COG1340 71 EKVKELKEERDELNEkLNELREELDElrKELAELNKAGG---SIDKLRKEIERLEWRQQTEVLSPEEEKELVE-KIKELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1178 QEINHLQKlfreENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQ---DLEIRLNEQAEKMKGKLEELSNQLHRSQ 1254
Cdd:COG1340 147 KELEKAKK----ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQelhEEMIELYKEADELRKEADELHKEIVEAQ 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 294862453 1255 EEEGTQRKAL-EAQNEIHtkEKEKLIDKIQEMQEAS 1289
Cdd:COG1340 223 EKADELHEEIiELQKELR--ELRKELKKLRKKQRAL 256
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
871-1036 |
3.41e-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: 52.37 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 871 ARRRFQSIRRFVLNiqLTYRVQRLQKKLEDQNKENHGLV-------EKLTSLAALRAGDVEKIQKLEAELEKA------- 936
Cdd:TIGR02168 808 LRAELTLLNEEAAN--LRERLESLERRIAATERRLEDLEeqieelsEDIESLAAEIEELEELIEELESELEALlnerasl 885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 937 ----ATHRRNYEEKGKRYRDaVEEKLAKLQKHNSELETQKEQIQLKLQekteELKEKMDNLTKQLFDDVQKEERQRMLLE 1012
Cdd:TIGR02168 886 eealALLRSELEELSEELRE-LESKRSELRRELEELREKLAQLELRLE----GLEVRIDNLQERLSEEYSLTLEEAEALE 960
|
170 180
....*....|....*....|....
gi 294862453 1013 KSFELKTQDYEKQIQSLKEEIKAL 1036
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKEL 984
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
890-1374 |
3.79e-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: 51.97 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 890 RVQRLQKKLEDQNKENHGLVEKLTSL------AALRAGDV-EKIQKLEAELEKAATH----------------------- 939
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQEKTELlveqgrLQLQADRHqEHIRARDSLIQSLATRleldgfergpfserqiknfhtlv 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 940 RRNYEEKGK---RYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFE 1016
Cdd:TIGR00606 400 IERQEDEAKtaaQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1017 LKTQDYE-------KQIQSLKEEIKALKDEKMQLqhlvegehvtsDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVE 1089
Cdd:TIGR00606 480 LRKAERElskaeknSLTETLKKEVKSLQNEKADL-----------DRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKD 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1090 KHVQSQKREMREKMSEI------TKQLLESYDIEDVRSRLSVEDLEHLNEDGElwfAYEGLKKATRVLESHFQSQKDCYE 1163
Cdd:TIGR00606 549 EQIRKIKSRHSDELTSLlgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELA---SLEQNKNHINNELESKEEQLSSYE 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1164 KEI------EALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQAE 1237
Cdd:TIGR00606 626 DKLfdvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLR 705
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1238 KMKGKLEELSNQLHRSQEE-EGTQRKALEAQNEIHTKEKEklidkIQEMQEASDHLKKQFEtesEVKCNFRQEASRLTLE 1316
Cdd:TIGR00606 706 LAPDKLKSTESELKKKEKRrDEMLGLAPGRQSIIDLKEKE-----IPELRNKLQKVNRDIQ---RLKNDIEEQETLLGTI 777
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294862453 1317 NRDLE--EELDMKDRVIKKLQDQVKTLSKTIGK-ANDVHSSSGPKEYLGMLQYKREDEAKL 1374
Cdd:TIGR00606 778 MPEEEsaKVCLTDVTIMERFQMELKDVERKIAQqAAKLQGSDLDRTVQQVNQEKQEKQHEL 838
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
915-1110 |
5.06e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 915 LAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQL------KLQEKTEELKE 988
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAleqelaALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 989 KMDNLTKQLfdDVQKEERQRMLLeKSFELKTQDYEKQIQSLKEEIKALKDEKMqLQHLVEGEHVTSDGLKAEVARLSKQV 1068
Cdd:COG4942 91 EIAELRAEL--EAQKEELAELLR-ALYRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 294862453 1069 KTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQL 1110
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
878-1197 |
5.42e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 878 IRRFVLNIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEK 957
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 958 LAKLQKHNSELETQKEQIQlKLQEKTEELKEKMDNLTKQLfddvQKEERQRMLLEKSFELKtqdyEKQIQSLKEEIKALK 1037
Cdd:COG4372 93 QAELAQAQEELESLQEEAE-ELQEELEELQKERQDLEQQR----KQLEAQIAELQSEIAER----EEELKELEEQLESLQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1038 DEKMQLQhlVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQaQKIDVEKHVQSQKREMREKMSEITKQLLESYDIE 1117
Cdd:COG4372 164 EELAALE--QELQALSEAEAEQALDELLKEANRNAEKEEELAEAE-KLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1118 DVRsrlSVEDLEHLNEDGELWFAYEGLKKATRVLESHfqsqkdcyEKEIEALNFKVVHLSQEINHLQKLFREENDINESI 1197
Cdd:COG4372 241 ALE---LEEDKEELLEEVILKEIEELELAILVEKDTE--------EEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1178-1345 |
5.58e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1178 QEINHLQKLFREENDINEsIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNE---QAEKMKGKLEELSNQLHRSQ 1254
Cdd:COG1579 4 EDLRALLDLQELDSELDR-LEHRLKELPAE---LAELEDELAALEARLEAAKTELEDlekEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1255 EEEGTQR-----KALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQF-ETESEVKcnfrQEASRLTLENRDLEEELDMKD 1328
Cdd:COG1579 80 EQLGNVRnnkeyEALQKEIESLKRRISDLEDEILELMERIEELEEELaELEAELA----ELEAELEEKKAELDEELAELE 155
|
170
....*....|....*..
gi 294862453 1329 RVIKKLQDQVKTLSKTI 1345
Cdd:COG1579 156 AELEELEAEREELAAKI 172
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1163-1297 |
5.64e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1163 EKEIEALNFKVVHLSQEINHLQKLFRE-ENDInESIRHEVTRLTSENMMIPDFKQ------QISELEKQKQDLE---IRL 1232
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRlELEI-EEVEARIKKYEEQLGNVRNNKEyealqkEIESLKRRISDLEdeiLEL 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294862453 1233 NEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEA-SDHLKKQFE 1297
Cdd:COG1579 116 MERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKiPPELLALYE 181
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
925-1335 |
5.87e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 51.36 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 925 KIQKLEAELEKAATHR----------RNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLT 994
Cdd:pfam10174 290 KIDQLKQELSKKESELlalqtkletlTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 995 -------------KQLFDDVQKEERQRMLLEKSFE-LKTQ--DYEKQIQSLKEEIKALkdekmqlqhlvEGEHVTSDglk 1058
Cdd:pfam10174 370 dlteekstlageiRDLKDMLDVKERKINVLQKKIEnLQEQlrDKDKQLAGLKERVKSL-----------QTDSSNTD--- 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1059 aevARLSKQVKTISEFEKEIELLQAQKidvekhvqsqKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDGELW 1138
Cdd:pfam10174 436 ---TALTTLEEALSEKERIIERLKEQR----------EREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLK 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1139 -----FAYEGLKKatrvlESHFQSQKDCYEKEIEALNfKVVHLSQEINHLQKLFREENDINESIRH---EVTRLTSENMm 1210
Cdd:pfam10174 503 ehassLASSGLKK-----DSKLKSLEIAVEQKKEECS-KLENQLKKAHNAEEAVRTNPEINDRIRLleqEVARYKEESG- 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1211 ipdfKQQiSELEKQKQDLEIRLNEQAEKMK--GKLEELSNQLHRSQEEEGTQRKALeaQNEIHTKEKEKLID-KIQEMQE 1287
Cdd:pfam10174 576 ----KAQ-AEVERLLGILREVENEKNDKDKkiAELESLTLRQMKEQNKKVANIKHG--QQEMKKKGAQLLEEaRRREDNL 648
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 294862453 1288 ASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQ 1335
Cdd:pfam10174 649 ADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLR 696
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
888-1102 |
8.10e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 8.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 888 TYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSE 967
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 968 LETQKEQI--QLKLQEKTEELKEKMDNLTKQLFDDVQKeeRQRMLLEKSFELKTQDYE-----KQIQSLKEEIKALKDEK 1040
Cdd:COG4942 99 LEAQKEELaeLLRALYRLGRQPPLALLLSPEDFLDAVR--RLQYLKYLAPARREQAEElradlAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 294862453 1041 MQLQHLVEGEHVTSDGLKAEVARLSKQV-KTISEFEKEIELLQAQKIDVEKHVQSQKREMREK 1102
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLeKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
890-1109 |
9.21e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 890 RVQRLQKKLEDQNKENHGLVEKLTSLAAlragDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELE 969
Cdd:TIGR02169 792 RIPEIQAELSKLEEEVSRIEARLREIEQ----KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 970 TQKEQIQLK---LQEKTEELKEKMDNLTKQLfddVQKEERQRMLLEKSFELKTQDYE--KQIQSLKEEIKALKDEKMQLQ 1044
Cdd:TIGR02169 868 EELEELEAAlrdLESRLGDLKKERDELEAQL---RELERKIEELEAQIEKKRKRLSElkAKLEALEEELSEIEDPKGEDE 944
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 294862453 1045 HLVEGEHVTSDgLKAEVARLSKQV--------KTISEFEkeiELLQAQKIDVEKH--VQSQKREMREKMSEITKQ 1109
Cdd:TIGR02169 945 EIPEEELSLED-VQAELQRVEEEIralepvnmLAIQEYE---EVLKRLDELKEKRakLEEERKAILERIEEYEKK 1015
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
881-1044 |
9.38e-06 |
|
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: 49.81 E-value: 9.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 881 FVLNIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYeEKGKRYRDAVEEKLAK 960
Cdd:pfam15905 176 MAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQV-EKYKLDIAQLEELLKE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 961 LQKHNSELetqkeqiQLKLQEKTEELKEKMDNLTKQLfdDVQKEERQRMLLEksFELKTQDYEKQIQSLKEEIKALKDEK 1040
Cdd:pfam15905 255 KNDEIESL-------KQSLEEKEQELSKQIKDLNEKC--KLLESEKEELLRE--YEEKEQTLNAELEELKEKLTLEEQEH 323
|
....
gi 294862453 1041 MQLQ 1044
Cdd:pfam15905 324 QKLQ 327
|
|
| Myo5p-like_CBD_Rasip1 |
cd15472 |
cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 ... |
1396-1675 |
1.12e-05 |
|
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: 49.58 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1396 PAHILFMCVRYADS-----------LNDANMLKSLMNSTINGIKQVVKEHLE--------------DFEMLSFWLSNT-- 1448
Cdd:cd15472 25 PAFLLCLCIQHSAThfepghfgkllLKIAKRIQEIVWEKTKELAEKQPEHQDpaslsllsiaelapDLQPLLFWMSNSie 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1449 --CHFLNCLKQYSGE-EEFMKHNSPQQNKNCLNNfDLSEYRQILSDVAIRIYHQFIIIMEKNIQPIIvPGMLE------- 1518
Cdd:cd15472 105 llYFIQQKVPLYEQSmEEELDVGSKESLLSSTLT-ASEEAMTVLEEVIMYTFQQCVYYLTKTLYVAL-PALLDsnpftae 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1519 -YESLQGISGLkPTGFRKrsssiddtdgytMTSVLQ---QLsyfyTTMCQngLDPELVRQAVKQLFFLIGAVTLNSLFLR 1594
Cdd:cd15472 183 eRESWSGGSRL-PEGVRR------------VLEIYQatlDL----LRQYQ--VHPEIASQMFAYLFFFSNASLFNQLMEK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1595 KDMCSC---RKGMQIRCNISYLEEWLKDKNLqNSLAKETLEPLSQAAWLLQVKKTT--DSDAKEIYERCTSLSAVQIIKI 1669
Cdd:cd15472 244 GSGGGFfqwSRGVQIRANLDLLLDWLQGAGL-GDLAEEFFRKLSSTVNLLATPKEQllQMSWSSLRAEFPALNPAQLHHL 322
|
....*.
gi 294862453 1670 LNSYTP 1675
Cdd:cd15472 323 LRQYQL 328
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1018-1289 |
1.14e-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: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1018 KTQDYEKQIQSLKEEIKALKDEKMQLQhlvEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKR 1097
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALK---KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1098 EMREKMSEITKQLLESYDIEDvRSRLsvedlehlnedgELWFAYEGLKKATRVLEshfqsqkdcYEKEIEAlnfkvvHLS 1177
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGR-QPPL------------ALLLSPEDFLDAVRRLQ---------YLKYLAP------ARR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1178 QEINHLQKLFREENDINESIRHEVTRLtsenmmipdfKQQISELEKQKQDLEIRLNEQaekmkgklEELSNQLHRSQEEE 1257
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAEL----------EALLAELEEERAALEALKAER--------QKLLARLEKELAEL 211
|
250 260 270
....*....|....*....|....*....|..
gi 294862453 1258 GTQRKALEAQNEIHTKEKEKLIDKIQEMQEAS 1289
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
957-1147 |
1.23e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 957 KLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKqLFDDVQKEERQRmlleKSFELKTQDYEKQIQSLKEEIKAL 1036
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEA-AKTELEDLEKEI----KRLELEIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1037 KDEK--MQLQHLVEgehvtsdGLKAEVARLSKQvktISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLEsy 1114
Cdd:COG1579 86 RNNKeyEALQKEIE-------SLKRRISDLEDE---ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE-- 153
|
170 180 190
....*....|....*....|....*....|....
gi 294862453 1115 dIEDVRSRLSVEDLEHLNE-DGELWFAYEGLKKA 1147
Cdd:COG1579 154 -LEAELEELEAEREELAAKiPPELLALYERIRKR 186
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
543-652 |
1.40e-05 |
|
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: 47.34 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 543 NTSFVIQHFAD-------KVEYKCEGFLEKNRDTVYDMLVEILraskfhlcanffqenptppsPFGSMITVksAKQVIKP 615
Cdd:cd01363 68 TMKGVIPYLASvafnginKGETEGWVYLTEITVTLEDQILQAN--------------------PILEAFGN--AKTTRNE 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 294862453 616 NS----KHFRTTV---GS-KFRSSLYLLMETLNATTPHYVRCIKP 652
Cdd:cd01363 126 NSsrfgKFIEILLdiaGFeIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1001-1342 |
1.55e-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: 49.82 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1001 VQKEERQRMLLEKSFELKTQDYEKQ----IQSLKEEIKALKDekmqLQHLVEGEHVTSDGLKAE---VARLSKQ--VKTI 1071
Cdd:pfam10174 47 LRKEEAARISVLKEQYRVTQEENQHlqltIQALQDELRAQRD----LNQLLQQDFTTSPVDGEDkfsTPELTEEnfRRLQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1072 SEFE---KEIELLQAQKIDVEKHVQSQKREMrEKMSEITKQLLE----------SYDIEDVRSRLSVEDLEHLNE-DGEL 1137
Cdd:pfam10174 123 SEHErqaKELFLLRKTLEEMELRIETQKQTL-GARDESIKKLLEmlqskglpkkSGEEDWERTRRIAEAEMQLGHlEVLL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1138 WFAYEGLKKATRVLESHFQSQKD-----CYEKEIEALNFKVVHLSQEINHLQ---KLFREENDINESIRH------EVTR 1203
Cdd:pfam10174 202 DQKEKENIHLREELHRRNQLQPDpaktkALQTVIEMKDTKISSLERNIRDLEdevQMLKTNGLLHTEDREeeikqmEVYK 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1204 LTSENMmipdfKQQISELekqKQDLEiRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNE---IHTKEKEKLID 1280
Cdd:pfam10174 282 SHSKFM-----KNKIDQL---KQELS-KKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQraaILQTEVDALRL 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 294862453 1281 KIQEMQEASDHLKKQFETESEvkcnfrqEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLS 1342
Cdd:pfam10174 353 RLEEKESFLNKKTKQLQDLTE-------EKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQ 407
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
916-1077 |
1.69e-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: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 916 AALRAGDVEKIQKLEAELEKAATH-RRNYEEKGKRYRDaVEEKLAKLQKHNSELEtqkeqiqlklqEKTEELKEKMDNLT 994
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEHeERELTEEEEEIRR-LEEQVERLEAEVEELE-----------AELEEKDERIERLE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 995 KQLfDDVQKEERQRMLLEKsfELKTQDYE-----KQIQSLKEEIKALKDEKMQLQHLVEGEHvtSDGLKAevarlskqVK 1069
Cdd:COG2433 448 REL-SEARSEERREIRKDR--EISRLDREierleRELEEERERIEELKRKLERLKELWKLEH--SGELVP--------VK 514
|
....*...
gi 294862453 1070 TISEFEKE 1077
Cdd:COG2433 515 VVEKFTKE 522
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
855-1324 |
1.71e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 855 EEHKAVILQKYARAWLARRRFQSIRRFvlniqltYRVQRlQKKLEDQNKENHGLVEKLTSLAAlragDVEKIQKLEAELE 934
Cdd:PRK04863 753 EELEKAVVVKIADRQWRYSRFPEVPLF-------GRAAR-EKRIEQLRAEREELAERYATLSF----DVQKLQRLHQAFS 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 935 K-AATHRrnyeekgkryrdAV------EEKLAKLQKHNSELETQKEQiqlkLQEKTEELKEKMDNLtKQLFDDVQKEERQ 1007
Cdd:PRK04863 821 RfIGSHL------------AVafeadpEAELRQLNRRRVELERALAD----HESQEQQQRSQLEQA-KEGLSALNRLLPR 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1008 RMLLEKsfelktQDYEKQIQSLKEEIKALKDEKMQL-QHlvegehvtsdglKAEVARLSKQVKTISEFEKEIELLQAQki 1086
Cdd:PRK04863 884 LNLLAD------ETLADRVEEIREQLDEAEEAKRFVqQH------------GNALAQLEPIVSVLQSDPEQFEQLKQD-- 943
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1087 dvekHVQSQKREMREKMseitkqllESYDIEDVRSRlsvedLEHlnedgelwFAYEglkkatrvleshfQSQKDCYEKei 1166
Cdd:PRK04863 944 ----YQQAQQTQRDAKQ--------QAFALTEVVQR-----RAH--------FSYE-------------DAAEMLAKN-- 983
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1167 EALNFKvvhLSQEINHLQklfREENDINESIRHEVTRLTSENMMIPDFK-------QQISELEKQKQDLEIRLNEQAE-K 1238
Cdd:PRK04863 984 SDLNEK---LRQRLEQAE---QERTRAREQLRQAQAQLAQYNQVLASLKssydakrQMLQELKQELQDLGVPADSGAEeR 1057
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1239 MKGKLEELSNQLHRSQeeegTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENR 1318
Cdd:PRK04863 1058 ARARRDELHARLSANR----SRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERR 1133
|
....*.
gi 294862453 1319 DLEEEL 1324
Cdd:PRK04863 1134 LHRREL 1139
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
987-1256 |
2.16e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 48.38 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 987 KEKMDNLTKQL---FDDVQKEERQRMLLEKSFELKTQD-----------YEKQIQSLKEEIKALKDEKMQLQhlvegehV 1052
Cdd:pfam00038 3 KEQLQELNDRLasyIDKVRFLEQQNKLLETKISELRQKkgaepsrlyslYEKEIEDLRRQLDTLTVERARLQ-------L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1053 TSDGLKAEVARLSKQVKT-----------ISEFEKEIELLQAQKIDVEKHVQS-------QKREMREKMSEITKQLLESY 1114
Cdd:pfam00038 76 ELDNLRLAAEDFRQKYEDelnlrtsaendLVGLRKDLDEATLARVDLEAKIESlkeelafLKKNHEEEVRELQAQVSDTQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1115 DIEDVRSRLSVEdlehlnedgelwfayegLKKATRVLESHFQSQKDCYEKEIEAL-NFKVVHLSQEIN-HLQKLFREEND 1192
Cdd:pfam00038 156 VNVEMDAARKLD-----------------LTSALAEIRAQYEEIAAKNREEAEEWyQSKLEELQQAAArNGDALRSAKEE 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 294862453 1193 INESiRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEE 1256
Cdd:pfam00038 219 ITEL-RRTIQSLEIE---LQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQE 278
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1025-1341 |
2.45e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.45 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1025 QIQSLKEEIKALKDEKMQLQHLvegeHVtsdGLKAEVARLSKQVKTISEFEKEIELLQAQKIDvekhvqsqkrEMREKMS 1104
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHL----HF---GYKSDETLIASRQEERQETSAELNQLLRTLDD----------QWKEKRD 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1105 EITKQL-LESYDIEDVRSRLSVEDLEHLNedgelwFAYEGLKKATRVLES--HFQSQKDCYEKEIEALNFKVVHLSQEIN 1181
Cdd:pfam12128 305 ELNGELsAADAAVAKDRSELEALEDQHGA------FLDADIETAAADQEQlpSWQSELENLEERLKALTGKHQDVTAKYN 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1182 HLQKLFREEN-----DINE---SIRHEVTRLTSENMmiPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRS 1253
Cdd:pfam12128 379 RRRSKIKEQNnrdiaGIKDklaKIREARDRQLAVAE--DDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQA 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1254 Q--EEEGTQRKAleaqneihtkeKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEAS-RLTLENRDLEEELDMKDRV 1330
Cdd:pfam12128 457 TatPELLLQLEN-----------FDERIERAREEQEAANAEVERLQSELRQARKRRDQASeALRQASRRLEERQSALDEL 525
|
330
....*....|.
gi 294862453 1331 IKKLQDQVKTL 1341
Cdd:pfam12128 526 ELQLFPQAGTL 536
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1220-1339 |
2.56e-05 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 45.29 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1220 ELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEaqneihtkEKEKLIDKIQEMQEASDHLKKQFETE 1299
Cdd:pfam20492 3 EAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEE--------EAERLEQKRQEAEEEKERLEESAEME 74
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 294862453 1300 SEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVK 1339
Cdd:pfam20492 75 AEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELE 114
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1054-1295 |
2.60e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1054 SDGLKAEVARLSKQVKTISEFEKEIELLQAQKidveKHVQSQKREMREKMSEITKQL--LESyDIEDVRSRLSVedlehl 1131
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEE----KALLKQLAALERRIAALARRIraLEQ-ELAALEAELAE------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1132 nedgelwfayegLKKATRVLESHFQSQKDCYEKEIEALnfkvvHLSQEINHLQKLFREEnDINESIRhevtRLTSENMMI 1211
Cdd:COG4942 88 ------------LEKEIAELRAELEAQKEELAELLRAL-----YRLGRQPPLALLLSPE-DFLDAVR----RLQYLKYLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1212 PDFKQQISELEKQKQDLEiRLNEQAEKMKGKLEELsnqlhrsQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDH 1291
Cdd:COG4942 146 PARREQAEELRADLAELA-ALRAELEAERAELEAL-------LAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
....
gi 294862453 1292 LKKQ 1295
Cdd:COG4942 218 LQQE 221
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
960-1276 |
2.62e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.27 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 960 KLQKHNSELETQKEQIQLKLQE-KTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKD 1038
Cdd:TIGR00606 180 SATRYIKALETLRQVRQTQGQKvQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEH 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1039 EKMQLqHLVEGEHVTSDGLKAEVARLSKQVKTIseFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLlESYDIEd 1118
Cdd:TIGR00606 260 NLSKI-MKLDNEIKALKSRKKQMEKDNSELELK--MEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQREL-EKLNKE- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1119 vRSRLSVEDLEHLNEDGELWFAYE-----GLKKATRVLESHFQSQKDCYEKEIEAlnfkvvhlSQEINHLQKLFRE-END 1192
Cdd:TIGR00606 335 -RRLLNQEKTELLVEQGRLQLQADrhqehIRARDSLIQSLATRLELDGFERGPFS--------ERQIKNFHTLVIErQED 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1193 INESIRHEVTRLTSENMMIpdfKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHT 1272
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLK---QEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRK 482
|
....
gi 294862453 1273 KEKE 1276
Cdd:TIGR00606 483 AERE 486
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
878-1035 |
2.74e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.01 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 878 IRRFVLNIQLTYRVQRLQKKLEDQNKEnhglVEKLTSLAALRAGdvEKIQKLEAELEKAATHRRNY----EEKGKRYRDA 953
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRILEEAKKE----AEAIKKEALLEAK--EEIHKLRNEFEKELRERRNElqklEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 954 VEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKEKMDNLtkqlfddvQKEERQRmlLEKSFELkTQDYEKQI--QSLKE 1031
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELE-QKQQELEKKEEELEEL--------IEEQLQE--LERISGL-TAEEAKEIllEKVEE 165
|
....
gi 294862453 1032 EIKA 1035
Cdd:PRK12704 166 EARH 169
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
960-1343 |
2.89e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 48.68 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 960 KLQKHNSELETQKEQI-------------QLKL----QEKTEELKEKMDNLTKQLFDDVQKE--------ERQRMLLEKS 1014
Cdd:PRK04778 26 RNYKRIDELEERKQELenlpvndelekvkKLNLtgqsEEKFEEWRQKWDEIVTNSLPDIEEQlfeaeelnDKFRFRKAKH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1015 fELKT-----QDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVarLSKQVK---TISEFEKEIELLQAQ-- 1084
Cdd:PRK04778 106 -EINEiesllDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSL--LANRFSfgpALDELEKQLENLEEEfs 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1085 ----------KIDVEKHVQSQKREM---REKMSEItKQLLESY---------DIEDVRSRLSVE--DLEHLNEDGELwfa 1140
Cdd:PRK04778 183 qfveltesgdYVEAREILDQLEEELaalEQIMEEI-PELLKELqtelpdqlqELKAGYRELVEEgyHLDHLDIEKEI--- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1141 yEGLKKATRvleshfQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDinesIRHEVTRLtsenmmIPDFKQQISE 1220
Cdd:PRK04778 259 -QDLKEQID------ENLALLEELDLDEAEEKNEEIQERIDQLYDILEREVK----ARKYVEKN------SDTLPDFLEH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1221 LEKQKQDLEI---------RLN----EQAEKMKGKLEELSNQLHRSQEEEGTQRKAL-EAQNEIhtKEKEKLIDKIQEMQ 1286
Cdd:PRK04778 322 AKEQNKELKEeidrvkqsyTLNeselESVRQLEKQLESLEKQYDEITERIAEQEIAYsELQEEL--EEILKQLEEIEKEQ 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 294862453 1287 -EASDHLKKQFETESEVKCN---FRQEAS--RLTLENRDL----EEELDMKDRVIKKLQDQVKTLSK 1343
Cdd:PRK04778 400 eKLSEMLQGLRKDELEAREKlerYRNKLHeiKRYLEKSNLpglpEDYLEMFFEVSDEIEALAEELEE 466
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
845-1378 |
3.16e-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: 49.20 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 845 LARRRYRKMLEEHKAVILQKYARAWLARRRFQSIRRFVLNIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAalragdvE 924
Cdd:pfam02463 185 LAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESS-------K 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 925 KIQKLEAE-----------------------------LEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQI 975
Cdd:pfam02463 258 QEIEKEEEklaqvlkenkeeekekklqeeelkllakeEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 976 QLKLQEKTE--ELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQdYEKQIQSLKEEIKALKDEKMQ----LQHLVEG 1049
Cdd:pfam02463 338 EELEKELKEleIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE-RLSSAAKLKEEELELKSEEEKeaqlLLELARQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1050 EHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKmseITKQLLESYDIEDVRSRLSVEDLE 1129
Cdd:pfam02463 417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK---SEDLLKETQLVKLQEQLELLLSRQ 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1130 HLNEDGELWFAYEGLKKATRVLESHFQSQKDCYE------KEIEALNFKVVHLS----------QEINHLQKLFREENDI 1193
Cdd:pfam02463 494 KLEERSQKESKARSGLKVLLALIKDGVGGRIISAhgrlgdLGVAVENYKVAISTavivevsataDEVEERQKLVRALTEL 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1194 NESIRHEVTRLTSENM-----MIPDFKQQISELEKQKQDLEIRLNEQAEK---MKGKLEELSNQLHRSQEEEGTQRKALE 1265
Cdd:pfam02463 574 PLGARKLRLLIPKLKLplksiAVLEIDPILNLAQLDKATLEADEDDKRAKvveGILKDTELTKLKESAKAKESGLRKGVS 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1266 AQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTL---- 1341
Cdd:pfam02463 654 LEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEaqdk 733
|
570 580 590
....*....|....*....|....*....|....*..
gi 294862453 1342 SKTIGKANDVHSSSGPKEYLGMLQYKREDEAKLIQNL 1378
Cdd:pfam02463 734 INEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELS 770
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
886-1085 |
4.16e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 886 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKH- 964
Cdd:COG4942 38 ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 965 ---------NSELETQKEQIQLKLQEKTEELKEKMDNLTKQLfddvQKEERQRMLLEKsfelKTQDYEKQIQSLKEEIKA 1035
Cdd:COG4942 118 rqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADL----AELAALRAELEA----ERAELEALLAELEEERAA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 294862453 1036 LKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQK 1085
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
884-1110 |
4.19e-05 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 46.66 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 884 NIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLaalragdvekiqKLEAELEKAATHRrnyeeKGKRYRDaVEEKLAKLQK 963
Cdd:pfam17078 19 NLQLTVQSQNLLSKLEIAQQKESKFLENLASL------------KHENDNLSSMLNR-----KERRLKD-LEDQLSELKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 964 HNSELETQKEQIQLKLQEKTE---ELKEKMDNLTKQLFDDVQKEERQRmlleksfelktQDYEKQIQSLKEEIKALK-DE 1039
Cdd:pfam17078 81 SYEELTESNKQLKKRLENSSAsetTLEAELERLQIQYDALVDSQNEYK-----------DHYQQEINTLQESLEDLKlEN 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 294862453 1040 KMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKE--IELLQ-----AQKIDVEKHVQSQKrEMREKMSEITKQL 1110
Cdd:pfam17078 150 EKQLENYQQRISSNDKDIDTKLDSYNNKFKNLDNIYVNknNKLLTkldslAQLLDLPSWLNLYP-ESRNKILEYAEKM 226
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1195-1370 |
4.62e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1195 ESIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKE 1274
Cdd:TIGR02169 240 EAIERQLASLEEE---LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1275 KEKLIDKIQEMQEASDHLKKQFEtesevkcNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVHSS 1354
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIE-------ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
170
....*....|....*.
gi 294862453 1355 SgpKEYLGMLQYKRED 1370
Cdd:TIGR02169 390 Y--REKLEKLKREINE 403
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
893-1329 |
5.00e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.25 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 893 RLQKKLEDqnkenhgLVEKLTSLAALrAGDVEKIQK----LEAElEKAAThRRNYEEKGKRYRDAvEEKLAKLQKHNSEL 968
Cdd:pfam01576 577 RLQQELDD-------LLVDLDHQRQL-VSNLEKKQKkfdqMLAE-EKAIS-ARYAEERDRAEAEA-REKETRALSLARAL 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 969 ETQKEQIQlKLQEKTEELKEKMDNLTKQLfDDVQKE----ERQRMLLEKSF-ELKTQdyekqIQSLKEEIKALKDEKMQL 1043
Cdd:pfam01576 646 EEALEAKE-ELERTNKQLRAEMEDLVSSK-DDVGKNvhelERSKRALEQQVeEMKTQ-----LEELEDELQATEDAKLRL 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1044 QhlvegehVTSDGLKAEvarlskqvktiseFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQL---------LESy 1114
Cdd:pfam01576 719 E-------VNMQALKAQ-------------FERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRaqavaakkkLEL- 777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1115 DIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCY------EKEIEALNFKVVHLSQEINHLQKLFR 1188
Cdd:pfam01576 778 DLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILaqskesEKKLKNLEAELLQLQEDLAASERARR 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1189 EENDINESIRHEVTRLTSENMMIPDFKQQIS--------ELEKQKQDLEIrLNEQAEKMKGKLEELSNQL----HRSQEE 1256
Cdd:pfam01576 858 QAQQERDELADEIASGASGKSALQDEKRRLEariaqleeELEEEQSNTEL-LNDRLRKSTLQVEQLTTELaaerSTSQKS 936
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 294862453 1257 EGTqRKALEAQNeihtkeKEkLIDKIQEMqeasdhlkkqfetESEVKCNFRQEASRLTLENRDLEEELDMKDR 1329
Cdd:pfam01576 937 ESA-RQQLERQN------KE-LKAKLQEM-------------EGTVKSKFKSSIAALEAKIAQLEEQLEQESR 988
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
923-1100 |
6.00e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.90 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 923 VEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKhnsELETQKEQIQLKLQEKTEELKEKMDNLTKQLfddvq 1002
Cdd:PRK00409 522 IASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQE---EEDKLLEEAEKEAQQAIKEAKKEADEIIKEL----- 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1003 keerQRMLLEKSFELKTQDYEKQIQSLKEEIKAL---KDEKMQLQH-LVEGEHV--TSDGLKAEVARLSKQVKTISEF-- 1074
Cdd:PRK00409 594 ----RQLQKGGYASVKAHELIEARKRLNKANEKKekkKKKQKEKQEeLKVGDEVkyLSLGQKGEVLSIPDDKEAIVQAgi 669
|
170 180 190
....*....|....*....|....*....|..
gi 294862453 1075 ------EKEIELLQAQKIDVEKHVQSQKREMR 1100
Cdd:PRK00409 670 mkmkvpLSDLEKIQKPKKKKKKKPKTVKPKPR 701
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1092-1336 |
6.08e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1092 VQSQKREMREKMSEITKQL--LESYDIEDV----RSRLS--VEDLEHLNEDGElwFAYEGLKKATRVLESHFQSQK--DC 1161
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIeeKEEKDLHERlnglESELAelDEEIERYEEQRE--QARETRDEADEVLEEHEERREelET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1162 YEKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSE----NMMIPDFKQQISELEKQKQDLEIRL----- 1232
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEagldDADAEAVEARREELEDRDEELRDRLeecrv 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1233 -----NEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKL--IDK-IQEMQEASDHLKKQFETESEVKC 1304
Cdd:PRK02224 336 aaqahNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIeeLEEeIEELRERFGDAPVDLGNAEDFLE 415
|
250 260 270
....*....|....*....|....*....|..
gi 294862453 1305 NFRQEASRLTLENRDLEEELDMKDRVIKKLQD 1336
Cdd:PRK02224 416 ELREERDELREREAELEATLRTARERVEEAEA 447
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
978-1352 |
8.56e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 978 KLQEKTEELKEKMDNLTKQLFD-DVQKEERQRMLLE--------KSFELKTQDYEKQIQSLKEEIKALKDEKmqlqhlve 1048
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNiDYLEEKLKSSNLElenikkqiADDEKSHSITLKEIERLSIEYNNAMDDY-------- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1049 gehvtsDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHV----QSQKREMR-------EKMSEITKQLLESYDIE 1117
Cdd:PRK01156 235 ------NNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNnyykELEERHMKiindpvyKNRNYINDYFKYKNDIE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1118 DVRSRLSvedlehlNEDGELWFAYEGLKKATrVLESHF------QSQKDCYEKEIEAL---NFKVVHLSQEINHLQKLFR 1188
Cdd:PRK01156 309 NKKQILS-------NIDAEINKYHAIIKKLS-VLQKDYndyikkKSRYDDLNNQILELegyEMDYNSYLKSIESLKKKIE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1189 EENDINESIRHEVTRLTSENMMIPD-FKQQISELEKQKQDLEIR---LNEQAEKMKGKLEELSnqlhRSQEEEGTQRKAL 1264
Cdd:PRK01156 381 EYSKNIERMSAFISEILKIQEIDPDaIKKELNEINVKLQDISSKvssLNQRIRALRENLDELS----RNMEMLNGQSVCP 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1265 EAQNEIHTKEKEKLIDKIQEmqEASDHLKKQFETESEVKC---NFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTL 1341
Cdd:PRK01156 457 VCGTTLGEEKSNHIINHYNE--KKSRLEEKIREIEIEVKDideKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDI 534
|
410
....*....|.
gi 294862453 1342 SKTIGKANDVH 1352
Cdd:PRK01156 535 KIKINELKDKH 545
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
932-1325 |
9.11e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.48 E-value: 9.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 932 ELEKAathRRNYEEKGKRYRDAVEEKLAKLQ-----KHNSELETQ--KEQIQLKLQEKTEELKEKMDNLTKQLFD---DV 1001
Cdd:pfam01576 682 ELERS---KRALEQQVEEMKTQLEELEDELQatedaKLRLEVNMQalKAQFERDLQARDEQGEEKRRQLVKQVREleaEL 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1002 QKEERQRMLL---EKSFELKTQDYEKQIQSL----KEEIKALKDEKMQLQHL---VEGEHVTSDGLKAEVARLSKQVKTI 1071
Cdd:pfam01576 759 EDERKQRAQAvaaKKKLELDLKELEAQIDAAnkgrEEAVKQLKKLQAQMKDLqreLEEARASRDEILAQSKESEKKLKNL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1072 sefekEIELLQAQKI-----DVEKHVQSQKREMREkmsEITKQLLESYDIEDVRSRLS--VEDLEHLNEDgelwfayegl 1144
Cdd:pfam01576 839 -----EAELLQLQEDlaaseRARRQAQQERDELAD---EIASGASGKSALQDEKRRLEarIAQLEEELEE---------- 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1145 kkatrvLESHFQSQKDCYEK---EIEALNfkvVHLSQEINHLQKlfreendiNESIRhevtrltsenmmipdfkqqiSEL 1221
Cdd:pfam01576 901 ------EQSNTELLNDRLRKstlQVEQLT---TELAAERSTSQK--------SESAR--------------------QQL 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1222 EKQKQDLEIRLNEQAEKMKGK-------LEELSNQLHRSQEEEGTQRKAleAQNEIHTKEK--EKLIDKIQEMQEASDHL 1292
Cdd:pfam01576 944 ERQNKELKAKLQEMEGTVKSKfkssiaaLEAKIAQLEEQLEQESRERQA--ANKLVRRTEKklKEVLLQVEDERRHADQY 1021
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 294862453 1293 KKQFE-TESEVKCNFRQ------EASRLTLENRDLEEELD 1325
Cdd:pfam01576 1022 KDQAEkGNSRMKQLKRQleeaeeEASRANAARRKLQRELD 1061
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
924-1115 |
1.23e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 924 EKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKEKMDNLTKQL----FD 999
Cdd:COG1340 29 EKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD-ELNEKLNELREELDELRKELaelnKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1000 DVQKEERQRML--LEKSFELKTQDYEK------QIQSLKEEIKALKDEKMQLQHLVEgehvtsdgLKAEVARLSKQVkti 1071
Cdd:COG1340 108 GGSIDKLRKEIerLEWRQQTEVLSPEEekelveKIKELEKELEKAKKALEKNEKLKE--------LRAELKELRKEA--- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 294862453 1072 SEFEKEIELL--QAQKIDVEKHVQSQKR-EMREKMSEITKQLLESYD 1115
Cdd:COG1340 177 EEIHKKIKELaeEAQELHEEMIELYKEAdELRKEADELHKEIVEAQE 223
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
903-1112 |
1.29e-04 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 46.21 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 903 KENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAatHRRNYEEKGKRYRDAVEEKLAKLQKHNSELET--QKEQIQLKLQ 980
Cdd:pfam15742 107 KSQNSLQEKLAQEKSRVADAEEKILELQQKLEHA--HKVCLTDTCILEKKQLEERIKEASENEAKLKQqyQEEQQKRKLL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 981 EKT-EELKEKMDNL----------TKQLFDDVQKEERQRMLLEKsfELKTQD-YEKQIQSLKEEIKALKDEK----MQLQ 1044
Cdd:pfam15742 185 DQNvNELQQQVRSLqdkeaqlemtNSQQQLRIQQQEAQLKQLEN--EKRKSDeHLKSNQELSEKLSSLQQEKealqEELQ 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1045 HLVE--GEHVTS-----DGLKAEVAR----LSKQV----KTISEFEKEIELLQaQKIDVEKHVQSQKREMREKMSEITKQ 1109
Cdd:pfam15742 263 QVLKqlDVHVRKynekhHHHKAKLRRakdrLVHEVeqrdERIKQLENEIGILQ-QQSEKEKAFQKQVTAQNEILLLEKRK 341
|
...
gi 294862453 1110 LLE 1112
Cdd:pfam15742 342 LLE 344
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
956-1085 |
1.68e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 956 EKLAK--LQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEK--------- 1024
Cdd:PRK12704 37 EEEAKriLEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKreeelekke 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 294862453 1025 -QIQSLKEEIKALKDE--KMQLQHLVEGEHVTsdGLKAEVAR--LSKQVK---------TISEFEKEIElLQAQK 1085
Cdd:PRK12704 117 kELEQKQQELEKKEEEleELIEEQLQELERIS--GLTAEEAKeiLLEKVEeearheaavLIKEIEEEAK-EEADK 188
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
845-1343 |
1.90e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 46.27 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 845 LARRRYRKMLEEHKAVILQKYARAWLARRRFQSIRRfvlNIQLTYRVQRLQKKLEDQNKENHGLVE----KLTSLAALRA 920
Cdd:pfam05557 14 LQNEKKQMELEHKRARIELEKKASALKRQLDRESDR---NQELQKRIRLLEKREAEAEEALREQAElnrlKKKYLEALNK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 921 GDVEKIQKLE----------------------AELEKAATH------RRNYEEKGKRYRDAvEEKLAKLQKHNSELETQK 972
Cdd:pfam05557 91 KLNEKESQLAdarevisclknelselrrqiqrAELELQSTNseleelQERLDLLKAKASEA-EQLRQNLEKQQSSLAEAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 973 EQIQ-----LKLQEK-TEELKE---------KMDNLTKQLFDDV---------------QKEERQRML------------ 1010
Cdd:pfam05557 170 QRIKelefeIQSQEQdSEIVKNskselaripELEKELERLREHNkhlnenienklllkeEVEDLKRKLereekyreeaat 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1011 --LEKS-FELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVtsdgLKAEVARLSKQVK----TISEFEKEIELLQA 1083
Cdd:pfam05557 250 leLEKEkLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIV----LKEENSSLTSSARqlekARRELEQELAQYLK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1084 QKIDVE---KHVQSQKREMREKMSEITK------QLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVlesh 1154
Cdd:pfam05557 326 KIEDLNkklKRHKALVRRLQRRVLLLTKerdgyrAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEA---- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1155 fqsQKDCYEKEIEALNFKVVHLSQEInhlqKLFREENDINE--SIRHEVTRLTSENmmiPDFKQQISELEKQKQDLEIRL 1232
Cdd:pfam05557 402 ---QLSVAEEELGGYKQQAQTLEREL----QALRQQESLADpsYSKEEVDSLRRKL---ETLELERQRLREQKNELEMEL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1233 neqaekMKGKLEELSNQ-----LHRSQEEEGTQRKALEAQNEIHTKEKEKL---IDKIQEMQEASDHLKkqfetESEVKC 1304
Cdd:pfam05557 472 ------ERRCLQGDYDPkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIERLkrlLKKLEDDLEQVLRLP-----ETTSTM 540
|
570 580 590
....*....|....*....|....*....|....*....
gi 294862453 1305 NFRqeasrltlENRDLEEELDMKDRVIKKLQDQVKTLSK 1343
Cdd:pfam05557 541 NFK--------EVLDLRKELESAELKNQRLKEVFQAKIQ 571
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1211-1289 |
2.29e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1211 IPDFKQQISELEKQKQDLE---IRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQE 1287
Cdd:COG3883 18 IQAKQKELSELQAELEAAQaelDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
..
gi 294862453 1288 AS 1289
Cdd:COG3883 98 SG 99
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
927-1030 |
2.43e-04 |
|
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: 44.88 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 927 QKLEAELEKAATHRRnyEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEer 1006
Cdd:cd16269 192 ALTEKEKEIEAERAK--AEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKE-- 267
|
90 100
....*....|....*....|....
gi 294862453 1007 QRMLLEKSFELKTQDYEKQIQSLK 1030
Cdd:cd16269 268 QEALLEEGFKEQAELLQEEIRSLK 291
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
886-1129 |
2.49e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 886 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEE------KLA 959
Cdd:TIGR00606 840 TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQdspletFLE 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 960 KLQKHNSELETQKEQIQLKLQEKTEELKEKMDNL---TKQLFDDVQ---------KE-------------ERQRMLLEKS 1014
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgyMKDIENKIQdgkddylkqKEtelntvnaqleecEKHQEKINED 999
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1015 FELKTQDYEKQIQS------------LKEEIKALKDEKMqlQHLVEGEHVTSDGLKAEVARLSKQVKTIsefEKEIELLQ 1082
Cdd:TIGR00606 1000 MRLMRQDIDTQKIQerwlqdnltlrkRENELKEVEEELK--QHLKEMGQMQVLQMKQEHQKLEENIDLI---KRNHVLAL 1074
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 294862453 1083 AQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLE 1129
Cdd:TIGR00606 1075 GRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLD 1121
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
897-1118 |
2.49e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 44.71 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 897 KLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELE-TQKEQI 975
Cdd:pfam06008 41 QIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFaLPSSDL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 976 QLKLQEKTEELKE-KMDNLTKQLFDDVQKEERQRMLLEKSfelktqdyEKQIQSLKEEIKALKDekmQLQHLVeGEHvtS 1054
Cdd:pfam06008 121 SRMLAEAQRMLGEiRSRDFGTQLQNAEAELKAAQDLLSRI--------QTWFQSPQEENKALAN---ALRDSL-AEY--E 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 294862453 1055 DGLKAEVARLSKQVKTISEFEkeiELLQAQKIDVEKHvQSQKREMREKMSEITKQLLESYDIED 1118
Cdd:pfam06008 187 AKLSDLRELLREAAAKTRDAN---RLNLANQANLREF-QRKKEEVSEQKNQLEETLKTARDSLD 246
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
887-1325 |
2.86e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 45.67 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 887 LTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRA--------GDVEKIQKLEAELEKAAT--HRRNYEEKGKRyRDAVEE 956
Cdd:pfam15964 236 LESQVKSLRKDLAESQKTCEDLKERLKHKESLVAastssrvgGLCLKCAQHEAVLAQTHTnvHMQTIERLTKE-RDDLMS 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 957 KLAKLQKHNSELETQK----EQIQLKLQEKTEELKEKMDNLTKqlFDDVQKE-ERQRMLLEKSFELKTQDYEKQIQSLKE 1031
Cdd:pfam15964 315 ALVSVRSSLAEAQQREssayEQVKQAVQMTEEANFEKTKALIQ--CEQLKSElERQKERLEKELASQQEKRAQEKEALRK 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1032 EIKALKDEKMQLQhLVEGEHVTSdgLKAEVARLSKQ-VKTISEFEKEIELLQAQKIDVEK----------HVQSQK---- 1096
Cdd:pfam15964 393 EMKKEREELGATM-LALSQNVAQ--LEAQVEKVTREkNSLVSQLEEAQKQLASQEMDVTKvcgemryqlnQTKMKKdeae 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1097 REMREKMSEITKQL-LESYDIEDVRSRL--SVEDLEHLNEDG-----ELWFAYEGLKKATRVLESHFQ---SQKDCYEKE 1165
Cdd:pfam15964 470 KEHREYRTKTGRQLeIKDQEIEKLGLELseSKQRLEQAQQDAarareECLKLTELLGESEHQLHLTRLekeSIQQSFSNE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1166 IEALNFKVVHLSQEINhlQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKqkqdleiRLNEQAEKMKGKLEE 1245
Cdd:pfam15964 550 AKAQALQAQQREQELT--QKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAK-------KLEEITQKSRSEVEQ 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1246 LSNQ---LHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEmqeasdhLKKQFETESEVKCNFRQEASRLTLENRDLEE 1322
Cdd:pfam15964 621 LSQEkeyLQDRLEKLQKRNEELEEQCVQHGRMHERMKQRLRQ-------LDKHCQATAQQLVQLLSKQNQLFKERQNLTE 693
|
...
gi 294862453 1323 ELD 1325
Cdd:pfam15964 694 EVQ 696
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1150-1347 |
3.54e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1150 VLESHFQSQKDCYEKEIEALNFKVvhlSQEINHLQKLFREENDINESIRHEVTRLTSEnmmipdfkqqISELEKQKQDLE 1229
Cdd:PHA02562 188 MKIDHIQQQIKTYNKNIEEQRKKN---GENIARKQNKYDELVEEAKTIKAEIEELTDE----------LLNLVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1230 I---RLNEQAEKMKGKLEELSNQLHR----------SQEEEGTQRKALEAQNEIH--TKEKEKLIDKIQEMQEASDHLKK 1294
Cdd:PHA02562 255 AalnKLNTAAAKIKSKIEQFQKVIKMyekggvcptcTQQISEGPDRITKIKDKLKelQHSLEKLDTAIDELEEIMDEFNE 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 294862453 1295 QFETESEVKC---NFRQEASRLTLENRDLEEELD--MKDRV-----IKKLQDQVKTLSKTIGK 1347
Cdd:PHA02562 335 QSKKLLELKNkisTNKQSLITLVDKAKKVKAAIEelQAEFVdnaeeLAKLQDELDKIVKTKSE 397
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1071-1288 |
4.66e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1071 ISEFEKEIELLQAQKidveKHVQSQKREMREKMSEITKQLLE-SYDIEDVRSRLSV--EDLEHLNEDgelwfayegLKKA 1147
Cdd:COG3883 18 IQAKQKELSELQAEL----EAAQAELDALQAELEELNEEYNElQAELEALQAEIDKlqAEIAEAEAE---------IEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1148 TRVLESHFQSQkdcYEKeiealnfkvvhlSQEINHLQKLFrEENDINESIR--HEVTRLTS-ENMMIPDFKQQISELEKQ 1224
Cdd:COG3883 85 REELGERARAL---YRS------------GGSVSYLDVLL-GSESFSDFLDrlSALSKIADaDADLLEELKADKAELEAK 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 294862453 1225 KQDLEIRLNEqAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEA 1288
Cdd:COG3883 149 KAELEAKLAE-LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
890-1138 |
4.86e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 890 RVQRLQKKLEDQNKENHGLVEKLTSLAALRA------GDVEKIQKLEAELEKA---ATHRRNYEEKgkryrdaVEEKLAK 960
Cdd:COG1340 72 KVKELKEERDELNEKLNELREELDELRKELAelnkagGSIDKLRKEIERLEWRqqtEVLSPEEEKE-------LVEKIKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 961 LQKhnsELETQKEQIQLKlqEKTEELKEKMDNLTKQLfddvqKEERQRMlleksfelktQDYEKQIQSLKEEIKALKDEK 1040
Cdd:COG1340 145 LEK---ELEKAKKALEKN--EKLKELRAELKELRKEA-----EEIHKKI----------KELAEEAQELHEEMIELYKEA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1041 MQLQHLVEGEHVTSDGLKAEVARLSKQ----VKTISEFEKEIELLQAQKIDVEKhvQSQKREMREKMSEITKQLLESydi 1116
Cdd:COG1340 205 DELRKEADELHKEIVEAQEKADELHEEiielQKELRELRKELKKLRKKQRALKR--EKEKEELEEKAEEIFEKLKKG--- 279
|
250 260
....*....|....*....|..
gi 294862453 1117 edvrSRLSVEDLEHLNEDGELW 1138
Cdd:COG1340 280 ----EKLTTEELKLLQKSGLLE 297
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
904-1036 |
5.44e-04 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 42.89 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 904 ENHGLVEKLTSLAALRAgdvEKIQKLEAELEKaathRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKT 983
Cdd:pfam06785 66 EKSFLEEKEAKLTELDA---EGFKILEETLEE----LQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFR 138
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 294862453 984 EELKEKMDNLTKQLFDDVQKEERQRMLLEKSFElKTQDYEKQIQSLKEEIKAL 1036
Cdd:pfam06785 139 LESEEQLAEKQLLINEYQQTIEEQRSVLEKRQD-QIENLESKVRDLNYEIKTL 190
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
952-1137 |
5.57e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 952 DAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLfddvqkEERQRMLLEksFELKTQDYEKQIQSLKE 1031
Cdd:PHA02562 191 DHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEI------EELTDELLN--LVMDIEDPSAALNKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1032 EIKALKDEKMQLQ---HLVEGEHV---TSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHV------QSQKREM 1099
Cdd:PHA02562 263 AAAKIKSKIEQFQkviKMYEKGGVcptCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMdefneqSKKLLEL 342
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 294862453 1100 REKMSEItKQLLESY-----DIEDVRSRLSVedlEHLNEDGEL 1137
Cdd:PHA02562 343 KNKISTN-KQSLITLvdkakKVKAAIEELQA---EFVDNAEEL 381
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
890-1129 |
5.65e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 44.68 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 890 RVQRLQKKLEDQNKENhglvEKLTSLAA-----------LRAGdVEKIQKLEAELEkaaTHRRNYEEKG--KRYRDAVEE 956
Cdd:pfam05622 88 KCEELEKEVLELQHRN----EELTSLAEeaqalkdemdiLRES-SDKVKKLEATVE---TYKKKLEDLGdlRRQVKLLEE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 957 KLA-----------KLQKHN---SELETQKEQIQ---LKLQE---KTEELKEKMDNLTKQLfDDVQKeERQRMLLEK--- 1013
Cdd:pfam05622 160 RNAeymqrtlqleeELKKANalrGQLETYKRQVQelhGKLSEeskKADKLEFEYKKLEEKL-EALQK-EKERLIIERdtl 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1014 ----------------------------------SFELKTQDYEKQIQSLKEEIKALK--------DEKMQLQHLVEGEH 1051
Cdd:pfam05622 238 retneelrcaqlqqaelsqadallspssdpgdnlAAEIMPAEIREKLIRLQHENKMLRlgqegsyrERLTELQQLLEDAN 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1052 VTSDGLKAEvARLSKQvktisefekEIELLQAQKIDVEKHVQSQ--KRE----MREKMSEITKQLLESYDiEDVRSRLSV 1125
Cdd:pfam05622 318 RRKNELETQ-NRLANQ---------RILELQQQVEELQKALQEQgsKAEdsslLKQKLEEHLEKLHEAQS-ELQKKKEQI 386
|
....
gi 294862453 1126 EDLE 1129
Cdd:pfam05622 387 EELE 390
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
951-1263 |
5.81e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 44.30 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 951 RDAVEEKLAKLQKHNSELET-----QKE--QIQLKLQEKTEELKEKMDNL--TKQLFDDVQKEERQRMLLeksfelktqD 1021
Cdd:pfam04108 37 RRGLSVQLANLEKVREGLEKvlnelKKDfkQLLKDLDAALERLEETLDKLrnTPVEPALPPGEEKQKTLL---------D 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1022 Y--EKQIQSLKEEIKALKDEkmqlqhlvegehvtsdgLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKH---VQSQK 1096
Cdd:pfam04108 108 FidEDSVEILRDALKELIDE-----------------LQAAQESLDSDLKRFDDDLRDLQKELESLSSPSESislIPTLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1097 REMREKMSEItKQLLES----YDiedvrsrLSVEDLEHLNEDGELWFAYegLKKATRVLESHFQSQKDCYE--------- 1163
Cdd:pfam04108 171 KELESLEEEM-ASLLESltnhYD-------QCVTAVKLTEGGRAEMLEV--LENDARELDDVVPELQDRLDemennyerl 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1164 -KEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLE----------IRL 1232
Cdd:pfam04108 241 qKLLEQKNSLIDELLSALQLIAEIQSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLREFYEGFPsaygslllevERR 320
|
330 340 350
....*....|....*....|....*....|.
gi 294862453 1233 NEQAEKMKGKLEELSNQLHRSQEEEGTQRKA 1263
Cdd:pfam04108 321 REWAEKMKKILRKLAEELDRLQEEERKRREK 351
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
892-1041 |
6.36e-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: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 892 QRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQ 971
Cdd:smart00787 147 EGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKK 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294862453 972 KEQIQLKLQEKTEELkEKMDNLTKQLFDDVQKEERQRmlleksfeLKTQDYE-KQIQSLKEEIKALKDEKM 1041
Cdd:smart00787 227 LEELEEELQELESKI-EDLTNKKSELNTEIAEAEKKL--------EQCRGFTfKEIEKLKEQLKLLQSLTG 288
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
842-1036 |
6.93e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 6.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 842 RGFLARRRYRKMLEEHKAVILQKYARAWLARRRFQSIRRFVLNIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAG 921
Cdd:COG1196 583 RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSL 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 922 DVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQI--QLKLQEKTEELKEKMDNLTKQLFD 999
Cdd:COG1196 663 TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERleEELEEEALEEQLEAEREELLEELL 742
|
170 180 190
....*....|....*....|....*....|....*..
gi 294862453 1000 DVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKAL 1036
Cdd:COG1196 743 EEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
772-1308 |
7.48e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 772 QRKKFLRERRAALIIQQyfrgQQTVRKAITAVALKEAWAAIIIQKHcrgylvrslyQLIRMATITMQAYSRGFLARRRYR 851
Cdd:COG1196 309 ERRRELEERLEELEEEL----AELEEELEELEEELEELEEELEEAE----------EELEEAEAELAEAEEALLEAEAEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 852 KMLEEHKAVILQKYARAwLARRRFQSIRRFVLNIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEA 931
Cdd:COG1196 375 AEAEEELEELAEELLEA-LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 932 ELEKAATHRRNYEEKGKRY---RDAVEEKLAKLQKHNSELETQKEQIQLKLQE----KTEELKEKMDNLTKQLFDDVQKE 1004
Cdd:COG1196 454 LEEEEEALLELLAELLEEAallEAALAELLEELAEAAARLLLLLEAEADYEGFlegvKAALLLAGLRGLAGAVAVLIGVE 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1005 ERQRMLLEKSFELKTQDY--------EKQIQSLKEE------------IKALKDEKMQLQHLVEGEHVtsDGLKAEVARL 1064
Cdd:COG1196 534 AAYEAALEAALAAALQNIvveddevaAAAIEYLKAAkagratflpldkIRARAALAAALARGAIGAAV--DLVASDLREA 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1065 SKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDGElwfAYEGL 1144
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE---LAERL 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1145 KKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQ 1224
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE 768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1225 KQDLEIRL------NEQAekmkgkLEELsnqlhrsqEEEGTQRKALEAQNEIHTKEKEKLIDKIQEM-QEASDHLKKQFE 1297
Cdd:COG1196 769 LERLEREIealgpvNLLA------IEEY--------EELEERYDFLSEQREDLEEARETLEEAIEEIdRETRERFLETFD 834
|
570
....*....|.
gi 294862453 1298 tesEVKCNFRQ 1308
Cdd:COG1196 835 ---AVNENFQE 842
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
952-1062 |
7.49e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.30 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 952 DAVEEKLAKLQKHNSELETQKEQI----QLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEK--Q 1025
Cdd:COG0542 407 DSKPEELDELERRLEQLEIEKEALkkeqDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRygK 486
|
90 100 110
....*....|....*....|....*....|....*..
gi 294862453 1026 IQSLKEEIKALKDEKMQLQHLVEgEHVTSDglkaEVA 1062
Cdd:COG0542 487 IPELEKELAELEEELAELAPLLR-EEVTEE----DIA 518
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
885-1129 |
7.92e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.46 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 885 IQLTYRVQRLQKKLEDQNKENHGLVEKLTSlaalragdvEKIQKLEAELEKAATHRrnYEEKGkryrdaVEEKLAKLQKH 964
Cdd:PLN03229 432 RELEGEVEKLKEQILKAKESSSKPSELALN---------EMIEKLKKEIDLEYTEA--VIAMG------LQERLENLREE 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 965 NSELETQKEQIQLKLQEKTEELKEKMD-NLT--------KQLFDDVQKEERQRMLLE---KSFELKtQDYEKQIQS---- 1028
Cdd:PLN03229 495 FSKANSQDQLMHPVLMEKIEKLKDEFNkRLSrapnylslKYKLDMLNEFSRAKALSEkksKAEKLK-AEINKKFKEvmdr 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1029 --LKEEIKALKDEKMQLQHLVEGEhvTSDGLKAEVARLSKQV-----KTISEFEKEIELLQAQKIDVEKHVQSQkrEMRE 1101
Cdd:PLN03229 574 peIKEKMEALKAEVASSGASSGDE--LDDDLKEKVEKMKKEIelelaGVLKSMGLEVIGVTKKNKDTAEQTPPP--NLQE 649
|
250 260 270
....*....|....*....|....*....|..
gi 294862453 1102 KMS----EITKQLLESYDIEDVRSRLSVEDLE 1129
Cdd:PLN03229 650 KIEslneEINKKIERVIRSSDLKSKIELLKLE 681
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1215-1345 |
8.76e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.86 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1215 KQQISELEKQKQDLEirlnEQAEKMKGKLEELSNQLHRSqEEEGTQRKALEAQNEIHTKEKEKLID----------KIQE 1284
Cdd:pfam05667 334 EEELEELQEQLEDLE----SSIQELEKEIKKLESSIKQV-EEELEELKEQNEELEKQYKVKKKTLDllpdaeeniaKLQA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1285 MQEASD----HLKKQFET----------ESEVKCNFRQEASRLTLEN--------RDLEEELDMKDRVIKKLQDQVKTLS 1342
Cdd:pfam05667 409 LVDASAqrlvELAGQWEKhrvplieeyrALKEAKSNKEDESQRKLEEikelrekiKEVAEEAKQKEELYKQLVAEYERLP 488
|
...
gi 294862453 1343 KTI 1345
Cdd:pfam05667 489 KDV 491
|
|
| YkyA |
pfam10368 |
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ... |
895-1043 |
8.91e-04 |
|
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.
Pssm-ID: 431235 [Multi-domain] Cd Length: 185 Bit Score: 42.19 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 895 QKKLEDQNKENHGLVEKLTSLAAlraGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKeq 974
Cdd:pfam10368 24 QEPLVELEKKEQELYEEIIELGM---DEFDEIKKLSDEALENVEEREELLEKEKESIEEAKEEFKKIKEIIEEIEDEE-- 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 294862453 975 iqlkLQEKTEELKEKMDNLTK---QLFDDVQK---EERQ--RMLLEKSFELKtqDYEKQIQSLKEEIKALKDEKMQL 1043
Cdd:pfam10368 99 ----LKKEAEELIDAMEERYEaydELYDAYKKaleLDKElyEMLKDEDLTLE--ELQEQIEKINESYEEVKEANEQF 169
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
960-1131 |
9.03e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.47 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 960 KLQKHNSELETQK----------EQIQLKLQEKTEELKEKMDNLTKQlfddvqkeerqrMLLEKSFELKTQDYEkqiQSL 1029
Cdd:smart00787 120 QLVKTFARLEAKKmwyewrmkllEGLKEGLDENLEGLKEDYKLLMKE------------LELLNSIKPKLRDRK---DAL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1030 KEEIKALKdekmqlQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQS---QKREMREKMSEI 1106
Cdd:smart00787 185 EEELRQLK------QLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDltnKKSELNTEIAEA 258
|
170 180
....*....|....*....|....*...
gi 294862453 1107 TKQLLES--YDIEDVRS-RLSVEDLEHL 1131
Cdd:smart00787 259 EKKLEQCrgFTFKEIEKlKEQLKLLQSL 286
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
890-1024 |
1.23e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 41.14 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 890 RVQRLQKKLEDQNKENHGLVEKLTSLAAlragdveKIQKLEAELEKAathrrnyEEKGKRYRDAVEEKLAK------LQK 963
Cdd:pfam12718 15 RAEELEEKVKELEQENLEKEQEIKSLTH-------KNQQLEEEVEKL-------EEQLKEAKEKAEESEKLktnnenLTR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 294862453 964 HNSELETQKEQIQLKLQEKTEELKEkMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEK 1024
Cdd:pfam12718 81 KIQLLEEELEESDKRLKETTEKLRE-TDVKAEHLERKVQALEQERDEWEKKYEELEEKYKE 140
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
948-1345 |
1.38e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.89 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 948 KRYRDAVEEKLA--KLQKHNSELETQKEQIQLKLQeKTEELKEKMDNLtkQLFDDVQKEERQRMLLEKSFELKTQDYEKQ 1025
Cdd:TIGR01612 466 KRFFEIFEEEWGsyDIKKDIDENSKQDNTVKLILM-RMKDFKDIIDFM--ELYKPDEVPSKNIIGFDIDQNIKAKLYKEI 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1026 IQSLKEEIKALKD-EKMQLQHLVEGEHVTSDGLKaevarLSKQVKTIseFEKEIELlqaqkIDVEKHVQSQKREMREKMS 1104
Cdd:TIGR01612 543 EAGLKESYELAKNwKKLIHEIKKELEEENEDSIH-----LEKEIKDL--FDKYLEI-----DDEIIYINKLKLELKEKIK 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1105 EITKQ---LLESYDIEDV--RSRLSVEDLEHLNEdgelWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQE 1179
Cdd:TIGR01612 611 NISDKneyIKKAIDLKKIieNNNAYIDELAKISP----YQVPEHLKNKDKIYSTIKSELSKIYEDDIDALYNELSSIVKE 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1180 --INHLQKLFREEnDINESIRHEVTRLtsENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGkleELSNQLHRSQEEe 1257
Cdd:TIGR01612 687 naIDNTEDKAKLD-DLKSKIDKEYDKI--QNMETATVELHLSNIENKKNELLDIIVEIKKHIHG---EINKDLNKILED- 759
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1258 gtqrkaleaqneIHTKEKEkLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQ 1337
Cdd:TIGR01612 760 ------------FKNKEKE-LSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIK 826
|
....*...
gi 294862453 1338 VKTLSKTI 1345
Cdd:TIGR01612 827 EDEIFKII 834
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1183-1341 |
1.63e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1183 LQKLFREENDINE---SIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLhRSQEEEGT 1259
Cdd:COG3883 25 LSELQAELEAAQAeldALQAELEELNEE---YNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA-RALYRSGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1260 QRKALE----------------AQNEIHTKEKEkLIDKIQEMQEASDHLKKQFETESEvkcNFRQEASRLTLENRDLEEE 1323
Cdd:COG3883 101 SVSYLDvllgsesfsdfldrlsALSKIADADAD-LLEELKADKAELEAKKAELEAKLA---ELEALKAELEAAKAELEAQ 176
|
170
....*....|....*...
gi 294862453 1324 LDMKDRVIKKLQDQVKTL 1341
Cdd:COG3883 177 QAEQEALLAQLSAEEAAA 194
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
904-1134 |
1.69e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.90 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 904 ENHGLVEKL-TSLAALRAgDVEKIQKLEAELEK---------AATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKE 973
Cdd:PRK04778 195 EAREILDQLeEELAALEQ-IMEEIPELLKELQTelpdqlqelKAGYRELVEEGYHLDHLDIEKEIQDLKEQIDENLALLE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 974 QIQLK-LQEKTEELKEKMDNL-----------------TKQLFDDVQKEERQ-RMLLE------KSFELKTQDYEKQiQS 1028
Cdd:PRK04778 274 ELDLDeAEEKNEEIQERIDQLydilerevkarkyveknSDTLPDFLEHAKEQnKELKEeidrvkQSYTLNESELESV-RQ 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1029 LKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEI-ELLQAQKIDvEKHVQSQKREMREKMSEIt 1107
Cdd:PRK04778 353 LEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLsEMLQGLRKD-ELEAREKLERYRNKLHEI- 430
|
250 260 270
....*....|....*....|....*....|...
gi 294862453 1108 KQLLESYDI----EDVRSRL--SVEDLEHLNED 1134
Cdd:PRK04778 431 KRYLEKSNLpglpEDYLEMFfeVSDEIEALAEE 463
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
884-1374 |
1.71e-03 |
|
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: 43.27 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 884 NIQLTYRVQRLQKKLEDQNKENHGLVEKLTSlAALRAGDVEKIQKLEAE--LEKAATHRRNYEEKgKRYRDAVEEKLAKL 961
Cdd:pfam10174 69 NQHLQLTIQALQDELRAQRDLNQLLQQDFTT-SPVDGEDKFSTPELTEEnfRRLQSEHERQAKEL-FLLRKTLEEMELRI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 962 QKHNSELETQKEQIQlKLQEKTEelkekMDNLTKQLFDDVQkeERQRMLLEksFELKTQDYEKQIQSLKEEIKALKDE-- 1039
Cdd:pfam10174 147 ETQKQTLGARDESIK-KLLEMLQ-----SKGLPKKSGEEDW--ERTRRIAE--AEMQLGHLEVLLDQKEKENIHLREElh 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1040 -KMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQ-KIDVEKH---------VQSQKREMREKMSEItK 1108
Cdd:pfam10174 217 rRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNgLLHTEDReeeikqmevYKSHSKFMKNKIDQL-K 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1109 QLLESYDIEDVRSRLSVEDLEHLNEDGELWFayEGLKKATRVLE---SHFQSQKDCYEKEIEAlnfKVVHLSQEINHLQK 1185
Cdd:pfam10174 296 QELSKKESELLALQTKLETLTNQNSDCKQHI--EVLKESLTAKEqraAILQTEVDALRLRLEE---KESFLNKKTKQLQD 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1186 LFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNqlhrSQEEEGTQRKALe 1265
Cdd:pfam10174 371 LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSN----TDTALTTLEEAL- 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1266 aqneihtKEKEKLIDKIQEMQEASDHlkkqfetesevkcNFRQEASRLTLENRDLEEELDM-------KDRVIKKLQDQV 1338
Cdd:pfam10174 446 -------SEKERIIERLKEQREREDR-------------ERLEELESLKKENKDLKEKVSAlqpelteKESSLIDLKEHA 505
|
490 500 510
....*....|....*....|....*....|....*.
gi 294862453 1339 KTLSKTIGKANdvhssSGPKEYLGMLQYKREDEAKL 1374
Cdd:pfam10174 506 SSLASSGLKKD-----SKLKSLEIAVEQKKEECSKL 536
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
810-828 |
1.73e-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: 1.73e-03
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1023-1238 |
1.74e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1023 EKQIQSLKEEIKALKDEKMQLQHLVegehvtsDGLKAEVARLSKQVKTIsefEKEIELLQAQKIDVEKHVQSQKREMREK 1102
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAEL-------DALQAELEELNEEYNEL---QAELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1103 MSEITKQ----------------LLESYDIEDVRSRLSVedLEHLNE-DGELwfaYEGLKKATRVLEshfqSQKDCYEKE 1165
Cdd:COG3883 85 REELGERaralyrsggsvsyldvLLGSESFSDFLDRLSA--LSKIADaDADL---LEELKADKAELE----AKKAELEAK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 294862453 1166 IEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLtsenmmipdfKQQISELEKQKQDLEIRLNEQAEK 1238
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA----------EAQLAELEAELAAAEAAAAAAAAA 218
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
886-1076 |
1.85e-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: 42.96 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 886 QLTYRVQRLQK----------KLEDQNKENHGLVEKLT----SLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYR 951
Cdd:pfam07888 77 ELESRVAELKEelrqsrekheELEEKYKELSASSEELSeekdALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 952 DAVEEKLAKLQkhnsELETQKEQIQLKLQEKTEELKEKMDNLtkQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKE 1031
Cdd:pfam07888 157 ERAKKAGAQRK----EEEAERKQLQAKLQQTEEELRSLSKEF--QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEA 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 294862453 1032 EIKALKDEKMQLQHLVEGEHVTSDGLKAEVARL-SKQVKTISEFEK 1076
Cdd:pfam07888 231 ENEALLEELRSLQERLNASERKVEGLGEELSSMaAQRDRTQAELHQ 276
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
999-1300 |
1.99e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.93 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 999 DDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKalKDEKMQLQHLVEGEhvtsDGLKAEVARLSKQVKTISEFEKEI 1078
Cdd:pfam02029 34 ESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTA--KREERRQKRLQEAL----ERQKEFDPTIADEKESVAERKENN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1079 ELLQAQkiDVEKHVQSQKREMREKMSEITkqllesydiedVRSRlsvEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQ 1158
Cdd:pfam02029 108 EEEENS--SWEKEEKRDSRLGRYKEEETE-----------IREK---EYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1159 KDCYEKEIEALNFK---------VVHLSQEINHL-QKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDL 1228
Cdd:pfam02029 172 ENFAKEEVKDEKIKkekkvkyesKVFLDQKRGHPeVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1229 EIRL------NEQAEKMKGK-------LEEL---SNQLHRSQEEEGTQRKALEAQNEIHTKE-KEKLIDKIqEMQEASDH 1291
Cdd:pfam02029 252 ELRRrrqekeSEEFEKLRQKqqeaeleLEELkkkREERRKLLEEEEQRRKQEEAERKLREEEeKRRMKEEI-ERRRAEAA 330
|
....*....
gi 294862453 1292 LKKQFETES 1300
Cdd:pfam02029 331 EKRQKLPED 339
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
886-1154 |
2.00e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 886 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQkhn 965
Cdd:COG4372 77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK--- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 966 sELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKmqLQH 1045
Cdd:COG4372 154 -ELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSL--EAK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1046 LVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSV 1125
Cdd:COG4372 231 LGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310
|
250 260
....*....|....*....|....*....
gi 294862453 1126 EDLEHLNEDGELWFAYEGLKKATRVLESH 1154
Cdd:COG4372 311 GALEDALLAALLELAKKLELALAILLAEL 339
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1220-1347 |
2.27e-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: 42.11 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1220 ELEKQKQDLEIRLNE---QAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEK---EKLIDKIQEMQEASDHLK 1293
Cdd:pfam15905 160 ELMKLRNKLEAKMKEvmaKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKsetEKLLEYITELSCVSEQVE 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 294862453 1294 KQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGK 1347
Cdd:pfam15905 240 KYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEE 293
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1202-1352 |
2.27e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1202 TRLTSENMMIPDFKQQISELEKQKQDLEIR---LNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKL 1278
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKrdeLNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 294862453 1279 IDKIQEMQEASDHLKKQFEtESEVKCNFRQEASRLTLENRDLEEELDMKD---RVIKKLQDQVKTLSKTIGKANDVH 1352
Cdd:COG1340 81 DELNEKLNELREELDELRK-ELAELNKAGGSIDKLRKEIERLEWRQQTEVlspEEEKELVEKIKELEKELEKAKKAL 156
|
|
| IQ |
pfam00612 |
IQ calmodulin-binding motif; Calmodulin-binding motif. |
810-828 |
2.32e-03 |
|
IQ calmodulin-binding motif; Calmodulin-binding motif.
Pssm-ID: 459869 Cd Length: 21 Bit Score: 36.91 E-value: 2.32e-03
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1052-1335 |
2.39e-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: 42.11 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1052 VTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLE----SYDIEDVRSRLSveD 1127
Cdd:pfam15905 56 VKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREktslSASVASLEKQLL--E 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1128 LEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKlfreenDINESiRHEVTRLTSE 1207
Cdd:pfam15905 134 LTRVNELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQK------NLEHS-KGKVAQLEEK 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1208 NMMIPDFKQQiSELEKQKQDLEIR----LNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQ 1283
Cdd:pfam15905 207 LVSTEKEKIE-EKSETEKLLEYITelscVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCK 285
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 294862453 1284 EMQEASDHLKKQFETESEvkcnfrqeasRLTLENRDLEEELDMKDRVIKKLQ 1335
Cdd:pfam15905 286 LLESEKEELLREYEEKEQ----------TLNAELEELKEKLTLEEQEHQKLQ 327
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1088-1321 |
2.41e-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: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1088 VEKHVQSQKREMREKMSEITKQLlesydiEDVRSRLsvEDLEHlnedgelwfAYEGLKKATRVLEShfQSQKDCYEKEIE 1167
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQL------PELRKEL--EEAEA---------ALEEFRQKNGLVDL--SEEAKLLLQQLS 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1168 ALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLtSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELS 1247
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL-LQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA 301
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 294862453 1248 NQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQfetesevkcnfRQEASRLtleNRDLE 1321
Cdd:COG3206 302 ALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL-----------EAELRRL---EREVE 361
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
895-1301 |
2.59e-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: 42.73 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 895 QKKLEDQNKENHGLVEKLTSLAALRagdvEKIQKLEAELEKAATH---------RRNYEEKGKRYRDAvEEKLAKLQKhn 965
Cdd:TIGR00606 254 LKEIEHNLSKIMKLDNEIKALKSRK----KQMEKDNSELELKMEKvfqgtdeqlNDLYHNHQRTVREK-ERELVDCQR-- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 966 sELETQKEQIQLKLQEKTEELKEKMdnlTKQLFDDVQKEErqrmlleksfelkTQDYEKQIQSLkeeikALKDEKMQLQH 1045
Cdd:TIGR00606 327 -ELEKLNKERRLLNQEKTELLVEQG---RLQLQADRHQEH-------------IRARDSLIQSL-----ATRLELDGFER 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1046 LVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIEllqaqkiDVEKHVQSQKREMREKMSEITKQLlesyDIEDVRSRLSV 1125
Cdd:TIGR00606 385 GPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQ-------SKERLKQEQADEIRDEKKGLGRTI----ELKKEILEKKQ 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1126 EDLEHLNEDGELwfAYEGLKKATRVLESHFQSQKDCYEKE----IEALNFKVVHLSQEINHLQKLFREENDINESIRHEV 1201
Cdd:TIGR00606 454 EELKFVIKELQQ--LEGSSDRILELDQELRKAERELSKAEknslTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHT 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1202 TRLTSENMMIPD---FKQQISELEKQKQDLEI-----------------RLNEQAEKMKGKLEELSNQLHRSQEEEGTQR 1261
Cdd:TIGR00606 532 TTRTQMEMLTKDkmdKDEQIRKIKSRHSDELTsllgyfpnkkqledwlhSKSKEINQTRDRLAKLNKELASLEQNKNHIN 611
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 294862453 1262 KALEAQNEIHTKEKEKLIDKIQEMQEASD--HLKKQFETESE 1301
Cdd:TIGR00606 612 NELESKEEQLSSYEDKLFDVCGSQDEESDleRLKEEIEKSSK 653
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
1213-1376 |
2.72e-03 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 40.91 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1213 DFKQQISELEKQKQDLEIRLNEQaekmkgkLEELSNQLHRSQEEEGTQRKALEAQNEIhTKEKEKLIDKIQEMQEASDHL 1292
Cdd:pfam14988 26 QYVQECEEIERRRQELASRYTQQ-------TAELQTQLLQKEKEQASLKKELQALRPF-AKLKESQEREIQDLEEEKEKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1293 KKQF-ETESEVKCNFRQEASRLTLENRDLeEELDMKDRVIKKLQDQVKTLSKTIGKANDVHSSSGPKEYlgmlQYKREDE 1371
Cdd:pfam14988 98 RAETaEKDREAHLQFLKEKALLEKQLQEL-RILELGERATRELKRKAQALKLAAKQALSEFCRSIKREN----RQLQKEL 172
|
....*
gi 294862453 1372 AKLIQ 1376
Cdd:pfam14988 173 LQLIQ 177
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
926-1291 |
2.80e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.73 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 926 IQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQK---------HNSELETQKEQIQLKLQEKteelKEKMDNLtKQ 996
Cdd:TIGR01612 1120 IKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDvadkaisndDPEEIEKKIENIVTKIDKK----KNIYDEI-KK 1194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 997 LFDDVQKEERQRMLLEKSFELKTQdYEKQIQSLKEEikALKDEKMQLQHLV---EGEHVTSDGLKAEVARLSKQVKTISE 1073
Cdd:TIGR01612 1195 LLNEIAEIEKDKTSLEEVKGINLS-YGKNLGKLFLE--KIDEEKKKSEHMIkamEAYIEDLDEIKEKSPEIENEMGIEMD 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1074 FEKEIELLQAQKIDVEKH-VQSQKR-----EMREKMSEITKQLLESYDIEDVRSRLSvedlehlnedgelwfayeglkka 1147
Cdd:TIGR01612 1272 IKAEMETFNISHDDDKDHhIISKKHdenisDIREKSLKIIEDFSEESDINDIKKELQ----------------------- 1328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1148 TRVLESH-FQSQKDCYEKEIEALnFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISeLEKQKQ 1226
Cdd:TIGR01612 1329 KNLLDAQkHNSDINLYLNEIANI-YNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDIN-LEECKS 1406
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 294862453 1227 DLEIRL-----NEQAEKMKGK-----LEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDH 1291
Cdd:TIGR01612 1407 KIESTLddkdiDECIKKIKELknhilSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDH 1481
|
|
| TBCA |
pfam02970 |
Tubulin binding cofactor A; |
1144-1248 |
2.80e-03 |
|
Tubulin binding cofactor A;
Pssm-ID: 460769 [Multi-domain] Cd Length: 99 Bit Score: 39.03 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1144 LKKATRVLEsHFQSQKDCYEKEIEalnfkvvhlsQEINHLQKLFREENDINEsIRHEVTRLTSENMMIPDFKQQIselEK 1223
Cdd:pfam02970 6 LKIKTGVVK-RLVKEEASYEKELE----------EQEARLEKLKADGADEYD-LKKQEEVLEETKAMIPDLKKRL---EE 70
|
90 100
....*....|....*....|....*
gi 294862453 1224 QKQDLEIRLNEQAEKMKGkLEELSN 1248
Cdd:pfam02970 71 AVEDLEEFLEEEEDLGAD-TEELTA 94
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1215-1341 |
3.13e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1215 KQQISELEKQKQDLEIRL---NEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEihtkEKEKLIDKIQEMQEASDH 1291
Cdd:COG4372 51 REELEQAREELEQLEEELeqaRSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE----EAEELQEELEELQKERQD 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 294862453 1292 LKkqfetesevkcnfrQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTL 1341
Cdd:COG4372 127 LE--------------QQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
|
| DUF6262 |
pfam19776 |
Family of unknown function (DUF6262); This family of proteins, functionally uncharacterized, ... |
942-1043 |
3.63e-03 |
|
Family of unknown function (DUF6262); This family of proteins, functionally uncharacterized, is found in bacteria. Proteins in this family are typically between 124 and 143 amino acids in length. Some members included in this family are hypothetical transposases, associated with transposon Tn554. There is a conserved sequence GV/LSR/K and a highly conserved tyrosine residue.
Pssm-ID: 466180 [Multi-domain] Cd Length: 110 Bit Score: 38.75 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 942 NYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQL-KLQEKT----------EELKEKMDNLTKQlfddvQKE--ERQR 1008
Cdd:pfam19776 1 KYDKMVELNRKESEEKIELAKKAIQEMLEEGEKITVpELVKRTglsrgffyknPEVRRELDEAIEQ-----QGGmvNPKR 75
|
90 100 110
....*....|....*....|....*....|....*
gi 294862453 1009 MLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQL 1043
Cdd:pfam19776 76 EILDMALEKRIELLKKEIKELKRENEELKKENEKL 110
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1025-1286 |
3.67e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1025 QIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKA---EVARLSKQV----KTISEFEKEIELLQAQKIDVEKHVQSQKR 1097
Cdd:PRK01156 160 EINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSsnlELENIKKQIaddeKSHSITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1098 EMREKMS-EITKQLLESyDIEDVRSRLSVEdLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHL 1176
Cdd:PRK01156 240 ALNELSSlEDMKNRYES-EIKTAESDLSME-LEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNI 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1177 SQEINHLQKLFREENDInESIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNEqAEKMKGKLEELSNQLHRSQEE 1256
Cdd:PRK01156 318 DAEINKYHAIIKKLSVL-QKDYNDYIKKKSR---YDDLNNQILELEGYEMDYNSYLKS-IESLKKKIEEYSKNIERMSAF 392
|
250 260 270
....*....|....*....|....*....|
gi 294862453 1257 EGTQRKALEAQNEIHTKEKEKLIDKIQEMQ 1286
Cdd:PRK01156 393 ISEILKIQEIDPDAIKKELNEINVKLQDIS 422
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
986-1254 |
3.83e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 986 LKEKMDNLTKQL-------FDDVQKEErQRMLLEKSFELKTQDYEK--QIQSLKEEIKALKDEKMQLQHLVegehvTSDG 1056
Cdd:PRK05771 14 LKSYKDEVLEALhelgvvhIEDLKEEL-SNERLRKLRSLLTKLSEAldKLRSYLPKLNPLREEKKKVSVKS-----LEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1057 LKAEVARLSKQVKTISEFEKEIELLQaqkidvekhvqSQKREMREKMSEITKqlLESYDIedvrsrlsveDLEHLNeDGE 1136
Cdd:PRK05771 88 IKDVEEELEKIEKEIKELEEEISELE-----------NEIKELEQEIERLEP--WGNFDL----------DLSLLL-GFK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1137 LWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFRE-------ENDINESIrhEVTRLtsenm 1209
Cdd:PRK05771 144 YVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEElkklgfeRLELEEEG--TPSEL----- 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 294862453 1210 mIPDFKQQISELEKQKQDLEIRLNEQAEK----MKGKLEELSNQLHRSQ 1254
Cdd:PRK05771 217 -IREIKEELEEIEKERESLLEELKELAKKyleeLLALYEYLEIELERAE 264
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
886-1110 |
4.11e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 886 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYR--DAVEEKLAKLQK 963
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQleELEQEIAALLAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 964 HNSELETQKEQIQLKLQEKtEELKEKMDNLTKQLfDDVQKEERQRMLLEKSFELKT--QDYEKQIQSLKEEIKALKDEKM 1041
Cdd:COG4717 379 AGVEDEEELRAALEQAEEY-QELKEELEELEEQL-EELLGELEELLEALDEEELEEelEELEEELEELEEELEELREELA 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 294862453 1042 QLQHLVE--GEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKR-EMREKMSEITKQL 1110
Cdd:COG4717 457 ELEAELEqlEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLpPVLERASEYFSRL 528
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
954-1168 |
4.46e-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: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 954 VEEKLAKLQKH---NSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEER-----QRMLLEKSFELktQDYEKQ 1025
Cdd:pfam05701 231 AEEELQRLNQQllsAKDLKSKLETASALLLDLKAELAAYMESKLKEEADGEGNEKKtstsiQAALASAKKEL--EEVKAN 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1026 IQSLKEEIKALKDEKMQLQHLVEGEhvtsdglKAEVARLSKQ----VKTISEFEKEIELLQaQKIDVekhVQSQKREMRE 1101
Cdd:pfam05701 309 IEKAKDEVNCLRVAAASLRSELEKE-------KAELASLRQRegmaSIAVSSLEAELNRTK-SEIAL---VQAKEKEARE 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1102 KMSEITKQLLE-SYDIEDVRS--RLSVEDLEHLNEDGELwfayegLKKATRVLESHFQSQKdcyeKEIEA 1168
Cdd:pfam05701 378 KMVELPKQLQQaAQEAEEAKSlaQAAREELRKAKEEAEQ------AKAAASTVESRLEAVL----KEIEA 437
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
923-1069 |
4.58e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 41.12 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 923 VEKIQKLEAELEKAATHRRNYEEKGKRY---RDAVEEKLAKLQKHNSELETQKEqiqlKLQEKTEELKEKmdnltKQLFD 999
Cdd:pfam02841 154 LEERDKLEAKYNQVPRKGVKAEEVLQEFlqsKEAVEEAILQTDQALTAKEKAIE----AERAKAEAAEAE-----QELLR 224
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294862453 1000 DVQKEERQRMlleksfELKTQDYEKQIQSLKEEIKALKD------EKMQLQHLVEGEHVTSDGLKAEVARLSKQVK 1069
Cdd:pfam02841 225 EKQKEEEQMM------EAQERSYQEHVKQLIEKMEAEREqllaeqERMLEHKLQEQEELLKEGFKTEAESLQKEIQ 294
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1142-1349 |
4.61e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.87 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1142 EGLKKATRVLESHFQSQKDCYEKEIEALNfKVVHLSQEINHLQKLFREENDI-NESIRHEVTRLTSENMMIPDFKQQISE 1220
Cdd:COG5185 186 LGLLKGISELKKAEPSGTVNSIKESETGN-LGSESTLLEKAKEIINIEEALKgFQDPESELEDLAQTSDKLEKLVEQNTD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1221 LEK----QKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEK-LIDKIQEMQEASDHLKKQ 1295
Cdd:COG5185 265 LRLeklgENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQeLEESKRETETGIQNLTAE 344
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 294862453 1296 FETESEvKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKAN 1349
Cdd:COG5185 345 IEQGQE-SLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIP 397
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
924-1139 |
4.67e-03 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 40.97 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 924 EKIQKLEAELEKAAthrRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQK 1003
Cdd:pfam09755 85 KKIQALKKEKETLA---MNYEQEEEFLTNDLSRKLTQLRQEKVELEQTLEQEQEYQVNKLMRKIEKLEAETLNKQTNLEQ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1004 EERQRMLLEKSFElktQDYEKQIQSLKEEIKALKDEKMQLQHLVE-------------GEHVTSDGLKAEVARLSKQVkt 1070
Cdd:pfam09755 162 LRREKVELENTLE---QEQEALVNRLWKRMDKLEAEKRLLQEKLDqpvsappsprdstSEGDTAQNLTAHIQYLRKEV-- 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 294862453 1071 iSEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDGELWF 1139
Cdd:pfam09755 237 -ERLRRQLATAQQEHTEKMAQYAQEERHIREENLRLQRKLQLEMERREALCRHLSESESSLEMDEERYF 304
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
959-1042 |
5.34e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.10 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 959 AKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQlfddvQKEERqrmllEKSFELKTQDYEKQIQSLKEEIKALKD 1038
Cdd:smart00935 21 KQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEA-----AREKK-----EKELQKKVQEFQRKQQKLQQDLQKRQQ 90
|
....
gi 294862453 1039 EKMQ 1042
Cdd:smart00935 91 EELQ 94
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
952-1033 |
5.74e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 39.43 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 952 DAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQ--LFDDVQKEERQRML--LEKSFELKTQDYEKQIQ 1027
Cdd:COG2825 32 QRILQESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEaaTLSEEERQKKERELqkKQQELQRKQQEAQQDLQ 111
|
....*.
gi 294862453 1028 SLKEEI 1033
Cdd:COG2825 112 KRQQEL 117
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
885-1021 |
6.90e-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: 41.57 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 885 IQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKR---YRDAVEEKLAKL 961
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRrqqFEEQLVELSTEV 897
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 294862453 962 QKHNSELETQKEQI------QLKLQEKTEEL---KEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQD 1021
Cdd:TIGR00606 898 QSLIREIKDAKEQDspletfLEKDQQEKEELissKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQD 966
|
|
| IQ |
pfam00612 |
IQ calmodulin-binding motif; Calmodulin-binding motif. |
831-851 |
7.32e-03 |
|
IQ calmodulin-binding motif; Calmodulin-binding motif.
Pssm-ID: 459869 Cd Length: 21 Bit Score: 35.37 E-value: 7.32e-03
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
979-1185 |
7.79e-03 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 39.75 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 979 LQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQiqsLKEEIKALKDEKMQLQHLvegehvtsdglk 1058
Cdd:pfam14988 9 LAKKTEEKQKKIEKLWNQYVQECEEIERRRQELASRYTQQTAELQTQ---LLQKEKEQASLKKELQAL------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1059 AEVARLSKQVktisefEKEIELLQAQKIDVEKHVQSQKREMREKMSEiTKQLLESyDIEDVRSRLSVEDLEHlnedgELW 1138
Cdd:pfam14988 74 RPFAKLKESQ------EREIQDLEEEKEKVRAETAEKDREAHLQFLK-EKALLEK-QLQELRILELGERATR-----ELK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 294862453 1139 FAYEGLK-KATRVLESHFQSQKdcyeKEIEALNFKVVHLSQEINHLQK 1185
Cdd:pfam14988 141 RKAQALKlAAKQALSEFCRSIK----RENRQLQKELLQLIQETQALEA 184
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
890-1016 |
7.86e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 38.87 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 890 RVQRLQKKLEDQNKENHGLVEKLtSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRY-RDAVEEKLAKLQKHNSEL 968
Cdd:pfam05672 21 RQAREQREREEQERLEKEEEERL-RKEELRRRAEEERARREEEARRLEEERRREEEERQRKaEEEAEEREQREQEEQERL 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 294862453 969 ETQKEQIQLKLQEKTEELKEKMDNLTkqlfddvQKEERQRMLLEKSFE 1016
Cdd:pfam05672 100 QKQKEEAEAKAREEAERQRQEREKIM-------QQEEQERLERKKRIE 140
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
933-1030 |
7.96e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 40.35 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 933 LEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDV-----QKEERQ 1007
Cdd:pfam02841 195 TDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEKMEAEREQLLAEQermleHKLQEQ 274
|
90 100
....*....|....*....|...
gi 294862453 1008 RMLLEKSFELKTQDYEKQIQSLK 1030
Cdd:pfam02841 275 EELLKEGFKTEAESLQKEIQDLK 297
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1178-1361 |
8.83e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1178 QEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLN-----EQAEKMKGKLEELSNQLHR 1252
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1253 SQEEEgTQRKALEaqneihtKEKEKLIDKIQEMQEASDHLKKQFETESevkcnfRQEASRLTLENRDLEEELDMKDRVIK 1332
Cdd:COG4717 151 LEERL-EELRELE-------EELEELEAELAELQEELEELLEQLSLAT------EEELQDLAEELEELQQRLAELEEELE 216
|
170 180
....*....|....*....|....*....
gi 294862453 1333 KLQDQVKTLSKTIGKANDVHSSSGPKEYL 1361
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALEERL 245
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1188-1297 |
9.47e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1188 REENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEirlnEQAEKMKGKLEELSNQLHRSQEEEgtqRKALEAQ 1267
Cdd:COG2433 392 EEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE----AELEEKDERIERLERELSEARSEE---RREIRKD 464
|
90 100 110
....*....|....*....|....*....|..
gi 294862453 1268 NEIHTKEKE--KLIDKIQEMQEASDHLKKQFE 1297
Cdd:COG2433 465 REISRLDREieRLERELEEERERIEELKRKLE 496
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1072-1327 |
9.65e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 40.71 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1072 SEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEIT-KQLLESYDIED------VRSRLSVED--LEHLNEDGELWFAYE 1142
Cdd:pfam15709 215 SKAEKKSELISKGKKTGAKRKRTQKERNLEVAAELSgPDVINSKETEDasergaFSSDSVVEDpwLSSKYDAEESQVSID 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1143 GLKKATR---VLESHFQSQKDCYEKEIEALNFKvvhLSQEINHLQKLfREENdiNESIRHEVTRLTSENMMIPDFKQQIS 1219
Cdd:pfam15709 295 GRSSPTQtfvVTGNMESEEERSEEDPSKALLEK---REQEKASRDRL-RAER--AEMRRLEVERKRREQEEQRRLQQEQL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294862453 1220 ELEKQ-KQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEasdhlKKQfet 1298
Cdd:pfam15709 369 ERAEKmREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQR-----KKQ--- 440
|
250 260
....*....|....*....|....*....
gi 294862453 1299 esevkcnfrQEASRLTLENRDLEEELDMK 1327
Cdd:pfam15709 441 ---------QEEAERAEAEKQRQKELEMQ 460
|
|
| |
