|
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: 1205.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFAESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01380 1 PAVLHNLKVRFCQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 161 GESGAGKTVSARYAMRYFATVSKSSSN-AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRT 239
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATVGGSSSGeTQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDF 319
Cdd:cd01380 161 YLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 320 QMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARD 399
Cdd:cd01380 241 QMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 400 ALAKKIYAHLFDFIVEQINQALHF--SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMK 477
Cdd:cd01380 321 ALAKHIYAQLFDWIVDRINKALASpvKEKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNK-NSLFEKPRMSNSSFIIQHFADKVE 556
Cdd:cd01380 401 EEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTAFIVKHFADDVE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 557 YQCEGFLEKNRDTVYDMLVEILRASKFHlcaaffqespvpsspfgamitvksakqviKPntkhfrtTVGNKFRSSLYLLM 636
Cdd:cd01380 481 YQVEGFLEKNRDTVSEEHLNVLKASKNR-----------------------------KK-------TVGSQFRDSLILLM 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 637 ETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDKKEV 716
Cdd:cd01380 525 ETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRDDKKKT 604
|
650 660
....*....|....*....|....*
gi 124486759 717 CKVVLHRLIQDSNQYQFGRTKIFFR 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: 959.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 62 NPDILVGENDLTALSYLHEPAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVA 141
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRY-LKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 142 EEAYKQMARNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNA-HVEDKVLASNPITEAVGNAKTTRNDNSSRFGK 220
Cdd:smart00242 80 DNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVgSVEDQILESNPILEAFGNAKTLRNNNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 221 YTEISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDR 300
Cdd:smart00242 160 FIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 301 ADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNE-RSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIV 379
Cdd:smart00242 240 EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDnAASTVKDKEELSNAAELLGVDPEELEKALTKRKIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 380 TSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKL 459
Cdd:smart00242 320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 460 QQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNKNSLFEK 538
Cdd:smart00242 400 QQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKpPGILSLLDEECRFPKGTDQTFLEKLNQHH-KKHPHFSK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 539 P-RMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESpvpsspfgamitVKSAKQVIKPnt 617
Cdd:smart00242 479 PkKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG------------VSNAGSKKRF-- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 618 khfrTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYS 697
Cdd:smart00242 545 ----QTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQ 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 124486759 698 RYGILMTQQELSLS-DKKEVCKVVLHRLIQDSNQYQFGRTKIFFRAGQVAYLEKLR 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: 912.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 70 NDLTALSYLHEPAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMA 149
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYK-SDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 150 RNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSSSN---AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISF 226
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAgnvGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 227 DERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVET 306
Cdd:pfam00063 161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 307 QKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVV 386
Cdd:pfam00063 241 DKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETVS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 387 KPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHF-SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNL 465
Cdd:pfam00063 321 KPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVkTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 466 HVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNKNSLFEKPR-MSN 543
Cdd:pfam00063 401 HMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKpLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHFQKPRlQGE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 544 SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvKSAKQVIKPNTKHFRTT 623
Cdd:pfam00063 480 THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAAN----ESGKSTPKRTKKKRFIT 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 624 VGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM 703
Cdd:pfam00063 556 VGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILA 635
|
650 660 670
....*....|....*....|....*....|....*....
gi 124486759 704 TQ-QELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:pfam00063 636 PKtWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
12-1252 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 897.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 12 RVWIPDPEEVWKSAEIAK-DYRAGDRVLRLLLEDGmELEyPVDPGSLPPLR-NPDILVGENDLTALSYLHEPAVLHNLRI 89
Cdd:COG5022 11 GCWIPDEEKGWIWAEIIKeAFNKGKVTEEGKKEDG-ESV-SVKKKVLGNDRiKLPKFDGVDDLTELSYLNEPAVLHNLEK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 90 RFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTV 169
Cdd:COG5022 89 RY-NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 170 SARYAMRYFATVSKSSSN--AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLLEKSRV 247
Cdd:COG5022 168 NAKRIMQYLASVTSSSTVeiSSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 248 VFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKIL 327
Cdd:COG5022 248 VHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKIL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 328 AAILHLGNVQVTTVGNERSSVSeDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYA 407
Cdd:COG5022 328 AAILHIGNIEFKEDRNGAAIFS-DNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYS 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 408 HLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDF 487
Cdd:COG5022 407 NLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 488 YDNQPVIDLIEAK--MGILELLDEECLLPHGTDENWLQKLYNNF-VNKNSLFEKPRMSNSSFIIQHFADKVEYQCEGFLE 564
Cdd:COG5022 487 FDNQPCIDLIEKKnpLGILSLLDEECVMPHATDESFTSKLAQRLnKNSNPKFKKSRFRDNKFVVKHYAGDVEYDVEGFLD 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 565 KNRDTVYDMLVEILRASKFHLCAAFFQEspvpsspfgamiTVKSAKQVIKPntkhfrtTVGNKFRSSLYLLMETLNATTP 644
Cdd:COG5022 567 KNKDPLNDDLLELLKASTNEFVSTLFDD------------EENIESKGRFP-------TLGSRFKESLNSLMSTLNSTQP 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 645 HYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM-----TQQELSLSDKKEVCKV 719
Cdd:COG5022 628 HYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSpskswTGEYTWKEDTKNAVKS 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 720 VLHRLIQDSNQYQFGRTKIFFRAGQVAYLEKLRLDKLRQDCIMIQKHVRGWLQRRKFLRERQAALTIQRYFRGQQTVR-- 797
Cdd:COG5022 708 ILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRlv 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 798 ----KAITATALKEAWAAIILQKYCRGYLvrnlyQLIRVATITIqahTRGFLARRRYRKLLQEHKAVILQKYARAWLARR 873
Cdd:COG5022 788 dyelKWRLFIKLQPLLSLLGSRKEYRSYL-----ACIIKLQKTI---KREKKLRETEEVEFSLKAEVLIQKFGRSLKAKK 859
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 874 RFQNIRRFVLNIQLTYRVQRLQKKLEDQNREnhglVEKLTSLAALRVGDLEKVQKLEAELE-------KAATHRHSYEEK 946
Cdd:COG5022 860 RFSLLKKETIYLQSAQRVELAERQLQELKID----VKSISSLKLVNLELESEIIELKKSLSsdlienlEFKTELIARLKK 935
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 947 GRRYRDTVEERLSKLQKHNAELELQRERAEqmLQEKSEELKEKMDKLTrQLFDDVQKEEQQRlvleKGFELKTQAYEKQI 1026
Cdd:COG5022 936 LLNNIDLEEGPSIEYVKLPELNKLHEVESK--LKETSEEYEDLLKKST-ILVREGNKANSEL----KNFKKELAELSKQY 1008
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1027 ESLREEIKALKDERSQL-HHQLEEGQVTSDRlkGEVARLSKQAKTISEFEKEIELLQAQKIDVekhvqSQKREMRERMSe 1105
Cdd:COG5022 1009 GALQESTKQLKELPVEVaELQSASKIISSES--TELSILKPLQKLKGLLLLENNQLQARYKAL-----KLRRENSLLDD- 1080
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1106 vtkqlLESYDIEDVRSRLSVedlehLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQK 1185
Cdd:COG5022 1081 -----KQLYQLESTENLLKT-----INVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLS 1150
|
1210 1220 1230 1240 1250 1260
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486759 1186 LFREETDIN--ESIRHEVTRLTSENMMIPDFKQQISELERQKQDLESRLKEQAEKIEGKLEEPFSHLNR 1252
Cdd:COG5022 1151 VLQLELDGLfwEANLEALPSPPPFAALSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFSGWPR 1219
|
|
| 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: 821.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMG-DMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd00124 1 AAILHNLRERYARDL-IYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 160 SGESGAGKTVSARYAMRYFATVSKSSSNAH------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQII 233
Cdd:cd00124 80 SGESGAGKTETTKLVLKYLAALSGSGSSKSsssassIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 234 GANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEE----FNYTRMGGNTVIEGVNDRADMVETQKT 309
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSyyylNDYLNSSGCDRIDGVDDAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 310 FTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNE--RSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVK 387
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 388 PMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQH--TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNL 465
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 466 HVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSNS 544
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKpLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAKL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 545 SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKfhlcaaffqespvpsspfgamitvksakqvikpntkhfrttv 624
Cdd:cd00124 480 EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS------------------------------------------ 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 625 gnKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMT 704
Cdd:cd00124 518 --QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAP 595
|
650 660 670
....*....|....*....|....*....|....*...
gi 124486759 705 Q-QELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 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: 740.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01377 1 ASVLHNLRERY-YSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 161 GESGAGKTVSARYAMRYFATVSKSSSNAH--------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQI 232
Cdd:cd01377 80 GESGAGKTENTKKVIQYLASVAASSKKKKesgkkkgtLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 233 IGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTL 312
Cdd:cd01377 160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 313 LGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 393 QAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQ 472
Cdd:cd01377 320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 473 EEYMKEDIPWTLIDF-YDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMS--NSSFII 548
Cdd:cd01377 400 EEYKKEGIEWTFIDFgLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKPKksEAHFIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 549 QHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAMITVKSAkqvikpntkhFRtTVGNKF 628
Cdd:cd01377 480 KHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGGGKKKKKGGS----------FR-TVSQLH 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 629 RSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQEL 708
Cdd:cd01377 549 KEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIP 628
|
650 660 670
....*....|....*....|....*....|....
gi 124486759 709 -SLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 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: 700.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd01384 1 PGVLHNLKVRY-ELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 160 SGESGAGKTVSARYAMRYFATVSK--SSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANM 237
Cdd:cd01384 80 SGESGAGKTETTKMLMQYLAYMGGraVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 238 RTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKK 317
Cdd:cd01384 160 RTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 318 DFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDS---HLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd01384 240 EEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKsefHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 395 INARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEE 474
Cdd:cd01384 320 TLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 475 YMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRMSNSSFIIQHFAD 553
Cdd:cd01384 400 YTKEEIDWSYIEFVDNQDVLDLIEKKPgGIIALLDEACMFPRSTHETFAQKLYQTLKD-HKRFSKPKLSRTDFTIDHYAG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 554 KVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSspfgamiTVKSAKqvikpntkhFrTTVGNKFRSSLY 633
Cdd:cd01384 479 DVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREG-------TSSSSK---------F-SSIGSRFKQQLQ 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 634 LLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDK 713
Cdd:cd01384 542 ELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLKGSDDE 621
|
650 660
....*....|....*....|....*...
gi 124486759 714 KEVCKVVLHRLiqDSNQYQFGRTKIFFR 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: 684.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDmdPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01383 1 PSVLHNLEYRY-SQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKLLDS--PHVYAVADTAYREMMRDEINQSIIIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 161 GESGAGKTVSARYAMRYFATVSKSSSNahVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTY 240
Cdd:cd01383 78 GESGAGKTETAKIAMQYLAALGGGSSG--IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 241 LLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQ 320
Cdd:cd01383 156 LLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKEDQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 321 MDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDA 400
Cdd:cd01383 236 EHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 401 LAKKIYAHLFDFIVEQINQALHFSGKQH-TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKED 479
Cdd:cd01383 316 LAKAIYASLFDWLVEQINKSLEVGKRRTgRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 480 IPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLyNNFVNKNSLFEKPRmsNSSFIIQHFADKVEYQ 558
Cdd:cd01383 396 IDWTKVDFEDNQECLDLIEKKpLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCFKGER--GGAFTIRHYAGEVTYD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 559 CEGFLEKNRDTVYDMLVEILRASKFHLCAAF------FQESPVPSSPFGamitvKSAKQvikpntkhfRTTVGNKFRSSL 632
Cdd:cd01383 473 TSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFaskmldASRKALPLTKAS-----GSDSQ---------KQSVATKFKGQL 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 633 YLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSD 712
Cdd:cd01383 539 FKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQD 618
|
650 660
....*....|....*....|....*....
gi 124486759 713 KKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01383 619 PLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| 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: 675.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 82 AVLHNLRIRFAEsKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd01381 2 GILRNLLIRYRE-KLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 162 ESGAGKTVSARYAMRYFATVSKSSSnaHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYL 241
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS--WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 242 LEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQM 321
Cdd:cd01381 159 LEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 322 DVFKILAAILHLGNVQ--VTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARD 399
Cdd:cd01381 239 DIFKLLAAILHLGNIKfeATVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 400 ALAKKIYAHLFDFIVEQINQALH-FSGKQH--TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYM 476
Cdd:cd01381 319 AFVKGIYGRLFIWIVNKINSAIYkPRGTDSsrTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEYD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 477 KEDIPWTLIDFYDNQPVIDLI-EAKMGILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRM-SNSSFIIQHFADK 554
Cdd:cd01381 399 KEGINWQHIEFVDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGN-NKNYLKPKSdLNTSFGINHFAGV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 555 VEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamitvKSAKQVIkpntkhfrtTVGNKFRSSLYL 634
Cdd:cd01381 478 VFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGS--------ETRKKSP---------TLSSQFRKSLDQ 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 635 LMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL------MTQQEL 708
Cdd:cd01381 541 LMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLvpgippAHKTDC 620
|
650 660 670
....*....|....*....|....*....|...
gi 124486759 709 SLSDKKEVCKVVLHrliqDSNqYQFGRTKIFFR 741
Cdd:cd01381 621 RAATRKICCAVLGG----DAD-YQLGKTKIFLK 648
|
|
| 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: 674.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd01378 2 AINENLKKRF-ENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 162 ESGAGKTVSARYAMRYFATVSKSSSN--AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRT 239
Cdd:cd01378 81 ESGAGKTEASKRIMQYIAAVSGGSESevERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDF 319
Cdd:cd01378 161 YLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 320 QMDVFKILAAILHLGNVQVTTVGNERSSVSeDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSE---TVVKPMTRPQAIN 396
Cdd:cd01378 241 QDSIFRILAAILHLGNIQFAEDEEGNAAIS-DTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGgrsVYEVPLNVEQAAY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 397 ARDALAKKIYAHLFDFIVEQINQALHFSGKQH-TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEY 475
Cdd:cd01378 320 ARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEEY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 476 MKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPH-GTDENWLQKLyNNFVNKNSLFEKP----RMSNSSFIIQ 549
Cdd:cd01378 400 VREGIEWTPIKYFNNKIICDLIEEKpPGIFAILDDACLTAGdATDQTFLQKL-NQLFSNHPHFECPsghfELRRGEFRIK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 550 HFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQEspvpsspfgamitvksakQVIKPNTKhfR-TTVGNKF 628
Cdd:cd01378 479 HYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPE------------------GVDLDSKK--RpPTAGTKF 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 629 RSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGilmtqqel 708
Cdd:cd01378 539 KNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYK-------- 610
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 124486759 709 SLSDK---------KEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01378 611 LLSPKtwpawdgtwQGGVESILKDLNIPPEEYQMGKTKIFIR 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: 664.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1369 EDEGKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRYADSLNDANMLKSLMNSAINGIKHVVKEHFEDLEMLSFWLSNT 1448
Cdd:cd15476 1 EDEAKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRHADYLNDANKLKSLMNAIITGVKQVIKEHQEDFEMLSFWLSNT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1449 CHFLNCLKQYSGEEEFMKYNSPQQNKNCLNNFDLTEYRQILSDVAIRIYHQFIIVMENNLQPiivpgmleyeslqgisgl 1528
Cdd:cd15476 81 YHFLNCLKQYSGEEEFMKHNTPRQNKNCLKNFDLSEHRQILSDLAIRIYHQFISVMENNLQP------------------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1529 kptgfrkrsssiddtdayTMTSILQQLSYFYSTMCQNGLDPEIVRQAVKQLFYLVGAVTLNSLLLRKDMCSCRKGMQIRC 1608
Cdd:cd15476 143 ------------------TISSILQQLSYFYSTMCQHGMDPELIKQAVKQLFFLIGAVTLNSIFLRKDMCSCRKGMQIRC 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1609 NISFLEEWLKDKNVQSSLAKETLEPLSQAAWLLQVKKTTDSDAKEIAQCCTSLSAVQIIKILNSYTPIDDFEKRVNPSFV 1688
Cdd:cd15476 205 NISYLEEWLKEKNLQNSNAKETLEPLSQAAWLLQVNKTTDDDAKEICERCTELSAVQIVKILNSYTPIDDFEKRVTPSFV 284
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 124486759 1689 RKVQALLNNRGDSAQLMLDTKYLFQVTFPFTASPHALEMTQIPSSFKL 1736
Cdd:cd15476 285 RKVQSLLQNREGSSQLMLDTKYRFQVTFPFCPSPQALEMLQVPSSLKL 332
|
|
| 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: 658.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14883 2 GINTNLKVRYK-KDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 162 ESGAGKTVSARYAMRYFATVSKSSSnaHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYL 241
Cdd:cd14883 81 ESGAGKTETTKLILQYLCAVTNNHS--WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 242 LEKSRVVFQSENERNYHIFYQLCASAQQS-EFKH-LKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDF 319
Cdd:cd14883 159 LEQSRITFQAPGERNYHVFYQLLAGAKHSkELKEkLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPEEM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 320 QMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSH-LKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINAR 398
Cdd:cd14883 239 QEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEiLKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 399 DALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKE 478
Cdd:cd14883 319 DAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 479 DIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNKNSLFEKP--RMSNSSFIIQHFADKV 555
Cdd:cd14883 399 GINWSHIVFTDNQECLDLIEKPpLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPdrRRWKTEFGVKHYAGEV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 556 EYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFF----QESPVPSSPFGAMITVKSAkqvikpnTKHFRTTVGNKFRSS 631
Cdd:cd14883 478 TYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtypdLLALTGLSISLGGDTTSRG-------TSKGKPTVGDTFKHQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 632 LYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQ-QELSL 710
Cdd:cd14883 551 LQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRaRSADH 630
|
650 660 670
....*....|....*....|....*....|.
gi 124486759 711 SDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14883 631 KETCGAVRALMGLGGLPEDEWQVGKTKVFLR 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: 610.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14872 1 AMIVHNLRKRFKNDQ-IYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 161 GESGAGKTVSARYAMRYFATVSKSSSNahVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTY 240
Cdd:cd14872 80 GESGAGKTEATKQCLSFFAEVAGSTNG--VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 241 LLEKSRVVFQSENERNYHIFYQLCASAQQSefKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQ 320
Cdd:cd14872 158 LLEKSRVVYQIKGERNFHIFYQLLASPDPA--SRGGWGSSAAYGYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFDDADI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 321 MDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCE---LLGLETSKVAQWLCNRKI-VTSSETVVKPMTRPQAIN 396
Cdd:cd14872 236 NNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSRLMeIKGCDPTRIPLTPAQATD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 397 ARDALAKKIYAHLFDFIVEQINQALH-FSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEY 475
Cdd:cd14872 316 ACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEALY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 476 MKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNF-VNKNSLFEKPRMSNSSFIIQHFAD 553
Cdd:cd14872 396 QSEGVKFEHIDFIDNQPVLDLIEKKQpGLMLALDDQVKIPKGSDATFMIAANQTHaAKSTFVYAEVRTSRTEFIVKHYAG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 554 KVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvpsspfgamitvksakQVIKPNTKHFRTTVGNKFRSSLY 633
Cdd:cd14872 476 DVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF--------------------PPSEGDQKTSKVTLGGQFRKQLS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 634 LLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSL-SD 712
Cdd:cd14872 536 ALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVKTIAKRVgPD 615
|
650 660
....*....|....*....|....*....
gi 124486759 713 KKEVCKVVLHRLIQDSNQYQFGRTKIFFR 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: 601.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14903 1 AAILYNVKKRFL-RKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 160 SGESGAGKTVSARYAMRYFATVSKSSSNAHVEdKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRT 239
Cdd:cd14903 80 SGESGAGKTETTKILMNHLATIAGGLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEfkHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDF 319
Cdd:cd14903 159 YLLEKTRVISHERPERNYHIFYQLLASPDVEE--RLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 320 QMDVFKILAAILHLGNVQVTTVGN--ERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINA 397
Cdd:cd14903 237 QEVLFEVLAGILHLGQLQIQSKPNddEKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDC 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 398 RDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMK 477
Cdd:cd14903 317 RDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSNSSFIIQHFADKVEY 557
Cdd:cd14903 397 EGIRWAHIDFADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSRTQFTIKHYAGPVTY 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 558 QCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAMITVKSAKQVIKPNTKhfrTTVGNKFRSSLYLLME 637
Cdd:cd14903 477 ESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGGALTT---TTVGTQFKDSLNELMT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 638 TLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDKKEVC 717
Cdd:cd14903 554 TIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGRNTDVPVAERC 633
|
650 660
....*....|....*....|....*
gi 124486759 718 KVVLHRL-IQDSNQYQFGRTKIFFR 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: 594.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 84 LHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd01382 4 LNNIRVRYSKDK-IYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 163 SGAGKTVSARYAMRYFaTVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLL 242
Cdd:cd01382 83 SGAGKTESTKYILRYL-TESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 243 EKSRVVFQSENERNYHIFYQLCASAQQSEFKHLklgsaeefnytrmggnTVIEGVNDRADMVETQKTFTLLGFKKDFQMD 322
Cdd:cd01382 162 EKSRICVQSKEERNYHIFYRLCAGAPEDLREKL----------------LKDPLLDDVGDFIRMDKAMKKIGLSDEEKLD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 323 VFKILAAILHLGNVQVTTVGNER---SSVSEDDSH-LKVFCELLGLETSKVAQWLCNRKIVTSSE----TVVK-PMTRPQ 393
Cdd:cd01382 226 IFRVVAAVLHLGNIEFEENGSDSgggCNVKPKSEQsLEYAAELLGLDQDELRVSLTTRVMQTTRGgakgTVIKvPLKVEE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 394 AINARDALAKKIYAHLFDFIVEQINQALHFSGKQHtFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd01382 306 ANNARDALAKAIYSKLFDHIVNRINQCIPFETSSY-FIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKEEQE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 474 EYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFvNKNSLFEKPRMSNSS------- 545
Cdd:cd01382 385 LYEKEGLGVKEVEYVDNQDCIDLIEAKLvGILDLLDEESKLPKPSDQHFTSAVHQKH-KNHFRLSIPRKSKLKihrnlrd 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 546 ---FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamitvKSAKQVIKPNTKhfrt 622
Cdd:cd01382 464 degFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNK--------DSKQKAGKLSFI---- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 623 TVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL 702
Cdd:cd01382 532 SVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKY 611
|
650 660 670
....*....|....*....|....*....|....*....
gi 124486759 703 MTqQELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01382 612 LP-PKLARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 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: 588.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 84 LHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGES 163
Cdd:cd01385 4 LENLRARFKHGK-IYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 164 GAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLLE 243
Cdd:cd01385 83 GSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 244 KSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDV 323
Cdd:cd01385 163 KSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQRQI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 324 FKILAAILHLGNVQV---TTVGNERSSVSEDDShLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDA 400
Cdd:cd01385 243 FSVLSAVLHLGNIEYkkkAYHRDESVTVGNPEV-LDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 401 LAKKIYAHLFDFIVEQINQAL----HFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYM 476
Cdd:cd01385 322 MAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 477 KEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKlYNNFVNKNSLFEKPRMSNSSFIIQHFADKV 555
Cdd:cd01385 402 KEGISWHNIEYTDNTGCLQLISKKpTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQVMEPAFIIAHYAGKV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 556 EYQCEGFLEKNRDTVYDMLVEILRASK-----------------------FHLCAAFFQESPVPSS----PFGAMITVKS 608
Cdd:cd01385 481 KYQIKDFREKNLDLMRPDIVAVLRSSSsafvreligidpvavfrwavlraFFRAMAAFREAGRRRAqrtaGHSLTLHDRT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 609 AKQVIKPNTKHFRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPS 688
Cdd:cd01385 561 TKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSV 640
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 124486759 689 RWTYLEFYSRYGILMTQQELSlsdKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd01385 641 RYTFQEFITQFQVLLPKGLIS---SKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| 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: 570.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14873 2 SIMYNLFQRYKRNQ-IYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 161 GESGAGKTVSARYAMRYFATVSKSSSNA-------HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQII 233
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELslkektsCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 234 GANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLL 313
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 314 GFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSvseDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEFITAGGAQVS---FKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 394 AINARDALAKKIYAHLFDFIVEQINQALHfsGKQH-TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQ 472
Cdd:cd14873 318 AVDSRDSLAMALYARCFEWVIKKINSRIK--GKEDfKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 473 EEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRMSNSSFIIQHFA 552
Cdd:cd14873 396 LEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHAN-NHFYVKPRVAVNNFGVKHYA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 553 DKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQEspvpsspfgamITVKSAKQVIKPNTKHFRTTVGNKFRSSL 632
Cdd:cd14873 475 GEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEH-----------VSSRNNQDTLKCGSKHRRPTVSSQFKDSL 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 633 YLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLsD 712
Cdd:cd14873 544 HSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPE-D 622
|
650 660
....*....|....*....|....*....
gi 124486759 713 KKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14873 623 VRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| 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: 569.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMAR----NNRNQS 156
Cdd:cd14890 2 SLLHTLRLRY-ERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 157 IIVSGESGAGKTVSARYAMRYFATVSKSSSN-----------------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFG 219
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQgasgegeaaseaieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 220 KYTEISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVND 299
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLR-GECSSIPSCDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 300 RADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVgnERSSVSEDDS---HLKVFCELLGLETSKVAQWLCNR 376
Cdd:cd14890 240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESE--NDTTVLEDATtlqSLKLAAELLGVNEDALEKALLTR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 377 KIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYAN 456
Cdd:cd14890 318 QLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 457 EKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM----GILELLDEECLLpHGTDEN--WLQKLYNNF- 529
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVngkpGIFITLDDCWRF-KGEEANkkFVSQLHASFg 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 530 -----------VNKNSLFEKPRMSNS-SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASkfhlcaaffqespvps 597
Cdd:cd14890 477 rksgsggtrrgSSQHPHFVHPKFDADkQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQS---------------- 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 598 spfgamitvksakqvikpnTKHFR-TTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVL 676
Cdd:cd14890 541 -------------------RRSIReVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMM 601
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124486759 677 ETIRISAQSYPSRWTYLEFYSRYGILMTQQElslsDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14890 602 EAIQIRQQGFALREEHDSFFYDFQVLLPTAE----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: 568.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd01387 2 TVLWNLKTRY-ERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 162 ESGAGKTVSARYAMRYFATVSKSSSNAhVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFdERNQIIGANMRTYL 241
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNL-VTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAITSQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 242 LEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQM 321
Cdd:cd01387 159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 322 DVFKILAAILHLGNV----QVTTVGNERSSVSEDdSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINA 397
Cdd:cd01387 239 SIFRILASVLHLGNVyfhkRQLRHGQEGVSVGSD-AEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 398 RDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMK 477
Cdd:cd01387 318 RDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYIR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 478 EDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKL-YNNFVNKnsLFEKPRMSNSSFIIQHFADKV 555
Cdd:cd01387 398 EQIDWTEIAFADNQPVINLISKKpVGILHILDDECNFPQATDHSFLEKChYHHALNE--LYSKPRMPLPEFTIKHYAGQV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 556 EYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQ------ESPVPSSPFGAMITvksakqvIKPNTKhfrtTVGNKFR 629
Cdd:cd01387 476 WYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSshraqtDKAPPRLGKGRFVT-------MKPRTP----TVAARFQ 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 630 SSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQeLS 709
Cdd:cd01387 545 DSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALK-LP 623
|
650 660 670
....*....|....*....|....*....|....
gi 124486759 710 LSDKKEVCKVVLHRL--IQDSNQYQFGRTKIFFR 741
Cdd:cd01387 624 RPAPGDMCVSLLSRLctVTPKDMYRLGATKVFLR 657
|
|
| 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: 560.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFAESkLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01379 1 DTIVSQLQKRYSRD-QIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 161 GESGAGKTVSARYAMRYFATVSKSSsNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTY 240
Cdd:cd01379 80 GESGAGKTESANLLVQQLTVLGKAN-NRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 241 LLEKSRVVFQSENERNYHIFYQLCAS-AQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMV---ETQKTFTLLGFK 316
Cdd:cd01379 159 LLEKSRVVHQAIGERNFHIFYYIYAGlAEDKKLAKYKLPENKPPRYLQNDGLTVQDIVNNSGNREkfeEIEQCFKVIGFT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 317 KDFQMDVFKILAAILHLGNVQVTTVGNE----RSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd01379 239 KEEVDSVYSILAAILHIGDIEFTEVESNhqtdKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 393 QAINARDALAKKIYAHLFDFIVEQINQAL----HFSGKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVF 468
Cdd:cd01379 319 EATDARDAMAKALYGRLFSWIVNRINSLLkpdrSASDEPLS-IGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 469 KLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvnKNSLFEKPRMSNSSFI 547
Cdd:cd01379 398 AWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKpMGLLALLDEESRFPKATDQTLVEKFHNNI--KSKYYWRPKSNALSFG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 548 IQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLcaaffqespvpsspfgamitvksakqvikpntkhFRTTVGNK 627
Cdd:cd01379 476 IHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPL----------------------------------VRQTVATY 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 628 FRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQE 707
Cdd:cd01379 522 FRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKWN 601
|
650 660 670
....*....|....*....|....*....|....
gi 124486759 708 LSLSDKKEVCKVVLHRLIQDSnqYQFGRTKIFFR 741
Cdd:cd01379 602 EEVVANRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
81-741 |
0e+00 |
|
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: 558.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14904 1 PSILFNLKKRFAASK-PYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 160 SGESGAGKTVSARYAMRYFATVSKSSSNAHVeDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRT 239
Cdd:cd14904 80 SGESGAGKTETTKIVMNHLASVAGGRKDKTI-AKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYtrMGGN---TVIEGVNDRADMVETQKTFTLLGFK 316
Cdd:cd14904 159 YLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQY--LGDSlaqMQIPGLDDAKLFASTQKSLSLIGLD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 317 KDFQMDVFKILAAILHLGNVQVTTVGnERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAIN 396
Cdd:cd14904 237 NDAQRTLFKILSGVLHLGEVMFDKSD-ENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 397 ARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEY 475
Cdd:cd14904 316 NRDALAKAIYSKLFDWMVVKINAAISTDDDRiKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 476 MKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNK--NSLFEKPRMSNSSFIIQHFAD 553
Cdd:cd14904 396 IREGLQWDHIEYQDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQTKkdNESIDFPKVKRTQFIINHYAG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 554 KVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvKSAKQVIKPNtkhfrtTVGNKFRSSLY 633
Cdd:cd14904 476 PVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSETKEG----KSGKGTKAPK------SLGSQFKTSLS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 634 LLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIlMTQQELSLSDK 713
Cdd:cd14904 546 QLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAI-MFPPSMHSKDV 624
|
650 660
....*....|....*....|....*....
gi 124486759 714 KEVCKVVLHRLIQDSN-QYQFGRTKIFFR 741
Cdd:cd14904 625 RRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| 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: 550.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1369 EDEGKLIQNLILDLKPRGVVvNMIPGLPAHILFMCVRYADSLNDANMLKSLMNSAINGIKHVVKEHFEDLEMLSFWLSNT 1448
Cdd:cd15470 1 EDESRLIKNLITDLKPRGAV-GLLPGLPAYILFMCIRHADYVNDEAKVRSLLTATINAIKKVLKKHSEDFEMLSFWLVNT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1449 CHFLNCLKQYSGEEEFMKYNSPQQNKNCLNNFDLTEYRQILSDVAIRIYHQFIIVMENNLQPiivpgmleyeslqgisgl 1528
Cdd:cd15470 80 CRLLNCLKQYSGEEEFMKHNTPKQNEHCLKNFDLSEYRQVLSDLAIQIYQQLIKRAEEILQP------------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1529 kptgfrkrsssiddtdayTMTSILQQLSYFYSTMCQNGLDPEIVRQAVKQLFYLVGAVTLNSLLLRKDMCSCRKGMQIRC 1608
Cdd:cd15470 142 ------------------TLDSLLQQLNSFHTTLTQHGLDPELIKQVFRQLFYLICASTLNNLLLRKDLCSWSKGMQIRY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1609 NISFLEEWLKDKNVQSSLAKETLEPLSQAAWLLQVKKTTDSDAKEIAQCCTSLSAVQIIKILNSYTPIDDFEKRVNPSFV 1688
Cdd:cd15470 204 NVSQLEEWLRDKGLQDSGARETLEPLIQAAQLLQVKKTTEEDAQSICEMCTKLTTAQIVKILNLYTPVDDFEERVTPSFI 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 124486759 1689 RKVQALLNNRGDSA--QLMLDTKYLFQVTFPFTASPHALEMTQIPSSFK 1735
Cdd:cd15470 284 RKVQARLNERADSNqlQLLMDTKYIFPVTFPFNPSPVALEELQIPPSLH 332
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
81-739 |
1.51e-177 |
|
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: 550.55 E-value: 1.51e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAY---SGQNMGD---MDPHIFAVAEEAYKQMARNNR- 153
Cdd:cd14901 1 PSILHVLRRRF-AHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehGERRAAGerkLPPHVYAVADKAFRAMLFASRg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 154 ---NQSIIVSGESGAGKTVSARYAMRYFATVS-KSSSNAH------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTE 223
Cdd:cd14901 80 qkcDQSILVSGESGAGKTETTKIIMNYLASVSsATTHGQNaterenVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 224 ISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTV-IEGVNDRAD 302
Cdd:cd14901 160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDrRDGVDDSVQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 303 MVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQ-VTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTS 381
Cdd:cd14901 240 YAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCfVKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 382 SETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHF--SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKL 459
Cdd:cd14901 320 GEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYseSTGASRFIGIVDIFGFEIFATNSLEQLCINFANEKL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 460 QQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKNSL-FE 537
Cdd:cd14901 400 QQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARpTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHASFsVS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 538 KPRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLcaaffqespVPSspfgamitvksakqvikpnt 617
Cdd:cd14901 480 KLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAF---------LSS-------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 618 khfrtTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYS 697
Cdd:cd14901 531 -----TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVH 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 124486759 698 RYGILMTQQElslSDKKEVCKVVLHR---------LIQDSNQYQFGRTKIF 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 |
9.65e-175 |
|
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: 542.81 E-value: 9.65e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 87 LRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMD---PHIFAVAEEAYKQM----ARNNRNQSIIV 159
Cdd:cd14892 7 LRRRY-ERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATASsppPHVFSIAERAYRAMkgvgKGQGTPQSIVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 160 SGESGAGKTVSARYAMRYFATVSKSSS---------NAH--VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDE 228
Cdd:cd14892 86 SGESGAGKTEASKYIMKYLATASKLAKgastskgaaNAHesIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 229 RNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQK 308
Cdd:cd14892 166 DGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVDGVDDATEFKQLRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKV--FCELLGLETSKVAQWLCNRKIVTSSETVV 386
Cdd:cd14892 246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNVakAAGLLGVDAAELMFKLVTQTTSTARGSVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 387 K-PMTRPQAINARDALAKKIYAHLFDFIVEQINQA----------LHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYA 455
Cdd:cd14892 326 EiKLTAREAKNALDALCKYLYGELFDWLISRINAChkqqtsgvtgGAASPTFSPFIGILDIFGFEIMPTNSFEQLCINFT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 456 NEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPH-GTDENWLQKLYNNFVNKN 533
Cdd:cd14892 406 NEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKpLGLLPLLEEQMLLKRkTTDKQLLTIYHQTHLDKH 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 534 SLFEKPRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKfhlcaaffqespvpsspfgamitvksakqvi 613
Cdd:cd14892 486 PHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS------------------------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 614 kpntkhfrttvgnKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYL 693
Cdd:cd14892 535 -------------KFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFE 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 124486759 694 EFYSRYGIL--------MTQQELSLSD-KKEVCKVVLHRLiqDSNQYQFGRTKIFFR 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 |
1.28e-172 |
|
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: 537.74 E-value: 1.28e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSgQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14888 1 ASILHSLNLRFDIDE-IYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 160 SGESGAGKTVSARYAMRYFATVSKSS--SNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN------- 230
Cdd:cd14888 79 SGESGAGKTESTKYVMKFLACAGSEDikKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLKskrmsgd 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 231 --QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQS-------EFKHLKLG----------------SAEEFNY 285
Cdd:cd14888 159 rgRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAkntglsyEENDEKLAkgadakpisidmssfePHLKFRY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 286 TRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQ-VTTVGNERSSV--SEDDSHLKVFCELL 362
Cdd:cd14888 239 LTKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILfENNEACSEGAVvsASCTDDLEKVASLL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 363 GLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHT-FIGVLDIYGFET 441
Cdd:cd14888 319 GVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLlFCGVLDIFGFEC 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 442 FDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDEN 520
Cdd:cd14888 399 FQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKpLGIFCMLDEECFVPGGKDQG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 521 WLQKLYNNFVNkNSLFEKPRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvpSSPF 600
Cdd:cd14888 479 LCNKLCQKHKG-HKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLF------SAYL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 601 GAMITVKSakqvikpnTKHFRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIR 680
Cdd:cd14888 552 RRGTDGNT--------KKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQ 623
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486759 681 ISAQSYPSRWTYLEFYSRYGILMTQQElslsdKKEVckvvlhrliqdsNQYQFGRTKIFFR 741
Cdd:cd14888 624 VSRAGYPVRLSHAEFYNDYRILLNGEG-----KKQL------------SIWAVGKTLCFFK 667
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
82-741 |
4.46e-164 |
|
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: 514.94 E-value: 4.46e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14920 2 SVLHNLKDRYY-SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 162 ESGAGKTVSARYAMRYFATVSKSSSN-------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIG 234
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 235 ANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVNDRADMVETQKTFTLLG 314
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIMG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 315 FKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14920 240 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 395 INARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd14920 320 DFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 474 EYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNKNSLFEKPRM--SNSSFI 547
Cdd:cd14920 400 EYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQE-QGSHSKFQKPRQlkDKADFC 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 548 IQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQE--SPVPSSPFGAMiTVKSAKQVIKPNTKHFRtTVG 625
Cdd:cd14920 479 IIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdRIVGLDQVTGM-TETAFGSAYKTKKGMFR-TVG 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 626 NKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQ 705
Cdd:cd14920 557 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 636
|
650 660 670
....*....|....*....|....*....|....*..
gi 124486759 706 Q-ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14920 637 AiPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
82-741 |
6.20e-162 |
|
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: 509.50 E-value: 6.20e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14927 2 SVLHNLRRRYS-RWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 162 ESGAGKTVSARYAMRYFATVS-------------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDE 228
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAalgdgpgkkaqflATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 229 RNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQ 307
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQI-LSGKKPELQDMLLVSMNPYDYHFCSqGVTTVDNMDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 308 KTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVK 387
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 388 PMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHV 467
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 468 FKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN--- 543
Cdd:cd14927 400 FILEQEEYKREGIEWVFIDFgLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKkrk 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 544 --SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqESPVPSSpfgamiTVKSAKQVIKPNTKHFR 621
Cdd:cd14927 480 yeAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY-ENYVGSD------STEDPKSGVKEKRKKAA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 622 T--TVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRY 699
Cdd:cd14927 553 SfqTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRY 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 124486759 700 GILMTQQ--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 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 |
6.45e-162 |
|
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: 509.21 E-value: 6.45e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14913 1 PAVLYNLKDRYT-SWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 161 GESGAGKTVSARYAMRYFATVS---------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQ 231
Cdd:cd14913 80 GESGAGKTVNTKRVIQYFATIAatgdlakkkDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 232 IIGANMRTYLLEKSRVVFQSENERNYHIFYQLCaSAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKTF 310
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQIL-SNKKPELIELLLITTNPYDYPFISqGEILVASIDDAEELLATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 311 TLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMT 390
Cdd:cd14913 239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 391 RPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKL 470
Cdd:cd14913 319 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 471 EQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRM----SNSS 545
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVvkgrAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 546 FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvpsSPFGAMITVKSAKQVIKPNTKHFRtTVG 625
Cdd:cd14913 479 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY-------ATFATADADSGKKKVAKKKGSSFQ-TVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 626 NKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQ 705
Cdd:cd14913 551 ALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNAS 630
|
650 660 670
....*....|....*....|....*....|....*...
gi 124486759 706 Q--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14913 631 AipEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
81-741 |
1.37e-161 |
|
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: 508.22 E-value: 1.37e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14909 1 ASVLHNLRQRY-YAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 161 GESGAGKTVSARYAMRYFATVSKSS-------SNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQII 233
Cdd:cd14909 80 GESGAGKTENTKKVIAYFATVGASKktdeaakSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 234 GANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKTFTL 312
Cdd:cd14909 160 GADIETYLLEKARVISQQSLERSYHIFYQI-MSGSVPGVKEMCLLSDNIYDYYIVSqGKVTVPNVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 313 LGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 393 QAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQ 472
Cdd:cd14909 319 QVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 473 EEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN-----SSF 546
Cdd:cd14909 399 EEYKREGIDWAFIDFgMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpgqqaAHF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 547 IIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvksAKQVIKPNTKHFrTTVGN 626
Cdd:cd14909 479 AIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQ------AKGGRGKKGGGF-ATVSS 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 627 KFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQ 706
Cdd:cd14909 552 AYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAG 631
|
650 660 670
....*....|....*....|....*....|....*
gi 124486759 707 ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14909 632 IQGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
81-741 |
2.33e-161 |
|
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: 507.21 E-value: 2.33e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14929 1 ASVLHTLRRRY-DHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 161 GESGAGKTVSARYAMRYFATVSKSSSN----AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGAN 236
Cdd:cd14929 80 GESGAGKTVNTKHIIQYFATIAAMIESkkklGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 237 MRTYLLEKSRVVFQSENERNYHIFYQLCASAQqsEFKHLKLGSA--EEFNYTRMGGNTViEGVNDRADMVETQKTFTLLG 314
Cdd:cd14929 160 IDIYLLEKSRVIFQQPGERNYHIFYQILSGKK--ELRDLLLVSAnpSDFHFCSCGAVAV-ESLDDAEELLATEQAMDILG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 315 FKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14929 237 FLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 395 INARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEE 474
Cdd:cd14929 317 TYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 475 YMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSNSSFIIQ---- 549
Cdd:cd14929 397 YRKEGIDWVSIDFgLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHfelv 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 550 HFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQE--SPVPSSPFGAMITVKSAKqvikpntkhFRtTVGNK 627
Cdd:cd14929 477 HYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENyiSTDSAIQFGEKKRKKGAS---------FQ-TVASL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 628 FRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQ-- 705
Cdd:cd14929 547 HKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRtf 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 124486759 706 QELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 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 |
2.00e-158 |
|
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: 487.83 E-value: 2.00e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1368 KEDEGKLIQNLILDLKPRgVVVNMIPGLPAHILFMCVRYADSLNDANMLKSLMNSAINGIKHVVKEHFEDLEMLSFWLSN 1447
Cdd:cd15477 1 KEDEALLIRNLVTDLKPQ-AVSATVPCLPAYILYMCIRHADYINDDQKVHSLLTSTINGIKKVLKKHNDDFEMTSFWLAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1448 TCHFLNCLKQYSGEEEFMKYNSPQQNKNCLNNFDLTEYRQILSDVAIRIYHQFIIVMENNLQPIIVPGMLEYESLQGISG 1527
Cdd:cd15477 80 TCRLLHCLKQYSGDEGFMTQNTAKQNEHCLKNFDLTEYRQVLSDLSIQIYQQLIKIAEGILQPMIVSAMLENESIQGLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1528 LKPTGFRKRSSSIDDTDA-YTMTSILQQLSYFYSTMCQNGLDPEIVRQAVKQLFYLVGAVTLNSLLLRKDMCSCRKGMQI 1606
Cdd:cd15477 160 VKPMGYRKRSSSMADGDNsYTLEALIRQLNTFHSIMCDQGLDPEIIQQVFKQLFYMINAVTLNNLLLRKDVCSWSTGMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1607 RCNISFLEEWLKDKNVQSSLAKETLEPLSQAAWLLQVKKTTDSDAKEIAQCCTSLSAVQIIKILNSYTPIDDFEKRVNPS 1686
Cdd:cd15477 240 RYNISQLEEWLRGRNLHQSGAAQTMEPLIQAAQLLQLKKKTSEDAEAICSLCTALSTQQIVKILNLYTPLNEFEERVTVS 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 124486759 1687 FVRKVQALLNNRGDSAQLMLDTKYLFQVTFPFTASPHALEMTQIPSSFKLGFL 1739
Cdd:cd15477 320 FIRTIQAQLQERNDPPQLLLDTKHMFPVLFPFNPSALTLDSIHIPASLNLDFL 372
|
|
| Myo5a_CBD |
cd15478 |
Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, ... |
1368-1742 |
3.91e-158 |
|
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: 487.23 E-value: 3.91e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1368 KEDEGKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRYADSLNDANMLKSLMNSAINGIKHVVKEHFEDLEMLSFWLSN 1447
Cdd:cd15478 1 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1448 TCHFLNCLKQYSGEEEFMKYNSPQQNKNCLNNFDLTEYRQILSDVAIRIYHQFIIVMENNLQPIIVPGMLEYESLQGISG 1527
Cdd:cd15478 81 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1528 LKPTGFRKRSSSIDDTDAYTMTSILQQLSYFYSTMCQNGLDPEIVRQAVKQLFYLVGAVTLNSLLLRKDMCSCRKGMQIR 1607
Cdd:cd15478 161 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1608 CNISFLEEWLKDKNVQSSLAKETLEPLSQAAWLLQVKKTTDSDAKEIAQCCTSLSAVQIIKILNSYTPIDDFEKRVNPSF 1687
Cdd:cd15478 241 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 124486759 1688 VRKVQALLNNRGDSAQLMLDTKYLFQVTFPFTASPHALEMTQIPSSFKLGFLRRL 1742
Cdd:cd15478 321 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 375
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
83-741 |
6.48e-157 |
|
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: 495.71 E-value: 6.48e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP---------IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14907 3 LLINLKKRYQQDK-IFTYVGPTLIVMNPYKQIDnlfseevmqMYKEQIIQNGEYFDIKKEPPHIYAIAALAFKQLFENNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 154 NQSIIVSGESGAGKTVSARYAMRYFATVS------------------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNS 215
Cdd:cd14907 82 KQAIVISGESGAGKTENAKYAMKFLTQLSqqeqnseevltltssiraTSKSTKSIEQKILSCNPILEAFGNAKTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 216 SRFGKYTEISFDERNQ-IIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKL---GSAEEFNYTRMGGN 291
Cdd:cd14907 162 SRFGKYVSILVDKKKRkILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLknqLSGDRYDYLKKSNC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 292 TVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQ---VTTVGNERSSVSeDDSHLKVFCELLGLETSK 368
Cdd:cd14907 242 YEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQfddSTLDDNSPCCVK-NKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 369 VAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSG--KQHTF------IGVLDIYGFE 440
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMPKDekDQQLFqnkylsIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 441 TFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTL--IDFYDNQPVIDLIE-AKMGILELLDEECLLPHGT 517
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSYTDNQDVIDLLDkPPIGIFNLLDDSCKLATGT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 518 DENWLQKLYNNFvNKNSLFEKPRMSNS-SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVP 596
Cdd:cd14907 481 DEKLLNKIKKQH-KNNSKLIFPNKINKdTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGEDGS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 597 SSPFGAMITVKSAKQvikpntkhfrTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVL 676
Cdd:cd14907 560 QQQNQSKQKKSQKKD----------KFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVL 629
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124486759 677 ETIRISAQSYPSRWTYLEFYSRYGILmtqqelslsdkkevckvvlhrliqdSNQYQFGRTKIFFR 741
Cdd:cd14907 630 ESIRVRKQGYPYRKSYEDFYKQYSLL-------------------------KKNVLFGKTKIFMK 669
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
83-741 |
2.11e-154 |
|
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: 487.66 E-value: 2.11e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDM-DPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14897 3 IVQTLKSRYNKDK-FYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVRSQrPPHLFWIADQAYRRLLETGRNQCILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 162 ESGAGKTVSARYAMRYFATVSkSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYL 241
Cdd:cd14897 82 ESGAGKTESTKYMIKHLMKLS-PSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 242 LEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVNDRADMVETQKTFT-------LLG 314
Cdd:cd14897 161 LEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILR-DDNRNRPVFNDSEELEYYRQMFHdltnimkLIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 315 F-KKDFQMdVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14897 240 FsEEDISV-IFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 394 AINARDALAKKIYAHLFDFIVEQINQALH----FSGK-QHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVF 468
Cdd:cd14897 319 ANDSRDALAKDLYSRLFGWIVGQINRNLWpdkdFQIMtRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 469 KLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLyNNFVNKNSLFEKPRMSNSSFI 547
Cdd:cd14897 399 PRERSEYEIEGIEWRDIEYHDNDDVLELFFKKpLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESPRYVASPGNRVAFG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 548 IQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvpsspfgamitvksakqvikpnTKHfrttvgnk 627
Cdd:cd14897 478 IRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF--------------------------TSY-------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 628 FRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQE 707
Cdd:cd14897 524 FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFSN 603
|
650 660 670
....*....|....*....|....*....|....
gi 124486759 708 LSLSDKKEVCKVVLHrlIQDSNQYQFGRTKIFFR 741
Cdd:cd14897 604 KVRSDDLGKCQKILK--TAGIKGYQFGKTKVFLK 635
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
82-741 |
5.88e-153 |
|
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: 485.25 E-value: 5.88e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14911 2 SVLHNIKDRYY-SGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 162 ESGAGKTVSARYAMRYFATVS----KSSSNAH------------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEIS 225
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAaskpKGSGAVPhpavnpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 226 FDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVNDRADMVE 305
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLS-NGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 306 TQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETV 385
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 386 VKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFN 464
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 465 LHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN 543
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDFRGV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 544 SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAMITVKSAKQVIKpntKHFRtT 623
Cdd:cd14911 480 ADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQFGARTRK---GMFR-T 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 624 VGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM 703
Cdd:cd14911 556 VSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLT 635
|
650 660 670
....*....|....*....|....*....|....*....
gi 124486759 704 TQQ-ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14911 636 PNViPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
81-741 |
2.14e-151 |
|
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: 480.75 E-value: 2.14e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14917 1 PAVLYNLKERYA-SWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 161 GESGAGKTVSARYAMRYFATVS---------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQ 231
Cdd:cd14917 80 GESGAGKTVNTKRVIQYFAVIAaigdrskkdQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 232 IIGANMRTYLLEKSRVVFQSENERNYHIFYQLCaSAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKTF 310
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYQIL-SNKKPELLDMLLITNNPYDYAFISqGETTVASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 311 TLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMT 390
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 391 RPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKL 470
Cdd:cd14917 319 VQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 471 EQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR----MSNSS 545
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRnikgKPEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 546 FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPfgamitVKSAKQVIKPNTKHfrTTVG 625
Cdd:cd14917 479 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAP------IEKGKGKAKKGSSF--QTVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 626 NKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQ 705
Cdd:cd14917 551 ALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 630
|
650 660 670
....*....|....*....|....*....|....*...
gi 124486759 706 Q--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14917 631 AipEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
81-741 |
1.55e-149 |
|
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: 475.94 E-value: 1.55e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAY------SGQNM---GDMDPHIFAVAEEAYKQMARN 151
Cdd:cd14908 1 PAILHSLSRRFFRGI-IYTWTGPVLIAVNPFQRLPLYGKEILESYrqegllRSQGIespQALGPHVFAIADRSYRQMMSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 152 NR-NQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAHVE----------DKVLASNPITEAVGNAKTTRNDNSSRFGK 220
Cdd:cd14908 80 IRaSQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEgeelgklsimDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 221 YTEISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGS--------AEEFNYTRMGGNT 292
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDgitgglqlPNEFHYTGQGGAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 293 VIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVS---EDDSHLKVFCELLGLETSKV 369
Cdd:cd14908 240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIaeeGNEKCLARVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 370 AQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ--HTFIGVLDIYGFETFDVNSF 447
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKdiRSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 448 EQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEA-KMGILELLDEECLLP-HGTDENWLQKL 525
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAkKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 526 YNNF-------VNKNSLFEKPRM--SNSSFIIQHFADKVEYQCE-GFLEKNRDTVydmlveilraskfhlcaaffqespv 595
Cdd:cd14908 480 YETYlpeknqtHSENTRFEATSIqkTKLIFAVRHFAGQVQYTVEtTFCEKNKDEI------------------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 596 psspfgamitvksakqvikPNTKHFRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGV 675
Cdd:cd14908 535 -------------------PLTADSLFESGQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGV 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 676 LETIRISAQSYPSRWTYLEFYSRYGILM-TQQELSLSDK-----------KEVCKV-VLHRLIQD--------SNQYQFG 734
Cdd:cd14908 596 LEAVRVARSGYPVRLPHKDFFKRYRMLLpLIPEVVLSWSmerldpqklcvKKMCKDlVKGVLSPAmvsmknipEDTMQLG 675
|
....*..
gi 124486759 735 RTKIFFR 741
Cdd:cd14908 676 KSKVFMR 682
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
83-741 |
7.18e-149 |
|
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: 473.62 E-value: 7.18e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 83 VLHNLRIRFAESkLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQM----ARNNRNQSII 158
Cdd:cd14889 3 LLEVLKVRFMQS-NIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMlgrlARGPKNQCIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 159 VSGESGAGKTVSARYAMRYFATVSKSssNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFdERNQIIGANMR 238
Cdd:cd14889 82 ISGESGAGKTESTKLLLRQIMELCRG--NSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 239 TYLLEKSRVVFQSENERNYHIFYQLCA--SAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADmvETQKTFTLLGFK 316
Cdd:cd14889 159 EYLLEKSRVVHQDGGEENFHIFYYMFAgiSAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYD--EVCNAMDMVGFT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 317 KDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSH-LKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAI 395
Cdd:cd14889 237 EQEEVDMFTILAGILSLGNITFEMDDDEALKVENDSNGwLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 396 NARDALAKKIYAHLFDFIVEQINQAL---HFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQ 472
Cdd:cd14889 317 DARDSIAKVAYGRVFGWIVSKINQLLapkDDSSVELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLMEQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 473 EEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNKNSLFEKPRMSNSSFIIQHF 551
Cdd:cd14889 397 KEYKKEGIDWKEITYKDNKPILDLFLNKpIGILSLLDEQSHFPQATDESFVDKLNIHF-KGNSYYGKSRSKSPKFTVNHY 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 552 ADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESpvpSSPFGAMITVKSAKQVIKPNTKHFR-TTVGNKFRS 630
Cdd:cd14889 476 AGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTAT---RSRTGTLMPRAKLPQAGSDNFNSTRkQSVGAQFKH 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 631 SLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSL 710
Cdd:cd14889 553 SLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILLCEPALPG 632
|
650 660 670
....*....|....*....|....*....|.
gi 124486759 711 SdkKEVCKVVLHRliQDSNQYQFGRTKIFFR 741
Cdd:cd14889 633 T--KQSCLRILKA--TKLVGWKCGKTRLFFK 659
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
82-741 |
6.75e-148 |
|
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: 470.66 E-value: 6.75e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14934 2 SVLDNLRQRYTNMR-IYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 162 ESGAGKTVSARYAMRYFATVSKSSSNA-----HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGAN 236
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSsdgkgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 237 MRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKL-GSAEEFNYTRMGgNTVIEGVNDRADMVETQKTFTLLGF 315
Cdd:cd14934 161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQG-VTVVDNMDDGEELQITDVAFDVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 316 KKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAI 395
Cdd:cd14934 240 SAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 396 NARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEY 475
Cdd:cd14934 320 NSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 476 MKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKP-----RMSNSSFIIQ 549
Cdd:cd14934 400 KREGIEWVFIDFgLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPkggkgKGPEAHFELV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 550 HFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamitvkSAKQviKPNTKHFrtTVGNKFR 629
Cdd:cd14934 480 HYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAG---------SKKQ--KRGSSFM--TVSNFYR 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 630 SSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQ-EL 708
Cdd:cd14934 547 EQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNViPQ 626
|
650 660 670
....*....|....*....|....*....|...
gi 124486759 709 SLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14934 627 GFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
81-741 |
1.91e-147 |
|
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: 469.99 E-value: 1.91e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14918 1 PGVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 161 GESGAGKTVSARYAMRYFATVSKSSS---------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQ 231
Cdd:cd14918 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 232 IIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKTF 310
Cdd:cd14918 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQI-TSNKKPDLIEMLLITTNPYDYAFVSqGEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 311 TLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMT 390
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 391 RPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKL 470
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 471 EQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRM----SNSS 545
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVvkgkAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 546 FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvpsSPFGAMITVKSAKQVIKPNTKHFRtTVG 625
Cdd:cd14918 479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLF-------STYASAEADSGAKKGAKKKGSSFQ-TVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 626 NKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQ 705
Cdd:cd14918 551 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 630
|
650 660 670
....*....|....*....|....*....|....*...
gi 124486759 706 Q--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14918 631 AipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
81-741 |
1.99e-147 |
|
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: 469.92 E-value: 1.99e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14916 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 161 GESGAGKTVSARYAMRYFATVSK----------SSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN 230
Cdd:cd14916 80 GESGAGKTVNTKRVIQYFASIAAigdrskkenpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 231 QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCaSAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKT 309
Cdd:cd14916 160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQIL-SNKKPELLDMLLVTNNPYDYAFVSqGEVSVASIDDSEELLATDSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 310 FTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPM 389
Cdd:cd14916 239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 390 TRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFK 469
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 470 LEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR----MSNS 544
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRnvkgKQEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 545 SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvpSSPFGAMITVKSAKQVIKPNTKHFRtTV 624
Cdd:cd14916 479 HFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLF------STYASADTGDSGKGKGGKKKGSSFQ-TV 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 625 GNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL-- 702
Cdd:cd14916 552 SALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILnp 631
|
650 660 670
....*....|....*....|....*....|....*....
gi 124486759 703 MTQQELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14916 632 AAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
82-741 |
8.13e-147 |
|
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: 468.35 E-value: 8.13e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14932 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 162 ESGAGKTVSARYAMRYFATVSKSS-----------SNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN 230
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 231 QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLgsaEEFNYTRM--GGNTVIEGVNDRADMVETQK 308
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCL---EDYSKYRFlsNGNVTIPGQQDKELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 389 MTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHV 467
Cdd:cd14932 318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 468 FKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPR--M 541
Cdd:cd14932 398 FILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQGN-NPKFQKPKklK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 542 SNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESP--VPSSPFGAMitVKSAKQVIKPNTKH 619
Cdd:cd14932 477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDriVGLDKVAGM--GESLHGAFKTRKGM 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 620 FRtTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRY 699
Cdd:cd14932 555 FR-TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 633
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 124486759 700 GILM-TQQELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14932 634 EILTpNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
81-741 |
1.46e-146 |
|
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: 467.67 E-value: 1.46e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14912 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 161 GESGAGKTVSARYAMRYFATVSKSSS-----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDER 229
Cdd:cd14912 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 230 NQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQK 308
Cdd:cd14912 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-TSNKKPELIEMLLITTNPYDYPFVSqGEISVASIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14912 239 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 389 MTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVF 468
Cdd:cd14912 319 QTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 469 KLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRM----SN 543
Cdd:cd14912 399 VLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVvkgkAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 544 SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvKSAKQVIKPNTKHFRtT 623
Cdd:cd14912 479 AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAG----GGAKKGGKKKGSSFQ-T 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 624 VGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM 703
Cdd:cd14912 554 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 633
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 124486759 704 TQQ--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14912 634 ASAipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
81-741 |
9.24e-146 |
|
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: 465.36 E-value: 9.24e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14910 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 161 GESGAGKTVSARYAMRYFATVSKSSS-----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDER 229
Cdd:cd14910 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 230 NQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQK 308
Cdd:cd14910 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-MSNKKPDLIEMLLITTNPYDYAFVSqGEITVPSIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14910 239 AIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 389 MTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVF 468
Cdd:cd14910 319 QTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 469 KLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN---- 543
Cdd:cd14910 399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKgkve 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 544 SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvksAKQVIKPNTKHFRtT 623
Cdd:cd14910 479 AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGG------GKKGGKKKGSSFQ-T 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 624 VGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM 703
Cdd:cd14910 552 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 631
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 124486759 704 TQQ--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 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 |
2.07e-145 |
|
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: 463.36 E-value: 2.07e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFA-ESKLIYTYSGIILVAMNPYKQLPiygDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNN---RNQS 156
Cdd:cd14891 1 AGILHNLEERSKlDNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSgrmQNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 157 IIVSGESGAGKTVSARYAMRY------------FATVSKSSSNAH-----VEDKVLASNPITEAVGNAKTTRNDNSSRFG 219
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFlttravggkkasGQDIEQSSKKRKlsvtsLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 220 KYTEISF-DERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVN 298
Cdd:cd14891 158 KFMKLQFtKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 299 DRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQV----TTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLC 374
Cdd:cd14891 238 DAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFdeedTSEGEAEIASESDKEALATAAELLGVDEEALEKVIT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 375 NRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFD-VNSFEQFCIN 453
Cdd:cd14891 318 QREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLIN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 454 YANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFvNK 532
Cdd:cd14891 398 YANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPnGILPLLDNEARNPNPSDAKLNETLHKTH-KR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 533 NSLF--EKPRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASkfhlcaaffqespvpsspfgamitvksak 610
Cdd:cd14891 477 HPCFprPHPKDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS----------------------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 611 qvikpntkhfrttvgNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRW 690
Cdd:cd14891 528 ---------------AKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRV 592
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 124486759 691 TYLEFYSRYGILMTQQELSL--SDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14891 593 TYAELVDVYKPVLPPSVTRLfaENDRTLTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
81-741 |
4.53e-144 |
|
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: 460.74 E-value: 4.53e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14915 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 161 GESGAGKTVSARYAMRYFATVSKSSS-----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDER 229
Cdd:cd14915 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeaasgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 230 NQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQK 308
Cdd:cd14915 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-MSNKKPELIEMLLITTNPYDFAFVSqGEITVPSIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14915 239 AVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 389 MTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVF 468
Cdd:cd14915 319 QTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 469 KLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR----MSN 543
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKpakgKAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 544 SSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvksAKQVIKPNTKHFRtT 623
Cdd:cd14915 479 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGG------GKKGGKKKGSSFQ-T 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 624 VGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILM 703
Cdd:cd14915 552 VSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 631
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 124486759 704 TQQ--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14915 632 ASAipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
81-741 |
7.76e-144 |
|
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: 460.31 E-value: 7.76e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14923 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 161 GESGAGKTVSARYAMRYFATVS----------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN 230
Cdd:cd14923 80 GESGAGKTVNTKRVIQYFATIAvtgdkkkeqqPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 231 QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRADMVETQKT 309
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQI-MSNKKPELIDLLLISTNPFDFPFVSqGEVTVASIDDSEELLATDNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 310 FTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPM 389
Cdd:cd14923 239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 390 TRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFK 469
Cdd:cd14923 319 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 470 LEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR----MSNS 544
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKpakgKAEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 545 SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGAmitvkSAKQVIKPNTKHFRtTV 624
Cdd:cd14923 479 HFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSG-----GSKKGGKKKGSSFQ-TV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 625 GNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMT 704
Cdd:cd14923 553 SAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNA 632
|
650 660 670
....*....|....*....|....*....|....*....
gi 124486759 705 QQ--ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14923 633 SAipEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
82-741 |
5.00e-143 |
|
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: 457.94 E-value: 5.00e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14921 2 SVLHNLRERYF-SGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 162 ESGAGKTVSARYAMRYFATVSKS-------SSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIG 234
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASShkgkkdtSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 235 ANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLgsaEEF-NYTRMGGNTVIEGVNDRADMV-ETQKTFTL 312
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLL---EGFnNYTFLSNGFVPIPAAQDDEMFqETLEAMSI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 313 LGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd14921 238 MGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 393 QAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLE 471
Cdd:cd14921 318 QADFAIEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 472 QEEYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRM--SNSS 545
Cdd:cd14921 398 QEEYQREGIEWNFIDFgLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQGN-HPKFQKPKQlkDKTE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 546 FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQE-SPVPSSPFGAMITVKSAKQVIKPNTKHFRtTV 624
Cdd:cd14921 477 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDvDRIVGLDQMAKMTESSLPSASKTKKGMFR-TV 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 625 GNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMT 704
Cdd:cd14921 556 GQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 635
|
650 660 670
....*....|....*....|....*....|....*...
gi 124486759 705 QQ-ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14921 636 NAiPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
71-791 |
1.19e-141 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 459.50 E-value: 1.19e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 71 DLTALSYLHEPAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAY-SGQNMGDMDPHIFAVAEEAYKQMA 149
Cdd:PTZ00014 100 DIGLLPHTNIPCVLDFLKHRY-LKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYrDAKDSDKLPPHVFTTARRALENLH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 150 RNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDER 229
Cdd:PTZ00014 179 GVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 230 NQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYtrMGGNTV-IEGVNDRADMVETQK 308
Cdd:PTZ00014 259 GGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKY--INPKCLdVPGIDDVKDFEEVME 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTtvGNERSSVSE----DDSHLKVF---CELLGLETSKVAQWLCNRKIVTS 381
Cdd:PTZ00014 337 SFDSMGLSESQIEDIFSILSGVLLLGNVEIE--GKEEGGLTDaaaiSDESLEVFneaCELLFLDYESLKKELTVKVTYAG 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 382 SETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQ 461
Cdd:PTZ00014 415 NQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQK 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 462 QFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR 540
Cdd:PTZ00014 495 NFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGkSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKV 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 541 MSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSPFGamitvksAKQVIkpntkhf 620
Cdd:PTZ00014 575 DSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKGKLA-------KGQLI------- 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 621 rttvGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYG 700
Cdd:PTZ00014 641 ----GSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFK 716
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 701 ILmtqqELSLS-----DKKEVCKVVLHRLIQDSNQYQFGRTKIFFR---AGQVAYLEKLRLDKLRQDCIMIQKHVRGWLQ 772
Cdd:PTZ00014 717 YL----DLAVSndsslDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKK 792
|
730
....*....|....*....
gi 124486759 773 RRKFLRERQAALTIQRYFR 791
Cdd:PTZ00014 793 KRKVRKNIKSLVRIQAHLR 811
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
82-741 |
3.88e-139 |
|
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: 447.23 E-value: 3.88e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14930 2 SVLHNLRERYY-SGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 162 ESGAGKTVSARYAMRYFATVSKSSSN-------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIG 234
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGrkepgvpGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 235 ANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTviEGVNDRADMVETQKTFTLLG 314
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSS--SPGQERELFQETLESLRVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 315 FKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14930 239 FSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 395 INARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd14930 319 DFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 474 EYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNKNSLFEKPR--MSNSSFI 547
Cdd:cd14930 399 EYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQE-QGGHPKFQRPRhlRDQADFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 548 IQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFF----------QESPVPSSPFGAmitvksakqviKPNT 617
Cdd:cd14930 478 VLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvegivgleQVSSLGDGPPGG-----------RPRR 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 618 KHFRtTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYS 697
Cdd:cd14930 547 GMFR-TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 124486759 698 RYGILMTQQ-ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14930 626 RYEILTPNAiPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
81-741 |
1.90e-138 |
|
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: 446.71 E-value: 1.90e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDaiIHAYSGQNMGDMD--PHIFAVAEEAYKQMARNN------ 152
Cdd:cd14895 1 PAFVDYLAQRYGVDQ-VYCRSGAVLIAVNPFKHIPGLYD--LHKYREEMPGWTAlpPHVFSIAEGAYRSLRRRLhepgas 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 153 -RNQSIIVSGESGAGKTVSARYAMRYFATVSK--------SSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTE 223
Cdd:cd14895 78 kKNQTILVSGESGAGKTETTKFIMNYLAESSKhttatsssKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 224 ISF-----DERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFK--HLKLGSAEEFNYTRMGGNTVI-E 295
Cdd:cd14895 158 MFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLelQLELLSAQEFQYISGGQCYQRnD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 296 GVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVqvtTVGNERSSVSEDDS---------------------H 354
Cdd:cd14895 238 GVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNV---LFVASSEDEGEEDNgaasapcrlasaspssltvqqH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 355 LKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALhfSGKQHT----- 429
Cdd:cd14895 315 LDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSAS--PQRQFAlnpnk 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 430 --------FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK- 500
Cdd:cd14895 393 aankdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRp 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 501 MGILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRMSNS--SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEIL 578
Cdd:cd14895 473 SGIFSLLDEECVVPKGSDAGFARKLYQRLQE-HSNFSASRTDQAdvAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 579 -RASKFHLCAAFfqespvpsSPFGAmiTVKSAKQVIKPNTKHFRTT-----VGNKFRSSLYLLMETLNATTPHYVRCIKP 652
Cdd:cd14895 552 gKTSDAHLRELF--------EFFKA--SESAELSLGQPKLRRRSSVlssvgIGSQFKQQLASLLDVVQQTQTHYIRCIKP 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 653 NDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQ---ELSLSDKKEVCKVvlhrliqdsN 729
Cdd:cd14895 622 NDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKnasDATASALIETLKV---------D 692
|
730
....*....|..
gi 124486759 730 QYQFGRTKIFFR 741
Cdd:cd14895 693 HAELGKTRVFLR 704
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
83-739 |
3.76e-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: 444.29 E-value: 3.76e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 83 VLHNLRIRFAESkLIYTYSGIILVAMNPYKQLP-IYGDAIIHAY-SGQNMGDMDPHIFAVAEEAYK--QMARNNRNQSII 158
Cdd:cd14880 3 VLRCLQARYTAD-TFYTNAGCTLVALNPFKPVPqLYSPELMREYhAAPQPQKLKPHIFTVGEQTYRnvKSLIEPVNQSIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 159 VSGESGAGKTVSARYAMRYFATVSKSSSN-------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQ 231
Cdd:cd14880 82 VSGESGAGKTWTSRCLMKFYAVVAASPTSweshkiaERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 232 IIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEgvndraDMVE-TQKTF 310
Cdd:cd14880 162 MTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNLEE------DCFEvTREAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 311 TLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSS---VSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVV- 386
Cdd:cd14880 236 LHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQVf 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 387 -KPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQHT-FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFN 464
Cdd:cd14880 316 kKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTtFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 465 LHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN 543
Cdd:cd14880 396 AHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSpISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKLSR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 544 S-SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFqespvPSSPfgamitVKSAKQVIKPNTKHFRT 622
Cdd:cd14880 476 EpSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLF-----PANP------EEKTQEEPSGQSRAPVL 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 623 TVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL 702
Cdd:cd14880 545 TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLL 624
|
650 660 670
....*....|....*....|....*....|....*..
gi 124486759 703 MTQQELSLSDKKEVCKVVLHrliqdSNQYQFGRTKIF 739
Cdd:cd14880 625 RRLRPHTSSGPHSPYPAKGL-----SEPVHCGRTKVF 656
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
82-741 |
1.46e-137 |
|
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: 442.99 E-value: 1.46e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14919 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 162 ESGAGKTVSARYAMRYFATVSKS----SSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANM 237
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASShkskKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 238 RTYLLEKSRVVFQSENERNYHIFYQLCASAQQsefkHLKLG-SAEEFNYTRM--GGNTVIEGVNDRADMVETQKTFTLLG 314
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGE----HLKTDlLLEPYNKYRFlsNGHVTIPGQQDKDMFQETMEAMRIMG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 315 FKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14919 237 IPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 395 INARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd14919 317 DFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 474 EYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNKNSLFEKPRM--SNSSFI 547
Cdd:cd14919 397 EYQREGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQE-QGTHPKFQKPKQlkDKADFC 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 548 IQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQE-SPVPSSPFGAMITVKSAKQVIKPNTKHFRtTVGN 626
Cdd:cd14919 476 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvDRIIGLDQVAGMSETALPGAFKTRKGMFR-TVGQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 627 KFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQ 706
Cdd:cd14919 555 LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS 634
|
650 660 670
....*....|....*....|....*....|....*.
gi 124486759 707 -ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14919 635 iPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
81-741 |
3.05e-136 |
|
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: 440.87 E-value: 3.05e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAY--------SGQNMGDMDPHIFAVAEEAYKQMARN 151
Cdd:cd14902 1 AALLQALSERF-EHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFGGLLKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 152 NR-NQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAHVED--------KVLASNPITEAVGNAKTTRNDNSSRFGKYT 222
Cdd:cd14902 80 ERrNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGsdaveigkRILQTNPILESFGNAQTIRNDNSSRFGKFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 223 EISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEF----NYTRMGGNTVIEGVN 298
Cdd:cd14902 160 KIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYellnSYGPSFARKRAVADK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 299 DRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVS---EDDSHLKVFCELLGLETSKVAQWLCN 375
Cdd:cd14902 240 YAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAvtaASRFHLAKCAELMGVDVDKLETLLSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 376 RKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQAL-HFSGKQH--------TFIGVLDIYGFETFDVNS 446
Cdd:cd14902 320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEInYFDSAVSisdedeelATIGILDIFGFESLNRNG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 447 FEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKL 525
Cdd:cd14902 400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSnGLFSLLDQECLMPKGSNQALSTKF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 526 YNNFVNKNslfekprmsnsSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamiT 605
Cdd:cd14902 480 YRYHGGLG-----------QFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRDSP------G 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 606 VKSAKQVIKPNTKHFRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQS 685
Cdd:cd14902 543 ADNGAAGRRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHG 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 686 YPSRWTYLEFYSRYGILMTQQELSLSDKK-------------EVCKVVLHRLIQDSNQ---------------------- 730
Cdd:cd14902 623 YSVRLAHASFIELFSGFKCFLSTRDRAAKmnnhdlaqalvtvLMDRVLLEDGVEREEKnpgaltavtgdgsgtafendcr 702
|
730
....*....|....
gi 124486759 731 ---YQFGRTKIFFR 741
Cdd:cd14902 703 rkdVQVGRTLVFCK 716
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
82-741 |
7.11e-136 |
|
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: 438.73 E-value: 7.11e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd15896 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 162 ESGAGKTVSARYAMRYFATVSKS-----------SSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN 230
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 231 QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLgsaEEFNYTRM--GGNTVIEGVNDRADMVETQK 308
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLL---ENYNNYRFlsNGNVTIPGQQDKDLFTETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 309 TFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKP 388
Cdd:cd15896 238 AFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 389 MTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHV 467
Cdd:cd15896 318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 468 FKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIE---AKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSN 543
Cdd:cd15896 398 FILEQEEYQREGIEWSFIDFgLDLQPCIDLIEkpaSPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 544 SS-FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQ--ESPVPSSPFGAMITVKSAkqvIKPNTKHF 620
Cdd:cd15896 478 EAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKdvDRIVGLDKVSGMSEMPGA---FKTRKGMF 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 621 RtTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYG 700
Cdd:cd15896 555 R-TVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 633
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 124486759 701 ILMTQQ-ELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd15896 634 ILTPNAiPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
81-739 |
1.94e-135 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 436.34 E-value: 1.94e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSG-QNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14876 1 PCVLDFLKHRYLKNQ-IYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 160 SGESGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRT 239
Cdd:cd14876 80 SGESGAGKTEATKQIMRYFASAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYtrMGGNTV-IEGVNDRADMVETQKTFTLLGFKKD 318
Cdd:cd14876 160 FLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKF--LNPKCLdVPGIDDVADFEEVLESLKSMGLTEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 319 FQMDVFKILAAILHLGNVQVTT-----VGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14876 238 QIDTVFSIVSGVLLLGNVKITGkteqgVDDAAAISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 394 AINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd14876 318 AEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERESK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 474 EYMKEDIPWTLIDFYDNQPVID-LIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSNSSFIIQHFA 552
Cdd:cd14876 398 LYKDEGIPTAELEYTSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVDSNINFIVVHTI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 553 DKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamitvKSAK-QVIkpntkhfrttvGNKFRSS 631
Cdd:cd14876 478 GDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG--------KIAKgSLI-----------GSQFLKQ 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 632 LYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILmtqqELSLS 711
Cdd:cd14876 539 LESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFL----DLGIA 614
|
650 660 670
....*....|....*....|....*....|...
gi 124486759 712 -DKKEVCKVVLHRLIQDSN----QYQFGRTKIF 739
Cdd:cd14876 615 nDKSLDPKVAALKLLESSGlsedEYAIGKTMVF 647
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
83-741 |
2.89e-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: 425.07 E-value: 2.89e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMG-----DMDPHIFAVAEEAYKQMARNNRNQS 156
Cdd:cd14886 3 VIDILRDRFAKDK-IYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 157 IIVSGESGAGKTVSARYAMRYFATVSKSSSNAhVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGAN 236
Cdd:cd14886 82 CIVSGESGAGKTETAKQLMNFFAYGHSTSSTD-VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 237 MRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFK 316
Cdd:cd14886 161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKLFSK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 317 KDFQmDVFKILAAILHLGNVQ---VTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14886 241 NEID-SFYKCISGILLAGNIEfseEGDMGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 394 AINARDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQE 473
Cdd:cd14886 320 AEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEIQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 474 EYMKEDIPWTLIDFYDNQPVIDLIEA-KMGILELLDEECLLPHGTDENWLQKLYNNFvnKNSLFEKPRMSNSSFIIQHFA 552
Cdd:cd14886 400 EYEIEGIDHSMITFTDNSNVLAVFDKpNLSIFSFLEEQCLIQTGSSEKFTSSCKSKI--KNNSFIPGKGSQCNFTIVHTA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 553 DKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSspfgamitvksakqvikPNTKHfrTTVGNKFRSSL 632
Cdd:cd14886 478 ATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNED-----------------GNMKG--KFLGSTFQLSI 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 633 YLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSL-- 710
Cdd:cd14886 539 DQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILISHNSSSQna 618
|
650 660 670
....*....|....*....|....*....|..
gi 124486759 711 -SDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14886 619 gEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
83-734 |
9.75e-131 |
|
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: 425.93 E-value: 9.75e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 83 VLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQN-MGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14906 3 ILNNLGKRY-KSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINqNKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 161 GESGAGKTVSARYAMRYFATVSKSSS---------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQ 231
Cdd:cd14906 82 GESGSGKTEASKTILQYLINTSSSNQqqnnnnnnnNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSDG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 232 II-GANMRTYLLEKSRVVFQSENER-NYHIFYQLCASAQQSEFKHLKLGS-AEEFNY-------------TRMGGNTVIE 295
Cdd:cd14906 162 KIdGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNdPSKYRYldarddvissfksQSSNKNSNHN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 296 GVNDRADMVETQKTFTL-LGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVF---CELLGLETSKVAQ 371
Cdd:cd14906 242 NKTESIESFQLLKQSMEsMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLesvSKLLGYIESVFKQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 372 WLCNRKIVTSSETVV--KPMTRPQAINARDALAKKIYAHLFDFIVEQINQ-----------ALHFSGKQHTFIGVLDIYG 438
Cdd:cd14906 322 ALLNRNLKAGGRGSVycRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRkfnqntqsndlAGGSNKKNNLFIGVLDIFG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 439 FETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGT 517
Cdd:cd14906 402 FENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKsDGILSLLDDECIMPKGS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 518 DENWLQKLYNNFVNKNSLFEKPrMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQEspvps 597
Cdd:cd14906 482 EQSLLEKYNKQYHNTNQYYQRT-LAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQ----- 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 598 spfgamitvksaKQVIKPNTKHFRT---TVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACG 674
Cdd:cd14906 556 ------------QITSTTNTTKKQTqsnTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVG 623
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 675 VLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSlSDKKEVCKVVLHRLIQDSNQYQFG 734
Cdd:cd14906 624 VLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRK-NNNNPKLASQLILQNIQSKLKTMG 682
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
83-702 |
1.18e-128 |
|
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: 417.01 E-value: 1.18e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAY---------SGQNMGD--MDPHIFAVAEEAYKQMAR 150
Cdd:cd14900 3 ILSALETRFYAQK-IYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssSTRNKGSdpMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 151 --NNR--NQSIIVSGESGAGKTVSARYAMRYFA---------TVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSR 217
Cdd:cd14900 82 glNGVmsDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaaSVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 218 FGKYTEISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKhlklgsaeEFNYTRMggntviegv 297
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK--------RDMYRRV--------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 298 NDRADMVetqktftllGFKKDFQMDVFKILAAILHLGNV--QVTTVGNERSSvseDDSHLKVFCE--------LLGLETS 367
Cdd:cd14900 225 MDAMDII---------GFTPHERAGIFDLLAALLHIGNLtfEHDENSDRLGQ---LKSDLAPSSIwsrdaaatLLSVDAT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 368 KVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHF--SGKQHT---FIGVLDIYGFETF 442
Cdd:cd14900 293 KLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMddSSKSHGglhFIGILDIFGFEVF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 443 DVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENW 521
Cdd:cd14900 373 PKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRpTGILSLIDEECVMPKGSDTTL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 522 LQKLYNNFVNkNSLFEKPRMSNSS--FIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRAskfhlcaaffqespvpssp 599
Cdd:cd14900 453 ASKLYRACGS-HPRFSASRIQRARglFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVY------------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 600 fgamitvksakqvikpntkhfrttvGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETI 679
Cdd:cd14900 513 -------------------------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAV 567
|
650 660
....*....|....*....|...
gi 124486759 680 RISAQSYPSRWTYLEFYSRYGIL 702
Cdd:cd14900 568 RVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
81-741 |
2.84e-127 |
|
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: 413.79 E-value: 2.84e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14896 1 SSVLLCLKKRF-HLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 161 GESGAGKTVSARYAMRYFATVSKSSSNAHVE--DKVLasnPITEAVGNAKTTRNDNSSRFGKYTEISFdERNQIIGANMR 238
Cdd:cd14896 80 GHSGSGKTEAAKKIVQFLSSLYQDQTEDRLRqpEDVL---PILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 239 TYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKD 318
Cdd:cd14896 156 HYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 319 FQMDVFKILAAILHLGNVQVTTVGNERSSVSE--DDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAIN 396
Cdd:cd14896 236 ELTAIWAVLAAILQLGNICFSSSERESQEVAAvsSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 397 ARDALAKKIYAHLFDFIVEQINQALHFSGKQHTF--IGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEE 474
Cdd:cd14896 316 ARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEEE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 475 YMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNkNSLFEKPRMSNSSFIIQHFAD 553
Cdd:cd14896 396 CQRELLPWVPIPQPPRESCLDLLVDQpHSLLSILDDQTWLSQATDHTFLQKCHYHHGD-HPSYAKPQLPLPVFTVRHYAG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 554 KVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESpvpsspfgamitvkSAKQVIKPNtkhfRTTVGNKFRSSLY 633
Cdd:cd14896 475 TVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEA--------------EPQYGLGQG----KPTLASRFQQSLG 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 634 LLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDK 713
Cdd:cd14896 537 DLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEALSDR 616
|
650 660
....*....|....*....|....*...
gi 124486759 714 KEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14896 617 ERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
82-699 |
4.02e-115 |
|
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: 382.14 E-value: 4.02e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYS---GQNMGDM-------DPHIFAVAEEAYKQMAR 150
Cdd:cd14899 2 SILNALRLRY-ERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhNSQFGDRvtstdprEPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 151 NNRNQSIIVSGESGAGKTVSARYAMRYFATVS----------------KSSSNAHVEDKVLASNPITEAVGNAKTTRNDN 214
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCgtgnnnltnsesisppASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 215 SSRFGKYTEISF-DERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQL------CASAQQSEFKHLKLGSAEEFNYTR 287
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELlsadnnCVSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 288 MGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNER------------SSVSEDDSHL 355
Cdd:cd14899 241 SLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKGddtvfadearvmSSTTGAFDHF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 356 KVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGK--------- 426
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 427 ------QHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK 500
Cdd:cd14899 401 vddeedATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 501 -MGILELLDEECLLPHGTDENWLQKLYNNFVNKNslfEKPRMSNSS-------FIIQHFADKVEYQCEGFLEKNRDTVYD 572
Cdd:cd14899 481 pIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKN---SHPHFRSAPliqrttqFVVAHYAGCVTYTIDGFLAKNKDSFCE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 573 MLVEILRASKFHLCAAFFQESPVPSSPFGAMITVKSAKQVIKPNTKHFRTTVGNKFRSSLYLLMETLNATTPHYVRCIKP 652
Cdd:cd14899 558 SAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIKP 637
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 124486759 653 NDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRY 699
Cdd:cd14899 638 NDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
83-741 |
7.82e-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: 368.37 E-value: 7.82e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 83 VLHNLRIRFAESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAY-SGQNMGDMDPHIFAVAEEAYKQM-ARNNRNQSIIVS 160
Cdd:cd14875 3 LLHCIKERFEKLHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 161 GESGAGKTVSARYAMRYFATVS----KSSSNAHVEDKVLA----SNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQI 232
Cdd:cd14875 83 GESGSGKTENAKMLIAYLGQLSymhsSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPTSGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 233 -IGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHL-KLGSAEEFNYTRmGGNTVI------EGVNDRADMV 304
Cdd:cd14875 163 mVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLN-GGNTFVrrgvdgKTLDDAHEFQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 305 ETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVsEDDSHLKVFCELLGLETSKVAQWLcnrkIVTSSET 384
Cdd:cd14875 242 NVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQI-ADETPFLTACRLLQLDPAKLRECF----LVKSKTS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 385 VVKPMTRPQ-AINARDALAKKIYAHLFDFIVEQINQALHFSG--KQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQ 461
Cdd:cd14875 317 LVTILANKTeAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 462 QFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR 540
Cdd:cd14875 397 HYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKrTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPYFVLPK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 541 MS-NSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASkfhlcAAFFQESPVPSSPFGAmitvksakqvikpntkH 619
Cdd:cd14875 477 STiPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNS-----TDEFIRTLLSTEKGLA----------------R 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 620 FRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRY 699
Cdd:cd14875 536 RKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYF 615
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 124486759 700 GILMTQQELSL---SDKKEVCKVVLHRLIQ----DSNQYQFGRTKIFFR 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 |
1.86e-110 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 366.49 E-value: 1.86e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 82 AVLHNLRIRFAESkLIYTY-SGIILVAMNPYKQLPIYGDAIIHAY-------SGQNMGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14879 5 AITSHLASRFRSD-LPYTRlGSSALVAVNPYKYLSSNSDASLGEYgseyydtTSGSKEPLPPHAYDLAARAYLRMRRRSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 154 NQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAH-VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQI 232
Cdd:cd14879 84 DQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKKGTkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 233 IGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYT-RMGGNTVIEGV--NDRADMVETQKT 309
Cdd:cd14879 164 IGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLaSYGCHPLPLGPgsDDAEGFQELKTA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 310 FTLLGFKKDFQMDVFKILAAILHLGNVQVTT--VGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNR-KIVtSSEtVV 386
Cdd:cd14879 244 LKTLGFKRKHVAQICQLLAAILHLGNLEFTYdhEGGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTYKtKLV-RKE-LC 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 387 KPMTRP-QAINARDALAKKIYAHLFDFIVEQINQALHFSGKQ-HTFIGVLDIYGFETFD---VNSFEQFCINYANEKLQQ 461
Cdd:cd14879 322 TVFLDPeGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDDfATFISLLDFPGFQNRSstgGNSLDQFCVNFANERLHN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 462 QFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMG--ILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKP 539
Cdd:cd14879 402 YVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGglLGILDDQTRRMPKKTDEQMLEALRKRFGNHSSFIAVG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 540 RMS----NSSFIIQHFADKVEYQCEGFLEKNRDtvydmlveilraskfHLCAAFfqespvpsspfgaMITVKSAKQvikp 615
Cdd:cd14879 482 NFAtrsgSASFTVNHYAGEVTYSVEGFLERNGD---------------VLSPDF-------------VNLLRGATQ---- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 616 ntkhfrttvgnkFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEF 695
Cdd:cd14879 530 ------------LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEF 597
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 124486759 696 YSRYGILMTQQELSLSDKKevckvVLHRLIQDSNQYQFGRTKIFF 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 |
8.55e-107 |
|
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: 353.82 E-value: 8.55e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQlpIYGDAIIHAYSgQNMGDMDPHIFAVAEEAYKQMARNNrNQSIIVSG 161
Cdd:cd14898 2 ATLEILEKRYASGK-IYTKSGLVFLALNPYET--IYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVHG-NQTIVISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 162 ESGAGKTVSARYAMRYFatVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDerNQIIGANMRTYL 241
Cdd:cd14898 77 ESGSGKTENAKLVIKYL--VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 242 LEKSRVVFQSENERNYHIFYQLCASAqqsefkhlKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKdFQm 321
Cdd:cd14898 153 LEKSRVTHHEKGERNFHIFYQFCASK--------RLNIKNDFIDTSSTAGNKESIVQLSEKYKMTCSAMKSLGIAN-FK- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 322 DVFKILAAILHLGNVQVTtvgNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDAL 401
Cdd:cd14898 223 SIEDCLLGILYLGSIQFV---NDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIRNSM 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 402 AKKIYAHLFDFIVEQINQALHFSGKQHtfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIP 481
Cdd:cd14898 300 ARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEGIE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 482 WTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKL--YNN-FVNKNslfekprmSNSSFIIQHFADKVEYQ 558
Cdd:cd14898 378 WPDVEFFDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIkkYLNgFINTK--------ARDKIKVSHYAGDVEYD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 559 CEGFLEKNRDtvydmlveilrasKFHLcaaffqespvpsSPFGAMITvksakqvikpNTKHFRTTVGNKFRSSLYLLMET 638
Cdd:cd14898 450 LRDFLDKNRE-------------KGQL------------LIFKNLLI----------NDEGSKEDLVKYFKDSMNKLLNS 494
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486759 639 LNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL 702
Cdd:cd14898 495 INETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRIL 558
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
81-741 |
2.54e-100 |
|
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: 340.09 E-value: 2.54e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFAES-------KLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14887 1 PNLLENLYQRYNKAyinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 154 NQSIIVSGESGAGKTVSARYAMRYFATVS---KSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERN 230
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSdrrHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 231 QIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSefKHLKLGSAEEFNYTrmggntviegvndrADMVETQKTF 310
Cdd:cd14887 161 KLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAA--ATQKSSAGEGDPES--------------TDLRRITAAM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 311 TLLGFKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLC---NRKIVTSSETVVK 387
Cdd:cd14887 225 KTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSVSVGCEETAADRSHSSEVKClssGLKVTEASRKHLK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 388 PMTRP--------------------------------QAINARDALAKKIYAHLFDFIVEQINQALHFSGK--------- 426
Cdd:cd14887 305 TVARLlglppgvegeemlrlalvsrsvretrsffdldGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsded 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 427 -----QHTFIGVLDIYGFETF---DVNSFEQFCINYANEKlqqqfnLHVFKLEQ----EE--YMKEDIPWTLIDFYDNQP 492
Cdd:cd14887 385 tpsttGTQTIGILDLFGFEDLrnhSKNRLEQLCINYANER------LHCFLLEQlilnEHmlYTQEGVFQNQDCSAFPFS 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 493 -------------VIDLI-EAKMGILELLDEECLLPH----------GTDENW------------LQKLYNNFVNKNSLF 536
Cdd:cd14887 459 fplastltsspssTSPFSpTPSFRSSSAFATSPSLPSslsslssslsSSPPVWegrdnsdlfyekLNKNIINSAKYKNIT 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 537 EKPRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRAskfhlCAAFFQESPVPSSPFGAMITVKsakqvikpn 616
Cdd:cd14887 539 PALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLA-----CSTYTRLVGSKKNSGVRAISSR--------- 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 617 tkhfRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFY 696
Cdd:cd14887 605 ----RSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELW 680
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 124486759 697 SRYGILMTQQELSLSDKKEVCKVVLHRLIQDSNQYQFGRTKIFFR 741
Cdd:cd14887 681 RRYETKLPMALREALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
83-741 |
4.72e-95 |
|
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: 321.96 E-value: 4.72e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 83 VLHNLRIRFaESKLIYTYSGIILVAMNPYKQLpiygDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd14937 3 VLNMLALRY-KKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 163 SGAGKTVSARYAMRYFatVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLL 242
Cdd:cd14937 78 SGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 243 EKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTrMGGNTVIEGVNDRADMVETQKTFTLLGFKkDFQMD 322
Cdd:cd14937 156 ENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYI-VNKNVVIPEIDDAKDFGNLMISFDKMNMH-DMKDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 323 VFKILAAILHLGNVQVTTV-GNERSSVSE-DDSHLKVFCE---LLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAINA 397
Cdd:cd14937 234 LFLTLSGLLLLGNVEYQEIeKGGKTNCSElDKNNLELVNEisnLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 398 RDALAKKIYAHLFDFIVEQINQALHFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMK 477
Cdd:cd14937 314 CKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYKA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPRMSNSSFIIQHFADKVEY 557
Cdd:cd14937 394 EDILIESVKYTTNESIIDLLRGKTSIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINKNFVIKHTVSDVTY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 558 QCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESPVPSSpfgamitvksakqVIKPNTKHFrttvgnKFRSSLYLLME 637
Cdd:cd14937 474 TITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSES-------------LGRKNLITF------KYLKNLNNIIS 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 638 TLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAqSYPSRWTYLEFYSRYGIL--MTQQELSLSDKKE 715
Cdd:cd14937 535 YLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNISF-FFQYKYTFDVFLSYFEYLdySTSKDSSLTDKEK 613
|
650 660
....*....|....*....|....*.
gi 124486759 716 VCKVVLHRLiqDSNQYQFGRTKIFFR 741
Cdd:cd14937 614 VSMILQNTV--DPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
82-741 |
3.35e-93 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 317.14 E-value: 3.35e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAY---SGQNMGDMDPHIFAVAEEAYKQMARNNRNQSII 158
Cdd:cd14878 2 SLLYEIQKRFGNNQ-IYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 159 VSGESGAGKTVSARYAMRYFATVSKSSSNAhVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISF-DERNQIIGANM 237
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTT-FDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 238 RTYLLEKSRVVFQSENERNYHIFYQLC--ASAQQSEFKHLKLGSAEEF-NYTRMGGNTVIEGVNDRADMVETQKTFTLLG 314
Cdd:cd14878 160 YTYMLEKSRLVSQPPGQSNFLIFYLLMdgLSAEEKYGLHLNNLCAHRYlNQTMREDVSTAERSLNREKLAVLKQALNVVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 315 FKKDFQMDVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14878 240 FSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 395 INARDALAKKIYAHLFDFIVEQINQALH----FSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKL 470
Cdd:cd14878 320 EFYRDLLAKSLYSRLFSFLVNTVNCCLQsqdeQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 471 EQEEYMKEDIPWTLIDFYDNQP-VIDLIEAK-MGILELLDEECLLPHGTDENWLQKL--YNNFVNKNSLFEK-------- 538
Cdd:cd14878 400 EQTECVQEGVTMETAYSPGNQTgVLDFFFQKpSGFLSLLDEESQMIWSVEPNLPKKLqsLLESSNTNAVYSPmkdgngnv 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 539 -PRMSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQESpvpsspfgamitvksakqvikpnt 617
Cdd:cd14878 480 aLKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSK------------------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 618 khfRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYS 697
Cdd:cd14878 536 ---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLS 612
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 124486759 698 RYGILMtqqELSLSDKK-----EVCKVVLHRLIQDSnqYQFGRTKIFFR 741
Cdd:cd14878 613 RYKPLA---DTLLGEKKkqsaeERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
82-740 |
2.84e-91 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 310.89 E-value: 2.84e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 82 AVLHNLRIRFAESKLiYTYSGIILVAMNPYKQLPiygdAIIHAYSGQNMGDMdPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14881 2 AVMKCLQARFYAKEF-FTNVGPILLSVNPYRDVG----NPLTLTSTRSSPLA-PQLLKVVQEAVRQQSETGYPQAIILSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 162 ESGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDErnqiiGANMRT-- 239
Cdd:cd14881 76 TSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-----GALYRTki 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 240 --YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKT-FTLLGFK 316
Cdd:cd14881 151 hcYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKAcLGILGIP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 317 kdFqMDVFKILAAILHLGNVQVTTvGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQAIN 396
Cdd:cd14881 231 --F-LDVVRVLAAVLLLGNVQFID-GGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKSVCDANMSNM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 397 ARDALAKKIYAHLFDFIVEQIN--QALHFSGKQHT---FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLE 471
Cdd:cd14881 307 TRDALAKALYCRTVATIVRRANslKRLGSTLGTHAtdgFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTHIFKSS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 472 QEEYMKEDIPWTL-IDFYDNQPVIDLIEA-KMGILELLDEECLlPHGTDENWLQKLYNNFVNKNSLFEKPRMSNSSFIIQ 549
Cdd:cd14881 387 IESCRDEGIQCEVeVDYVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAKPQDDRMFGIR 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 550 HFADKVEYQCEGFLEKNRDTVYDMLVEILRAskfHLCAaffqespvpsspFGamitvksakqvIKPNTKHFRTTVGNkfr 629
Cdd:cd14881 466 HFAGRVVYDASDFLDTNRDVVPDDLVAVFYK---QNCN------------FG-----------FATHTQDFHTRLDN--- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 630 sslylLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELS 709
Cdd:cd14881 517 -----LLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLR 591
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 124486759 710 LSDKKEV--CKVVL-----HRLIQDSN---QYQFGRTKIFF 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 |
1.17e-87 |
|
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: 302.21 E-value: 1.17e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYS-------GQNMGDMDPHIFAVAEEAYKQMARNN 152
Cdd:cd14884 1 PNVLQNLKNRYLKNK-IYTFHASLLLALNPYKPLKeLYDQDVMNVYLhkksnsaASAAPFPKAHIYDIANMAYKNMRGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 153 RNQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQI 232
Cdd:cd14884 80 KRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVENT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 233 I---------GANMRTYLLEKSRVVFQSENERNYHIFYQL---CASAQQSE------FKHLKLGSAEEFNYTR-MGGNTV 293
Cdd:cd14884 160 QknmfngcfrNIKIKILLLEINRCIAHNFGERNFHVFYQVlrgLSDEDLARrnlvrnCGVYGLLNPDESHQKRsVKGTLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 294 IEGVNDRADMVETQK---TFTLL-------GFKKDFQMDVFKILAAILHLGNvqvttvgnerssvseddSHLKVFCELLG 363
Cdd:cd14884 240 LGSDSLDPSEEEKAKdekNFVALlhglhyiKYDERQINEFFDIIAGILHLGN-----------------RAYKAAAECLQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 364 LETSKVAQWLCNRKIVTSSETVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQAlHFSGKQ-------------HTF 430
Cdd:cd14884 303 IEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRN-VLKCKEkdesdnediysinEAI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 431 IGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEE 510
Cdd:cd14884 382 ISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAKIFRRLDDITKL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 511 CLLPHG-TDENWLQKLYNNfVNKNSLFEK-------PRMSNSS----------FIIQHFADKVEYQCEGFLEKNRDTVYD 572
Cdd:cd14884 462 KNQGQKkTDDHFFRYLLNN-ERQQQLEGKvsygfvlNHDADGTakkqnikkniFFIRHYAGLVTYRINNWIDKNSDKIET 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 573 MLVEILRASKfhlcaaffqespvpsspfgaMITVKSAkqVIKPNTKHFrTTVGNKFRSSLYLLMETLNATTPHYVRCIKP 652
Cdd:cd14884 541 SIETLISCSS--------------------NRFLREA--NNGGNKGNF-LSVSKKYIKELDNLFTQLQSTDMYYIRCFLP 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 653 NDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRwtylefysrygilMTQQELSLSDKKEVCKVVLHRLIQDSNQYQ 732
Cdd:cd14884 598 NAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHK-------------IPKKETAAALKEQIAKELEKCNSNTDIEYQ 664
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
83-741 |
2.45e-86 |
|
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: 298.45 E-value: 2.45e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 83 VLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd01386 3 VLHTLRQRYG-ANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 163 SGAGKTVSARYAMRYFATVSKSSSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLL 242
Cdd:cd01386 82 SGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 243 EKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRA-DMVETQKTFTLLGFKKDFQM 321
Cdd:cd01386 162 ERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKAAaAFSKLQAAMKTLGISEEEQR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 322 DVFKILAAILHLGNVQVTTVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRK---IVTSSETVVKPMTRPQ----- 393
Cdd:cd01386 242 AIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHlsgGPQQSTTSSGQESPARsssgg 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 394 ----AINARDALAKKIYAHLFDFIVEQINQALhfSGKQHTF--IGVLDIYGFEtfdvN----------SFEQFCINYANE 457
Cdd:cd01386 322 pkltGVEALEGFAAGLYSELFAAVVSLINRSL--SSSHHSTssITIVDTPGFQ----NpahsgsqrgaTFEDLCHNYAQE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 458 KLQQQFNLHVFKLEQEEYMKEDIPWTLIDFYDN-QPVIDLI---------------EAKMGILELLDEECLLPHGTDENW 521
Cdd:cd01386 396 RLQLLFHERTFVAPLERYKQENVEVDFDLPELSpGALVALIdqapqqalvrsdlrdEDRRGLLWLLDEEALYPGSSDDTF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 522 LQKLYNNF----VNKNSLFEKPRMSNSSFIIQHF--ADKVEYQCEGFLeknrdtvydmlveilRASKFHLCA----AFFQ 591
Cdd:cd01386 476 LERLFSHYgdkeGGKGHSLLRRSEGPLQFVLGHLlgTNPVEYDVSGWL---------------KAAKENPSAqnatQLLQ 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 592 ESpvpSSPFGAmitVKsakqvikpntkhfRTTVGNKFRSSLYLLMETLNATTPHYVRCIKPN------DEKMPFEFDSKR 665
Cdd:cd01386 541 ES---QKETAA---VK-------------RKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkdERSTSSPAAGDE 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 666 IVQ------QLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMTQQELSLSDKKEVC--KVVLHRLIQ----DSNQYQF 733
Cdd:cd01386 602 LLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLNSEVAdeRKAVEELLEeldlEKSSYRI 681
|
....*...
gi 124486759 734 GRTKIFFR 741
Cdd:cd01386 682 GLSQVFFR 689
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
93-741 |
1.22e-80 |
|
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: 281.21 E-value: 1.22e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 93 ESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSgQNMGdMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTVSA 171
Cdd:cd14905 12 KKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN-QRRG-LPPHLFALAAKAISDMQDFRRDQLIFIGGESGSGKSENT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 172 RYAMRYFATVSKSSSNaHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLLEKSRVVFQS 251
Cdd:cd14905 90 KIIIQYLLTTDLSRSK-YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 252 ENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRADMVETQKTFTLLGFKKDFQMDVFKILAAIL 331
Cdd:cd14905 169 KGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFII 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 332 HLGNVQVTTvGNERSSVsEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSEtvvkpmtrpqAINARDALAKKIYAHLFD 411
Cdd:cd14905 249 ILGNVTFFQ-KNGKTEV-KDRTLIESLSHNITFDSTKLENILISDRSMPVNE----------AVENRDSLARSLYSALFH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 412 FIVEQINQALHFSGKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPW-TLIDFYDN 490
Cdd:cd14905 317 WIIDFLNSKLKPTQYSHT-LGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWmTPISFKDN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 491 QPVIDLIEAKMGILELLDEECllpHGTDENWLQKLyNNFVNKNSLF-EKPrmsnSSFIIQHFADKVEYQCEGFLEKNRDT 569
Cdd:cd14905 396 EESVEMMEKIINLLDQESKNI---NSSDQIFLEKL-QNFLSRHHLFgKKP----NKFGIEHYFGQFYYDVRGFIIKNRDE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 570 VYDML-----------------VEILRASKFHLCAAFFQESPVPSSPFGAMITVKSA-----KQVIKPNTKH------FR 621
Cdd:cd14905 468 ILQRTnvlhknsitkylfsrdgVFNINATVAELNQMFDAKNTAKKSPLSIVKVLLSCgsnnpNNVNNPNNNSggggggGN 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 622 TTVGNKFRSSLYLLMETLNATTP------HYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEF 695
Cdd:cd14905 548 SGGGSGSGGSTYTTYSSTNKAINnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIF 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 124486759 696 YSRYGILMTQQE--LSLSDKKEVCKVVLHRLIQDSnqYQFGRTKIFFR 741
Cdd:cd14905 628 FDRFSFFFQNQRnfQNLFEKLKENDINIDSILPPP--IQVGNTKIFLR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
82-741 |
6.99e-78 |
|
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: 271.74 E-value: 6.99e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYsgqnmgdmdpHIFAVAEEAYKQMARNNRN-QSIIVS 160
Cdd:cd14874 2 GIAQNLHERF-KKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 161 GESGAGKTVSARYAMRYFATVSKSS-SNAHVEdkvlASNPITEAVGNAKTTRNDNSSRFGKYTEISFdERNQIIGANMR- 238
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKvTTKHSS----AIESVFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLNLKy 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 239 TYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNT--VIEGVNDRADMVETQKTftlLGFK 316
Cdd:cd14874 146 TVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTenIQSDVNHFKHLEDALHV---LGFS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 317 KDFQMDVFKILAAILHLGNVQVTTVGNerSSVSED------DSHLKVFCELLGLEtskVAQWLcnrKIVTSSETVVKPMT 390
Cdd:cd14874 223 DDHCISIYKIISTILHIGNIYFRTKRN--PNVEQDvveignMSEVKWVAFLLEVD---FDQLV---NFLLPKSEDGTTID 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 391 RPQAINARDALAKKIYAHLFDFIVEQInqALHFSGKQHT-FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFK 469
Cdd:cd14874 295 LNAALDNRDSFAMLIYEELFKWVLNRI--GLHLKCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFH 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 470 LEQEEYMKEDIPwtlIDF-----YDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNKnSLFEKPRMSN 543
Cdd:cd14874 373 DQLVDYAKDGIS---VDYkvpnsIENGKTVELLFKKpYGLLPLLTDECKFPKGSHESYLEHCNLNHTDR-SSYGKARNKE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 544 S-SFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRASKFHLCAAFFQespvpSSPFGAMITVKSAKQVIKPNTKHfrt 622
Cdd:cd14874 449 RlEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE-----SYSSNTSDMIVSQAQFILRGAQE--- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 623 tvgnkfrsslylLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGIL 702
Cdd:cd14874 521 ------------IADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 124486759 703 MTQQELSLSDKKEVCKVVLH-RLIQDSNQYQFGRTKIFFR 741
Cdd:cd14874 589 LPGDIAMCQNEKEIIQDILQgQGVKYENDFKIGTEYVFLR 628
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
83-741 |
6.62e-77 |
|
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: 269.30 E-value: 6.62e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 83 VLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd14882 3 ILEELRHRY-LMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 163 SGAGKTVSARYAMRYFATVSKSSSNahVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDERNQIIGANMRTYLL 242
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNRG--ATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 243 EKSRVVFQSENERNYHIFYQLCASAQQSE-FKHLKLGSAEEFNYTRMGGNTVIEGV----NDRADMVETQKTFTLLGFKK 317
Cdd:cd14882 160 EKLRVSTTDGNQSNFHIFYYFYDFIEAQNrLKEYNLKAGRNYRYLRIPPEVPPSKLkyrrDDPEGNVERYKEFEEILKDL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 318 DFQMD----VFKILAAILHLGNVQVttVGNERSSVSEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14882 240 DFNEEqletVRKVLAAILNLGEIRF--RQNGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHTTEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 394 AINARDALAKKIYAHLFDFIVEQINQALHFS----GKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFK 469
Cdd:cd14882 318 ARDARDVLASTLYSRLVDWIINRINMKMSFPravfGDKYS-ISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYNQRIFI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 470 LEQEEYMKEDIPWTLIDFYDNQPVID-LIEAKMGILELLDEECLLPHGTdenwlQKLYNNFVNKNSLFEKPrMSNSSFII 548
Cdd:cd14882 397 SEMLEMEEEDIPTINLRFYDNKTAVDqLMTKPDGLFYIIDDASRSCQDQ-----NYIMDRIKEKHSQFVKK-HSAHEFSV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 549 QHFADKVEYQCEGFLEKNRDTVYDMLVEILRASkfhlcaaffqespvpsspfgamiTVKSAKQVIKPNTKHFRTTVGNKF 628
Cdd:cd14882 471 AHYTGRIIYDAREFADKNRDFVPPEMIETMRSS-----------------------LDESVKLMFTNSQVRNMRTLAATF 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 629 RSSLYLLMETL----NATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMT 704
Cdd:cd14882 528 RATSLELLKMLsigaNSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLAF 607
|
650 660 670
....*....|....*....|....*....|....*..
gi 124486759 705 QQELSLSDKKEVCKVVLHRLIQDSnqYQFGRTKIFFR 741
Cdd:cd14882 608 DFDETVEMTKDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| Myo5-like_CBD |
cd14945 |
Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied ... |
1369-1695 |
5.04e-66 |
|
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: 225.74 E-value: 5.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1369 EDEGKLIQNLILDLKPRGVVVnmiPGLPAHILFMCVRYADSLNDANMLKSLMNSAINGIKHVVKEHFEDLEMLSFWLSNT 1448
Cdd:cd14945 1 SEEDSLLRGIVTDFEPSSGDH---KLTPAYILYLCIRHAASNGLTGQSTSLLNKVLKTIQQVVQQHNDDMQLLAFWLSNA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1449 CHFLNCLKQYSGEEEFMKYNSPQQNKNCLNNFDLTEYRQILSDVAIRIYHQFIIVMENNLQPiivpgmleyeslqgisgl 1528
Cdd:cd14945 78 SELLYFLKQDSKLYGAAGEAPQKEEEQKLTVSDLNELKQDLEAVSIKIYQQALKYLNKNLQP------------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1529 kptgfrkrsssiddtdayTMTSILQQLSYFYSTMCQNGLDPEIVRQAVKQLFYLVGAVTLNSLLLRKDMCSCRKGMQIRC 1608
Cdd:cd14945 140 ------------------KIRDIVKFLNSFLDLLKSFHVHPEIRSQVFTQLFSFINARLFNQLITKKDALSWSRGMQIRA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1609 NISFLEEWLKdKNVQSSLAKETLEPLSQAAWLLQVKKTTDSDAKEIAQCCTSLSAVQIIKILNSYTPIDDFEKRVNPSFV 1688
Cdd:cd14945 202 NISRLEEWCE-GRGLEHLAVDFLSKLIQAVQLLQLKKYTQEDIEILCELCPSLNPAQLQAILTQYQPANYGESPVPKEIL 280
|
....*..
gi 124486759 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 |
1.02e-65 |
|
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: 238.72 E-value: 1.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 84 LHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQN----------MGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14893 4 LYTLRARYRMEQ-VYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSReqtplyekdtVNDAPPHVFALAQNALRCMQDAGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 154 NQSIIVSGESGAGKTVSARYAMRYFATVSKSSSNAH-----------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYT 222
Cdd:cd14893 83 DQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPdsegasgvlhpIGQQILHAFTILEAFGNAATRQNRNSSRFAKMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 223 EISFDERNQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQ--SEFKHLKLG-SAEEFNYTRMGGNTVIEGVND 299
Cdd:cd14893 163 SVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdpTLRDSLEMNkCVNEFVMLKQADPLATNFALD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 300 RADMVETQKTFTLLGFKKDFQMDVFKILAAILHLGNVQV---------------TTVGNERSSVSEDDSHLKVFCELLGL 364
Cdd:cd14893 243 ARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvggansTTVSDAQSCALKDPAQILLAAKLLEV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 365 ETSKVAQWLCNRKIVT--SSETV--VKPMTRPQAINARDALAKKIYAHLFDFIVEQINQAL-----HFSGK----QHTFI 431
Cdd:cd14893 323 EPVVLDNYFRTRQFFSkdGNKTVssLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdRYEKSniviNSQGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 432 GVLDIYGFETFD--VNSFEQFCINYANEK-----LQQQFNLHVFKLEQEEYMKED--IPWTLIDF-YDNQPVIDLIEAK- 500
Cdd:cd14893 403 HVLDMVGFENLTpsQNSFDQLCFNYWSEKvhhfyVQNTLAINFSFLEDESQQVENrlTVNSNVDItSEQEKCLQLFEDKp 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 501 MGILELLDEECLLPHGTDENWLQKLY--NNFV------NKNSLFEKPRMSNSS-----FIIQHFADKVEYQCEGFLEKNR 567
Cdd:cd14893 483 FGIFDLLTENCKVRLPNDEDFVNKLFsgNEAVgglsrpNMGADTTNEYLAPSKdwrllFIVQHHCGKVTYNGKGLSSKNM 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 568 DTVYDMLVEILRASKFHLCAAffqespVPSSPFGAMITVKSAKQVIKpntkhfRTTVGNKFRSSLY-------------- 633
Cdd:cd14893 563 LSISSTCAAIMQSSKNAVLHA------VGAAQMAAASSEKAAKQTEE------RGSTSSKFRKSASsaresknitdsaat 630
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486759 634 -------LLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRY 699
Cdd:cd14893 631 dvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY 703
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
104-227 |
2.99e-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: 158.66 E-value: 2.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 104 ILVAMNPYKQLPIYGDA-IIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTVSARYAMRYFATVS 182
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 124486759 183 KSSSNA--------------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 |
1.08e-41 |
|
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: 165.39 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQN-MGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14938 1 PSVLYHLKERF-KNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDcIEDLSLNEYHVVHNALKNLNELKRNQSIII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 160 SGESGAGKTVSARYAMRYFATVSKSS------SNAHVEDKVLAS----------------NPITEAVGNAKTTRNDNSSR 217
Cdd:cd14938 80 SGESGSGKSEIAKNIINFIAYQVKGSrrlptnLNDQEEDNIHNEentdyqfnmsemlkhvNVVMEAFGNAKTVKNNNSSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 218 FGKYTEISFDERnQIIGANMRTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEefNYTRMGGNTVIEGV 297
Cdd:cd14938 160 FSKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIE--NYSMLNNEKGFEKF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 298 NDRAD-MVETQKTFTLLgFKKDFQMD-VFKILAAILHLGNVQVTTV---------------------------GNERSSV 348
Cdd:cd14938 237 SDYSGkILELLKSLNYI-FDDDKEIDfIFSVLSALLLLGNTEIVKAfrkksllmgknqcgqninyetilseleNSEDIGL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 349 SEDDSHLKVFCELLGLETSKVAQWLCNRKIVTSSeTVVKPMTRPQAINARDALAKKIYAHLFDFIVEQINQALHFSGKQH 428
Cdd:cd14938 316 DENVKNLLLACKLLSFDIETFVKYFTTNYIFNDS-ILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNIN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 429 TF---IGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNLHVFKLEQEEYMKEDIPWTL-IDFYDNQPVID-LIEAKMGI 503
Cdd:cd14938 395 INtnyINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNlLVGPTEGS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 504 LELLDEECLLPHGTDENWLQKLYNNFVNKNSLFEKPR---MSNSSFIIQHFADKVEYQCEGFLEKNRDTVYDMLVEILRA 580
Cdd:cd14938 475 LFSLLENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDditGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 581 SKFHLCAAFFQESPVPSSpfgAMITVKSAKQVIKPNTKHFRTTVGNK-------FRSSLYLLMETLNATTPHYVRCIKPN 653
Cdd:cd14938 555 SENEYMRQFCMFYNYDNS---GNIVEEKRRYSIQSALKLFKRRYDTKnqmavslLRNNLTELEKLQETTFCHFIVCMKPN 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 654 DEK-MPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYLEFYSRYGILMtqqelslSDKKEVCKVVLHRLIQDSNQYQ 732
Cdd:cd14938 632 ESKrELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKN-------EDLKEKVEALIKSYQISNYEWM 704
|
....*..
gi 124486759 733 FGRTKIF 739
Cdd:cd14938 705 IGNNMIF 711
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
187-705 |
9.69e-35 |
|
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: 144.89 E-value: 9.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 187 NAHVEDK---VLASNPITEAVGNAKTTRNDNSSRFGKYT--EISFDERN---QIIGANMRTYLLEKSRVVFQ------SE 252
Cdd:cd14894 239 NPHAAKKlsiVLDSNIVLEAFGHATTSMNLNSSRFGKMTtlQVAFGLHPwefQICGCHISPFLLEKSRVTSErgresgDQ 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 253 NERNYHIFYQLCASAQQSEF-----KHLKLGSAEEFNYTRMG-GNTVIEGVNDRADM----VETQKT----FTLLGFKKD 318
Cdd:cd14894 319 NELNFHILYAMVAGVNAFPFmrllaKELHLDGIDCSALTYLGrSDHKLAGFVSKEDTwkkdVERWQQvidgLDELNVSPD 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 319 FQMDVFKILAAILHLGNVQVT--TVGNE--RSSVSEDDSHLKVfCELLGL-ETSKVAQWLCNRKIV--TSSETVVKPMTR 391
Cdd:cd14894 399 EQKTIFKVLSAVLWLGNIELDyrEVSGKlvMSSTGALNAPQKV-VELLELgSVEKLERMLMTKSVSlqSTSETFEVTLEK 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 392 PQAINARDALAKKIYAHLFDFIVEQINQALHFS-----GKQH------------TFIGVLDIYGFETFDVNSFEQFCINY 454
Cdd:cd14894 478 GQVNHVRDTLARLLYQLAFNYVVFVMNEATKMSalstdGNKHqmdsnasapeavSLLKIVDVFGFEDLTHNSLDQLCINY 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 455 ANEKLQQqfnlhvfKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQ-----KLY-NN 528
Cdd:cd14894 558 LSEKLYA-------REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENMNAQQeekrnKLFvRN 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 529 FVNKNS--LFEKPR-MSNSS-----------FIIQHFADKVEYQCEGFLEKNRDTVY-DMLVEILRASKFHLCAAFFQES 593
Cdd:cd14894 631 IYDRNSsrLPEPPRvLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYaNLLVGLKTSNSSHFCRMLNESS 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 594 PVPSSPFGAMITVKSAKQVIKpNTKHFrttVGnKFRSSLYLLMETLNATTPHYVRCIKPNDEKMPFEFDSKRIVQQLRAC 673
Cdd:cd14894 711 QLGWSPNTNRSMLGSAESRLS-GTKSF---VG-QFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQ 785
|
570 580 590
....*....|....*....|....*....|....*....
gi 124486759 674 GV---LETIRISAQSYP----SRWTYLefySRYGILMTQ 705
Cdd:cd14894 786 RLirqMEICRNSSSSYSaidiSKSTLL---TRYGSLLRE 821
|
|
| DIL |
pfam01843 |
DIL domain; The DIL domain has no known function. |
1574-1675 |
1.34e-33 |
|
DIL domain; The DIL domain has no known function.
Pssm-ID: 460359 [Multi-domain] Cd Length: 103 Bit Score: 125.40 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1574 QAVKQLFYLVGAVTLNSLLLRKDMCSCRKGMQIRCNISFLEEWLKDKNVQSSlAKETLEPLSQAAWLLQVKKTTDSDAKE 1653
Cdd:pfam01843 1 QLFSQLFYFINAELFNRLLLRKKYCSWSKGMQIRYNLSRLEEWARSNGLESE-ARDHLAPLIQAAQLLQLRKSTLEDLDS 79
|
90 100
....*....|....*....|..
gi 124486759 1654 IAQCCTSLSAVQIIKILNSYTP 1675
Cdd:pfam01843 80 ILQVCPALNPLQLHRLLTLYQP 101
|
|
| Myo5p-like_CBD_DIL_ANK |
cd15473 |
cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ... |
1363-1717 |
6.08e-25 |
|
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: 107.64 E-value: 6.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1363 MLEYKKEDEGKLIQNLILDLKPRgVVVNMIPgLPAHILFMCVRYADSLNDANMLKSLMNSAINGIKHVVKEHFEDLEMLS 1442
Cdd:cd15473 2 MFVFSEDELPRILDLLITNMTPQ-RSPSQRP-VPANLLFLCARYAHYHCSPELLEDLLLGALDRIEDVVEANPWDMTLLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1443 FWLSNTC---HFLNCLKQYsgeeefmkynspqqnknclnNFDLTEYRQILSDVAIRIYHQFIIVMENNLQPIIvpgmley 1519
Cdd:cd15473 80 FWLSNVTlllHYLKKDAGL--------------------VEATPEFQQELAELINEIFVLIIRDAERRIDKLL------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1520 eslqgisglkptgfrkrsssidDTDAYTMTSILQQLSYfysTMCQNGLDPEIVRQAVKQLFYLVGAVTLNSLLLRKDMCS 1599
Cdd:cd15473 133 ----------------------DASPRNITSLLSSTLY---VLELYDVHPAIIIQALSQLFYWLGCELFNRILTNKKYLC 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1600 CRKGMQIRCNISFLEEWLKDKNVQ-------SSLAKETLEPLSQAAWLLQVKKTTDSDAKEIA--QCCTSLSAVQIIKIL 1670
Cdd:cd15473 188 RSKAMQIRMNLSALEDWARSNNLQpekgespPRIARSHLAPVIQLLQWLQCLSSLDDFESLIAtiQQLDALNPLQLLRAV 267
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 124486759 1671 NSYTPiDDFEKRVNPSFVRKVQALLNNRgdsaqlmLDTKYLFQVTFP 1717
Cdd:cd15473 268 KDYRY-EVNEGRMPEECVKYLAQLQKDW-------LDSRYMLPFSLP 306
|
|
| fMyo2p_CBD |
cd15480 |
cargo binding domain of fungal myosin 2; Yeast myosin V travels along actin cables, actin ... |
1443-1742 |
4.33e-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: 103.04 E-value: 4.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1443 FWLSNTcHFLNCLKQYSgEEEFMKYNSPqqnKNCLNNFDLTEYRQILSDV-------AIRIYHQFIIVMENNLQPiivpg 1515
Cdd:cd15480 97 FWLSNV-HELLSFVCLA-ESDILQGIGP---GKDMREEEWEEYERLVTVVkhdleslEYNIYHTWMKELKKRLEK----- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1516 mleyeslqgisglkptgfrkrsssiddtdayTMTSILQQLSYFYSTMCQNGLDPEIVRQAVKQLFYLVGAVTLNSLLLRK 1595
Cdd:cd15480 167 -------------------------------TMDDILNFFNKVYKSMKSYYIEESVIRQVVTELLKLIGVTAFNDLLMRR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1596 DMCSCRKGMQIRCNISFLEEWLKDKNVQSSLAKetLEPLSQAAWLLQVKKTTDSDAKEIAQCCTSLSAVQIIKILNSYTp 1675
Cdd:cd15480 216 NFLSWKRGLQINYNITRLEEWCKSHDIPEGTLQ--LEHLMQATKLLQLKKATLEDIEIIYDVCWILTPAQIQKLISQYY- 292
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486759 1676 IDDFEKRVNPSFVRKVQALLNNRGDSAQLML----DTKYLFQVtfPFTASPHALEmTQIPSSFKLGFLRRL 1742
Cdd:cd15480 293 VADYENPISPEILKAVAARVKPEDKSDHLLLiplvEEVGPFED--PFPREIAGLE-AYIPAWLNLPHIRRL 360
|
|
| Myo5p-like_CBD_fungal |
cd15474 |
cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin ... |
1436-1694 |
3.11e-21 |
|
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: 97.49 E-value: 3.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1436 EDLEMLSFWLSNT-------CHFLNCLKQYSGEEEFMKYNSPQQNKNClnnfdltEYRQILSdvaiRIYHQFIIVMENNL 1508
Cdd:cd15474 78 ETIPDGAFWLANLhelrsfvVYLLSLIEHSSSDEFSKESEEYWNTLFD-------KTLKHLS----NIYSTWIDKLNKHL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1509 QPIIVPGMLEYESLQGISGlkptgFRKRSSSIDDTDAYTMTSILQQLSYFYSTMCQNGLDPEIVRQAVKQLFYLVGAVTL 1588
Cdd:cd15474 147 SPKIEGAVLVLLTSLDLSE-----LIDLNKEFFNKPKKKMADLITFLNEVYDLLQSFSVQPELLNAIVSSTLQYINVEAF 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1589 NSLLLRKDMCSCRKGMQIRCNISFLEEWLKDKNVqsSLAKETLEPLSQAAWLLQVKKTTDSDAKEIAQCCTSLSAVQIIK 1668
Cdd:cd15474 222 NSLITKRSALSWKRGSQISYNVSRLKEWCHQHGL--SDANLQLEPLIQASKLLQLRKDDENDFKIILSVCYALNPAQIQK 299
|
250 260
....*....|....*....|....*.
gi 124486759 1669 ILNSYTPiDDFEKRVNPSFVRKVQAL 1694
Cdd:cd15474 300 LLDKYQP-ANYEAPVPKEFLNALEKL 324
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
850-1378 |
5.96e-17 |
|
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: 87.42 E-value: 5.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 850 YRKLLQEHKAVILQKYARAWLARRRFQNIRRfvLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKL 929
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLER--QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 930 EAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQ---MLQEKSEELKEKMDKLTRQLFDDVQ---- 1002
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERledRRERLQQEIEELLKKLEEAELKELQaele 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1003 KEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHH----------QLEEGQVTSD----------RLKGEVA 1062
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQlqarldslerLQENLEGFSEgvkallknqsGLSGILG 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1063 RLSKQAKTISEFEKEIEL-------------LQAQKIDVE--------------------KHVQSQKREMRERMSEVTKQ 1109
Cdd:TIGR02168 524 VLSELISVDEGYEAAIEAalggrlqavvvenLNAAKKAIAflkqnelgrvtflpldsikgTEIQGNDREILKNIEGFLGV 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1110 L--LESYDIE---DVRSRLS----VEDLEHLNE--------------DGEL----WFAYEGLKKATRVLESHFQSQKDCy 1162
Cdd:TIGR02168 604 AkdLVKFDPKlrkALSYLLGgvlvVDDLDNALElakklrpgyrivtlDGDLvrpgGVITGGSAKTNSSILERRREIEEL- 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1163 EKEIEGLNFKVVHLSQEINHLQKLFREetdINESIRHEVTRLTSENMMIPDFKQQISELERQKQDLESRLKEQAEKIEgK 1242
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEE---LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT-E 758
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1243 LEEPFSHLNRIREEERMQGRAVEAQSEMhpegKERLVGAIHEPHEAIkfpKKQPEAEEEVESILQQEASRLSLEKRDLEE 1322
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEE----LEAQIEQLKEELKAL---REALDELRAELTLLNEEAANLRERLESLER 831
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 124486759 1323 ELDMKDRMIRRLQDQVKTLTKTTEKANHvhlpsgSREYLGMLEYKKEDEGKLIQNL 1378
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAA------EIEELEELIEELESELEALLNE 881
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
890-1346 |
9.57e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 86.66 E-value: 9.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 890 RVQRLQKKLEDQNRENHGLVEKLTSLAAlRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDT---VEERLSKLQKHNA 966
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEE-KVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRlsrLEEEINGIEERIK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 967 ELELQRERAEQmLQEKSEELKEKMDKLTR--QLFDDVQ--KEEQQRLVLEKG------FELKTQAYEKQIESLREEIKAL 1036
Cdd:PRK03918 332 ELEEKEERLEE-LKKKLKELEKRLEELEErhELYEEAKakKEELERLKKRLTgltpekLEKELEELEKAKEEIEEEISKI 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1037 KDERSQLHHQLEEGQVTSDRLKGE-----------------------VARLSKQAKTISEFEKEIELLQAQKIDVEKHVQ 1093
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKKAkgkcpvcgrelteehrkelleeyTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1094 SQKREMRERmsEVTKQllesydIEDVRSRLSVEDLEHLNEDGELwfaYEGLKKATRVLESHFQSQKDCYEKeIEGLNFKV 1173
Cdd:PRK03918 491 KESELIKLK--ELAEQ------LKELEEKLKKYNLEELEKKAEE---YEKLKEKLIKLKGEIKSLKKELEK-LEELKKKL 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1174 VHLSQEinhLQKLFREETDINESIRHE----VTRLTSENMMIPDFKQQISELERQKQDLESRLKEQaEKIEGKLEEPFSH 1249
Cdd:PRK03918 559 AELEKK---LDELEEELAELLKELEELgfesVEELEERLKELEPFYNEYLELKDAEKELEREEKEL-KKLEEELDKAFEE 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1250 LNRIREE-ERMQGRAVEAQSEMHPEGKERLVGAIHEPHEAIKFPKKQpeaEEEVESILQQEASRLslekRDLEEELDMKD 1328
Cdd:PRK03918 635 LAETEKRlEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAE---LEELEKRREEIKKTL----EKLKEELEERE 707
|
490
....*....|....*...
gi 124486759 1329 RMIRRLQDQVKTLTKTTE 1346
Cdd:PRK03918 708 KAKKELEKLEKALERVEE 725
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
849-1349 |
1.07e-15 |
|
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: 83.24 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 849 RYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNIQLTYRVQR--LQKKLEDQNRENHGLVEKLTSLAALRVGDLEKV 926
Cdd:pfam15921 268 RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNsmYMRQLSDLESTVSQLRSELREAKRMYEDKIEEL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 927 QK----LEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQmLQEKSEELKEKMDKLTRQLfDDVQ 1002
Cdd:pfam15921 348 EKqlvlANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKR-LWDRDTGNSITIDHLRREL-DDRN 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1003 KEEQQRLVLEKGFELKTQA-YEKQIESLREEIKALkDERSQLHHQLEEgqvTSDRLKGEVARLSKQAKTISEFEKEIEll 1081
Cdd:pfam15921 426 MEVQRLEALLKAMKSECQGqMERQMAAIQGKNESL-EKVSSLTAQLES---TKEMLRKVVEELTAKKMTLESSERTVS-- 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1082 qaqkiDVEKHVQSQKREMRERMSEVTKqllesydiedVRSR--LSVEDLEHLNEDGE-----------LWFAYEGLKKAT 1148
Cdd:pfam15921 500 -----DLTASLQEKERAIEATNAEITK----------LRSRvdLKLQELQHLKNEGDhlrnvqteceaLKLQMAEKDKVI 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1149 RVLESH-----------------FQSQKDCYEKEI-----EGLNFKVV---------HLSQEINHLQ------------- 1184
Cdd:pfam15921 565 EILRQQienmtqlvgqhgrtagaMQVEKAQLEKEIndrrlELQEFKILkdkkdakirELEARVSDLElekvklvnagser 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1185 ----KLFREETD--INE--SIRHEVTRLTSE-NMMIPDFKQQISELERQKQDLESRLKEQAEKIEgkleepfSHLNRIRE 1255
Cdd:pfam15921 645 lravKDIKQERDqlLNEvkTSRNELNSLSEDyEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELE-------QTRNTLKS 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1256 EERMQGRAVEAQSEMHPE-----GK-ERLVGAIHEPHEAIKFPKKQPEAEEEVESILQQEASRLSLEKRDLEEELDMKDR 1329
Cdd:pfam15921 718 MEGSDGHAMKVAMGMQKQitakrGQiDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRS 797
|
570 580
....*....|....*....|
gi 124486759 1330 MIRRLQDQVKTLTKTTEKAN 1349
Cdd:pfam15921 798 QERRLKEKVANMEVALDKAS 817
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
947-1345 |
1.58e-14 |
|
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: 79.72 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 947 GRRYRDTVEERLSKLQKHN--AELELQRERAEQMLQEKSEELKEkmdklTRQLFDDVQKEEQQRLVLEKGFELKTQAYEK 1024
Cdd:TIGR02168 659 GVITGGSAKTNSSILERRReiEELEEKIEELEEKIAELEKALAE-----LRKELEELEEELEQLRKELEELSRQISALRK 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1025 QIESLREEIKALKDERSQLHHQLEEGQvtsDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMS 1104
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQLSKELTELE---AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1105 EVTkqlLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLEShfqsqkdcYEKEIEGLNFKVVHLSQEINHLQ 1184
Cdd:TIGR02168 811 ELT---LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES--------LAAEIEELEELIEELESELEALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1185 KLFREETDINESIRHEVTRLTSEnmmIPDFKQQISELERQKQDLESRLKEQAEKIEGkLEEPFSHLN-RIREEERMQGRA 1263
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEE---LRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQeRLSEEYSLTLEE 955
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1264 VEAQSEMHPEGKERLVGAIHEPHEAIK-FPKKQPEAEEEVESiLQQEASRLSLEKRDLEEELDMKDRMIRRLQDQVKTLT 1342
Cdd:TIGR02168 956 AEALENKIEDDEEEARRRLKRLENKIKeLGPVNLAAIEEYEE-LKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERF 1034
|
...
gi 124486759 1343 KTT 1345
Cdd:TIGR02168 1035 KDT 1037
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
862-1383 |
2.38e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.95 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 862 LQKYARAW--------LARRRFQNIRRFvlnIQLTYRVQRL----QKKLEDQNRENHGLVEKLTSLAalrvgdlEKVQKL 929
Cdd:PRK03918 157 LDDYENAYknlgevikEIKRRIERLEKF---IKRTENIEELikekEKELEEVLREINEISSELPELR-------EELEKL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 930 EAELEKAATHRHSYEEKgrryrdtvEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRqlFDDVQKEEQQRL 1009
Cdd:PRK03918 227 EKEVKELEELKEEIEEL--------EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE--LKELKEKAEEYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1010 VLEK---GFELKTQAYEKQIESLREEIKALKDersqlhhQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKI 1086
Cdd:PRK03918 297 KLSEfyeEYLDELREIEKRLSRLEEEINGIEE-------RIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKA 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1087 DVEKHVQSQKREMRERMSEVTKQLLE----SYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVL--------ESH 1154
Cdd:PRK03918 370 KKEELERLKKRLTGLTPEKLEKELEElekaKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgreltEEH 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1155 FQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREEtdinESIRHEVTRLTSENMMIPDFKQ--------QISELERQKQ 1226
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELKEIEEKERKLRKELREL----EKVLKKESELIKLKELAEQLKEleeklkkyNLEELEKKAE 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1227 DLEsRLKEQAEKIEGKLEEPFSHLNRI-------REEERMQGRAVEAQSEMHPEGKERLVGAIHEPHEAIK----FPKKQ 1295
Cdd:PRK03918 526 EYE-KLKEKLIKLKGEIKSLKKELEKLeelkkklAELEKKLDELEEELAELLKELEELGFESVEELEERLKelepFYNEY 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1296 PEAeEEVESILQQEASRLSLEKRDLE---EELDMKDRMIRRLQDQVKTLTKTTEKANHVHLP----SGSREYLGMLEYKK 1368
Cdd:PRK03918 605 LEL-KDAEKELEREEKELKKLEEELDkafEELAETEKRLEELRKELEELEKKYSEEEYEELReeylELSRELAGLRAELE 683
|
570
....*....|....*
gi 124486759 1369 EDEgKLIQNLILDLK 1383
Cdd:PRK03918 684 ELE-KRREEIKKTLE 697
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
922-1262 |
3.91e-14 |
|
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: 78.17 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 922 DLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEE-----------RLSKLQKHNAELELQRERAEQMLQEKSEELKEKM 990
Cdd:TIGR02168 187 NLDRLEDILNELERQLKSLERQAEKAERYKELKAElrelelallvlRLEELREELEELQEELKEAEEELEELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 991 DKLTRQLFDDVQKEEQQRLVLEKGFELKT--QAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQa 1068
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANeiSRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1069 ktISEFEKEIELLQAQkidvEKHVQSQKREMRERMSEVTKQLlesydiEDVRSRLSvedlehlnedgelwfayeGLKKAT 1148
Cdd:TIGR02168 346 --LEELKEELESLEAE----LEELEAELEELESRLEELEEQL------ETLRSKVA------------------QLELQI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1149 RVLESHFQSqkdcYEKEIEGLNFKVVHLSQEINHLQKLFrEETDINESIRhevtRLTSENMMIPDFKQQISELERQKQDL 1228
Cdd:TIGR02168 396 ASLNNEIER----LEARLERLEDRRERLQQEIEELLKKL-EEAELKELQA----ELEELEEELEELQEELERLEEALEEL 466
|
330 340 350
....*....|....*....|....*....|....
gi 124486759 1229 ESRLKEQAEKIEGKLEEPFSHLNRIREEERMQGR 1262
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
895-1374 |
5.60e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 77.39 E-value: 5.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 895 QKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYR------DTVEERLSKLQKHNAEL 968
Cdd:PRK02224 191 QLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEerreelETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 969 ELQRERAEQMLQEKSEELKEKMDKLTRQL----FDDVQKE--EQQRLVLEKGFE----------LKTQAYEKQIESLREE 1032
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDLLaeagLDDADAEavEARREELEDRDEelrdrleecrVAAQAHNEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1033 IKALKDERSQLHhqlEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVE---KHVQSQKREMRERMSEVTKQ 1109
Cdd:PRK02224 351 ADDLEERAEELR---EEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPvdlGNAEDFLEELREERDELRER 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1110 LLE-SYDIEDVRSRlsVEDLEHLNEDG---ELWFAYEGLKKATRVLEShfQSQKDCYEKEIEGLNFKVVHLSQEINHLQK 1185
Cdd:PRK02224 428 EAElEATLRTARER--VEEAEALLEAGkcpECGQPVEGSPHVETIEED--RERVEELEAELEDLEEEVEEVEERLERAED 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1186 LFREETdinesirhevtrltsenmmipdfkqQISELERQKQDLESRLKEQAEKIEGKLEEpfshlnriREEERMQGRAVE 1265
Cdd:PRK02224 504 LVEAED-------------------------RIERLEERREDLEELIAERRETIEEKRER--------AEELRERAAELE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1266 AQSEMHPEGKERLVGAIHEPHEAIK-FPKKQPEAEEEVEsilqqeasrlSLEK-RDLEEELDMKDRMIRRLQDQVKTLTK 1343
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEAREEVAeLNSKLAELKERIE----------SLERiRTLLAAIADAEDEIERLREKREALAE 620
|
490 500 510
....*....|....*....|....*....|..
gi 124486759 1344 TTEKanhvhlpsgSREYLGML-EYKKEDEGKL 1374
Cdd:PRK02224 621 LNDE---------RRERLAEKrERKRELEAEF 643
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
893-1240 |
7.56e-14 |
|
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: 77.40 E-value: 7.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 893 RLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVE---ERLSKLQKHNAELE 969
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 970 LQRERAEQMLQEKSEELKEkmdkltrqlfDDVQKEEQQRLVlekgfelktQAYEKQIESLREEIKALKDERSQLHhqlEE 1049
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAE----------AEAEIEELEAQI---------EQLKEELKALREALDELRAELTLLN---EE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1050 GQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEkHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVEDLE 1129
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA-AEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1130 HLNEDGElwfAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEIN--------HLQKLFREETDINESIRHEV 1201
Cdd:TIGR02168 898 ELSEELR---ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeeysltleEAEALENKIEDDEEEARRRL 974
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 124486759 1202 TRLTSE-------NMM-IPDFKQQ---ISELERQKQDLESRLKEQAEKIE 1240
Cdd:TIGR02168 975 KRLENKikelgpvNLAaIEEYEELkerYDFLTAQKEDLTEAKETLEEAIE 1024
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
874-1198 |
1.00e-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: 77.02 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 874 RFQNIRRFVLNIQL---TYRVQRLQKKLEDQNRENHGLVEKLTSLAAlrvgdleKVQKLEAELEkaaTHRHSYEEkgrry 950
Cdd:TIGR02168 214 RYKELKAELRELELallVLRLEELREELEELQEELKEAEEELEELTA-------ELQELEEKLE---ELRLEVSE----- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 951 rdtVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLtRQLFDDVQKEEQQRLVLEKGFELKTQAYE---KQIE 1027
Cdd:TIGR02168 279 ---LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL-EELEAQLEELESKLDELAEELAELEEKLEelkEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1028 SLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISefeKEIELLQAQKIDVEKHVQSQKREMRERMSEvt 1107
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN---NEIERLEARLERLEDRRERLQQEIEELLKK-- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1108 kqlLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKAtrvleshfQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLF 1187
Cdd:TIGR02168 430 ---LEEAELKELQAELEELEEELEELQEELERLEEALEEL--------REELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
330
....*....|.
gi 124486759 1188 REETDINESIR 1198
Cdd:TIGR02168 499 ENLEGFSEGVK 509
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
988-1383 |
1.12e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.64 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 988 EKMDKLTRQL--FDDVQKEEQQRLVLEKGFELKTQAYEKQI---ESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVA 1062
Cdd:PRK03918 145 ESREKVVRQIlgLDDYENAYKNLGEVIKEIKRRIERLEKFIkrtENIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1063 RLSKQAKTISEFEKEIELLQAQKIDVEKHVQS---QKREMRERMSEVTKQllesydIEDVRSRlsVEDLEHLNEDGELWF 1139
Cdd:PRK03918 225 KLEKEVKELEELKEEIEELEKELESLEGSKRKleeKIRELEERIEELKKE------IEELEEK--VKELKELKEKAEEYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1140 AYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREEtdinESIRHEVTRLTSENMMIPDFKQQIS 1219
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL----KELEKRLEELEERHELYEEAKAKKE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1220 ELERQKQDLESRLKEQAEK-----------IEGKLEEPFSHLNRIREEERMQGRAVEAQSEmhPEGKERLVGA-IHEPHE 1287
Cdd:PRK03918 373 ELERLKKRLTGLTPEKLEKeleelekakeeIEEEISKITARIGELKKEIKELKKAIEELKK--AKGKCPVCGReLTEEHR 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1288 A---IKFPKKQPEAEEEVESILQQEaSRLSLEKRDLEEELDMKDRMI--RRLQDQVKTLTKTTEKANHVHLPSGSREYLG 1362
Cdd:PRK03918 451 KellEEYTAELKRIEKELKEIEEKE-RKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEELEKKAEEYEK 529
|
410 420
....*....|....*....|.
gi 124486759 1363 MLEYKKEDEGKlIQNLILDLK 1383
Cdd:PRK03918 530 LKEKLIKLKGE-IKSLKKELE 549
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
945-1269 |
3.63e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.10 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 945 EKGRRYRDTVEERLSKLQKHNAELELQRERaeqmLQEKSEElKEKMDKLTRQLfddvQKEEQQRLVLEK-GFELKTQAYE 1023
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLER----LRREREK-AERYQALLKEK----REYEGYELLKEKeALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1024 KQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQA-----KTISEFEKEIELLQAQKIDVEKHVQSQKRE 1098
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrvkEKIGELEAEIASLERSIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1099 MRERMSEVTKQLLESYDIEdvrsrlsvEDLEHLNEDGELWFA-YEGLKKATRVLESH-----------FQSQKDcYEKEI 1166
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELE--------REIEEERKRRDKLTEeYAELKEELEDLRAEleevdkefaetRDELKD-YREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1167 EGLNfkvvhlsQEINHLQKLFREETDINESIRHEVTRLtseNMMIPDFKQQISELERQKQDLESRLKEQAEKIE---GKL 1243
Cdd:TIGR02169 395 EKLK-------REINELKRELDRLQEELQRLSEELADL---NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEqlaADL 464
|
330 340
....*....|....*....|....*..
gi 124486759 1244 EEPFSHLNRIREE-ERMQGRAVEAQSE 1269
Cdd:TIGR02169 465 SKYEQELYDLKEEyDRVEKELSKLQRE 491
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
896-1338 |
4.05e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 74.69 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 896 KKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERA 975
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 976 EQmLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEkgfelktqAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSD 1055
Cdd:PRK02224 352 DD-LEERAEELREEAAELESELEEAREAVEDRREEIE--------ELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1056 RLKGEVARLSKQAKTISE-FEKEIELLQA-------QKIDVEKHVQSQKrEMRERMSEVTKQLLesyDIEDVRSRLSvED 1127
Cdd:PRK02224 423 ELREREAELEATLRTARErVEEAEALLEAgkcpecgQPVEGSPHVETIE-EDRERVEELEAELE---DLEEEVEEVE-ER 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1128 LEHLnedgelwfayEGLKKAtrvleshfqsqkdcyEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTSE 1207
Cdd:PRK02224 498 LERA----------EDLVEA---------------EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1208 nmmIPDFKQQISELERQKQD-------LESRLKEQAEKIEG--KLEEPFSHLNRIREE-ERMQGRaVEAQSEMHPEGKER 1277
Cdd:PRK02224 553 ---AEEKREAAAEAEEEAEEareevaeLNSKLAELKERIESleRIRTLLAAIADAEDEiERLREK-REALAELNDERRER 628
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486759 1278 LvgaihephEAIKFPKKQPEAEEEVESI--LQQEASRLSLEKRDLEEELDMKDRMIRRLQDQV 1338
Cdd:PRK02224 629 L--------AEKRERKRELEAEFDEARIeeAREDKERAEEYLEQVEEKLDELREERDDLQAEI 683
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
891-1348 |
1.38e-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: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 891 VQRLQKKLEDQNRENHglveklTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEE---RLSKLQKHNAE 967
Cdd:pfam01576 329 VTELKKALEEETRSHE------AQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAElqaELRTLQQAKQD 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 968 LELQRERAEQMLQE----------KSEELKEKMDKLTRQLfDDV----QKEEQQRLVLEKGF-ELKTQAYEKQiESLREE 1032
Cdd:pfam01576 403 SEHKRKKLEGQLQElqarlseserQRAELAEKLSKLQSEL-ESVssllNEAEGKNIKLSKDVsSLESQLQDTQ-ELLQEE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1033 ----------IKALKDERSQLHHQLEEGQVTSDRLKGEV----ARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKRE 1098
Cdd:pfam01576 481 trqklnlstrLRQLEDERNSLQEQLEEEEEAKRNVERQLstlqAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1099 MRERMSEVTK---------QLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEglkkatRVLESHFQSQKDCYEKEIEGL 1169
Cdd:pfam01576 561 LEEKAAAYDKlektknrlqQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEE------KAISARYAEERDRAEAEAREK 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1170 NFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTSENmmiPDFKQQISELERQKQDLESR---LKEQAEKIEGKLEEp 1246
Cdd:pfam01576 635 ETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSK---DDVGKNVHELERSKRALEQQveeMKTQLEELEDELQA- 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1247 fSHLNRIREEERMQG------RAVEAQSEMHPEGKERLVGAIHEpHEAikfpkkqpEAEEEVESILQQEASR--LSLEKR 1318
Cdd:pfam01576 711 -TEDAKLRLEVNMQAlkaqfeRDLQARDEQGEEKRRQLVKQVRE-LEA--------ELEDERKQRAQAVAAKkkLELDLK 780
|
490 500 510
....*....|....*....|....*....|....*..
gi 124486759 1319 DLEEELDMKDR-------MIRRLQDQVKTLTKTTEKA 1348
Cdd:pfam01576 781 ELEAQIDAANKgreeavkQLKKLQAQMKDLQRELEEA 817
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
890-1376 |
2.23e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.87 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 890 RVQRLQKKLEDQNRenhglVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELE 969
Cdd:PTZ00121 1303 KADEAKKKAEEAKK-----ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 970 LQRERAEQMLQE--KSEELKEKMDKLTRQLfDDVQKEEQQRlvlEKGFELKTQAYEKQIEslrEEIKALKDER---SQLH 1044
Cdd:PTZ00121 1378 KKADAAKKKAEEkkKADEAKKKAEEDKKKA-DELKKAAAAK---KKADEAKKKAEEKKKA---DEAKKKAEEAkkaDEAK 1450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1045 HQLEEGQVTSDRLKG--------EVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDI 1116
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKaeeakkadEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1117 EDVRSRLSVEDLEHLNEDGELWFAYEgLKKATRVLESHfQSQKDCYEKEIEGLNFKVVHLSQE--INHLQKLFREETDIN 1194
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKAEE-LKKAEEKKKAE-EAKKAEEDKNMALRKAEEAKKAEEarIEEVMKLYEEEKKMK 1608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1195 --ESIRHEVTRLTSENMMIPDFKQQISELERQKQDLESRLKEQAEKIEGKLEEPFSHLNRIREEERMQGRAVEAQSEMHP 1272
Cdd:PTZ00121 1609 aeEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1273 EGKERLVGAIHEPHEAIKFPKKQPE---------AEEEVESILQQEASRLSLEKRDLEEELDMKDRMIRRLQDQVKTLTK 1343
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEekkkaeelkKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
|
490 500 510
....*....|....*....|....*....|...
gi 124486759 1344 TTEKANHvhlpsgSREYLGMLEYKKEDEGKLIQ 1376
Cdd:PTZ00121 1769 KAEEIRK------EKEAVIEEELDEEDEKRRME 1795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
922-1332 |
4.00e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 71.64 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 922 DLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQM------LQEKSEELKEKMDKLTR 995
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLeqeeekLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 996 QLFDDvqKEEQQRLvlekgfELKTQAYEKQIESLREEIKALkdERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFE 1075
Cdd:TIGR02169 752 EIENV--KSELKEL------EARIEELEEDLHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1076 KEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQllesydIEDVRSRLsvEDLEhlnedgelwfayEGLKKatrvleshf 1155
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE------IENLNGKK--EELE------------EELEE--------- 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1156 qsqkdcYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLtsenmmipdfKQQISELERQKQDLESRLKEQ 1235
Cdd:TIGR02169 873 ------LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK----------RKRLSELKAKLEALEEELSEI 936
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1236 AEKIEGKLEEPfshlnrireEERMQGRAVEAQSEMHPEGKERLvgaihephEAIKFpkKQPEAEEEVE---SILQQEASR 1312
Cdd:TIGR02169 937 EDPKGEDEEIP---------EEELSLEDVQAELQRVEEEIRAL--------EPVNM--LAIQEYEEVLkrlDELKEKRAK 997
|
410 420
....*....|....*....|
gi 124486759 1313 LSLEKRDLEEELDMKDRMIR 1332
Cdd:TIGR02169 998 LEEERKAILERIEEYEKKKR 1017
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
848-1337 |
7.94e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 7.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 848 RRYRKLLQEHKavilQKYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRV---GDLE 924
Cdd:COG1196 213 ERYRELKEELK----ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELeleEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 925 KVQKLEAELEKAATHRHSYEEKGRRYRDTVEE----------RLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLT 994
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEEleeelaeleeELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 995 RQLFDDVQKEEQQRLVLEKGFELKTQAYE--KQIESLREEIKALKDERSQLHHQLEEGQvtsDRLKGEVARLSKQAKTIS 1072
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAElaAQLEELEEAEEALLERLERLEEELEELE---EALAELEEEEEEEEEALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1073 EFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTkQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLE 1152
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALA-ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1153 SHFQSQKDCYEKEieglnfKVVHLSQEINHLQKLFREETDINESIRHE-------VTRLTSENMMIPDFKQQISELERQK 1225
Cdd:COG1196 525 AVAVLIGVEAAYE------AALEAALAAALQNIVVEDDEVAAAAIEYLkaakagrATFLPLDKIRARAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1226 QDLESRLKEQAEKIEGKLEEPFSHLNRIREEERMQGRAVEAQSEMHPEGKERLVGAIHEPHEAIK--FPKKQPEAEEEVE 1303
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTggSRRELLAALLEAE 678
|
490 500 510
....*....|....*....|....*....|....
gi 124486759 1304 SILQQEASRLSLEKRDLEEELDMKDRMIRRLQDQ 1337
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEA 712
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
923-1354 |
1.21e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.80 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 923 LEKVQKLEAELEKAATHRHSYEEKgRRYRDTVEERLSKLQKHNAELELQRERAEQMLQekSEELKEKMDKLTRQLfddvq 1002
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQ--LLPLYQELEALEAEL----- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1003 KEEQQRLVlekgfelKTQAYEKQIESLREEIKALKDERSQLHHQLEE-----GQVTSDRLKGEVARLSKQAKTISEFEKE 1077
Cdd:COG4717 142 AELPERLE-------ELEERLEELRELEEELEELEAELAELQEELEElleqlSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1078 IELLQAQKIDVEKHVQSQKREM-RERMSEVTKQLLESYDIEDVRSRLSVEDLEHLN---EDGELWFAYEGLkkaTRVLES 1153
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELeAAALEERLKEARLLLLIAAALLALLGLGGSLLSlilTIAGVLFLVLGL---LALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1154 HFQSQKDCYEKEIEGLNfKVVHLSQEINHLQKLFREETDINESIrhEVTRLTSENMMIPDFKQQISELERQKQDL--ESR 1231
Cdd:COG4717 292 LLAREKASLGKEAEELQ-ALPALEELEEEELEELLAALGLPPDL--SPEELLELLDRIEELQELLREAEELEEELqlEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1232 LKEQAEKIE----GKLEEPFSHLNRIREEERMQGRAVEAQSEMHPEGKERLVGAIHEPHEAIK-----FPKKQPEAEEEV 1302
Cdd:COG4717 369 EQEIAALLAeagvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEeeleeLEEELEELEEEL 448
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124486759 1303 ESILQQEA---------------SRLSLEKRDLEEELDMKDRMIRRLQDQVKTLTKTTEKANHVHLP 1354
Cdd:COG4717 449 EELREELAeleaeleqleedgelAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLP 515
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
891-1342 |
1.26e-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: 66.74 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 891 VQRLQKKLEDQNREnhgLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQkhNAELEL 970
Cdd:pfam01576 403 SEHKRKKLEGQLQE---LQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQ--DTQELL 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 971 QRE---------RAEQM------LQEKSEELKEKMDKLTR-------QLFDDVQKEEQQRLVLEKG-------------- 1014
Cdd:pfam01576 478 QEEtrqklnlstRLRQLedernsLQEQLEEEEEAKRNVERqlstlqaQLSDMKKKLEEDAGTLEALeegkkrlqreleal 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1015 ---FELKTQAY---EKQIESLREEIKAL---KDERSQLHHQLEEGQVTSDRLKGEVARLS----------------KQAK 1069
Cdd:pfam01576 558 tqqLEEKAAAYdklEKTKNRLQQELDDLlvdLDHQRQLVSNLEKKQKKFDQMLAEEKAISaryaeerdraeaeareKETR 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1070 TISeFEKEIELLQAQKIDVEKHVQSQKREMRERMS------------EVTKQLLESyDIEDVRSRLS-VEDLEHLNEDGE 1136
Cdd:pfam01576 638 ALS-LARALEEALEAKEELERTNKQLRAEMEDLVSskddvgknvhelERSKRALEQ-QVEEMKTQLEeLEDELQATEDAK 715
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1137 LwfayeglkkatrVLESHFQSQKDCYEKEIEGLNFKVvhlSQEINHLQKLFRE-ETDINESIRHEVTRLTSENMMIPDFK 1215
Cdd:pfam01576 716 L------------RLEVNMQALKAQFERDLQARDEQG---EEKRRQLVKQVRElEAELEDERKQRAQAVAAKKKLELDLK 780
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1216 qqisELERQkQDLESRLKEQAEKIEGKLEEPFSHLNRIREEERMQGRAVEAQS---EMHPEGKERLVGAIHEPHEAIKFP 1292
Cdd:pfam01576 781 ----ELEAQ-IDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSkesEKKLKNLEAELLQLQEDLAASERA 855
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486759 1293 KKQPEAE-----EEV------ESILQQEASRLSLEKRDLEEELD--------MKDRMiRRLQDQVKTLT 1342
Cdd:pfam01576 856 RRQAQQErdelaDEIasgasgKSALQDEKRRLEARIAQLEEELEeeqsntelLNDRL-RKSTLQVEQLT 923
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
960-1326 |
2.81e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 960 KLQKHNAELELQR-----ERAEQMLqeksEELKEKMDKLtrqlfddvqkeEQQRLVLEKGFELKTQAYEKQIESLREEIK 1034
Cdd:COG1196 171 KERKEEAERKLEAteenlERLEDIL----GELERQLEPL-----------ERQAEKAERYRELKEELKELEAELLLLKLR 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1035 ALKDERSQLHHQLEEGQvtsdrlkgevARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTkQLLESY 1114
Cdd:COG1196 236 ELEAELEELEAELEELE----------AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA-RLEQDI 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1115 DIEDVRSRLSVEDLEHLNEDGELWfaYEGLKKATRVLESHFQSQKDcYEKEIEGLNfkvVHLSQEINHLQKLFREETDIN 1194
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAEL--EEELEELEEELEELEEELEE-AEEELEEAE---AELAEAEEALLEAEAELAEAE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1195 ESIRHEVTRLTSENMMIPDFKQQISELERQKQDLESRLKEQAEKIEGKLEEPFSHLNRIREEERMQGRAVEAQSEmhpeg 1274
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE----- 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 124486759 1275 KERLVGAIHEPHEAIKfpKKQPEAEEEVESILQQEASRLSLEKRDLEEELDM 1326
Cdd:COG1196 454 LEEEEEALLELLAELL--EEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| Myo5p-like_CBD_afadin |
cd15471 |
cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and ... |
1396-1700 |
5.97e-10 |
|
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: 62.71 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1396 PAHILFMCVRYADSLND---------ANMLKSLMNSAINGIKHVVKEHFEDLEMLSFWLSNTCHFLNCLKQysgeeefmk 1466
Cdd:cd15471 25 PAYTLYLAARYRLSTHYrpeltpterAHKLTAFLNKIASLIQQVIQEQRNIAGALAFWMANASELLNFLKQ--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1467 ynspqqnknclnNFDLTEYR----QILSDVAIRIYHQFIIVMENNLQPIIVPGMLEYESLQGISGlkptgfrkrsssIDD 1542
Cdd:cd15471 96 ------------DRDLSAFSvqaqDVLAEAVQSAFSYLVRCLQEELERSLPAFLDSLVSLDDEPA------------IGD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1543 TdaytmtsiLQQLSYFYSTMCQNGLDPEIVRQAVKQLFYLVGAVTLNSLLLRKD--MCSCRKGMQIRCNISFLEEWLKDK 1620
Cdd:cd15471 152 V--------LHTLSSAMRLLRRCRVNAALTIQLFSQLFHFINAWLFNSLVSNPDsgLCTRYWGKRLRQRLAHVEAWAERQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1621 NVQssLAKET-LEPLSQAAWLLQVKKTTDSDAKEIAQCCTSLSAVQIIKILNSYTPiDDFEKRVNPSFVRKVQALLNNRG 1699
Cdd:cd15471 224 GLE--LAADChLDRIVQAANLLTAPKYSAEDVANLSSTCFKLNSLQLRALLSHYQP-PPGEPPIPPDLIERVVRLAESQA 300
|
.
gi 124486759 1700 D 1700
Cdd:cd15471 301 D 301
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
866-1253 |
6.43e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.55 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 866 ARAWLARRRFQniRRFVlniqlTYRVQRLQKKLEDQNRENHGLVEKLTS--------LAAL--RVGDLEKVQKLEaELE- 934
Cdd:COG4913 501 ALRWVNRLHLR--GRLV-----YERVRTGLPDPERPRLDPDSLAGKLDFkphpfrawLEAElgRRFDYVCVDSPE-ELRr 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 935 --KAAT------HRHSYEEKGRRYRdtVEERL-------SKLQkhnaelELQRERAEqmLQEKSEELKEKMDKLTRQLFD 999
Cdd:COG4913 573 hpRAITragqvkGNGTRHEKDDRRR--IRSRYvlgfdnrAKLA------ALEAELAE--LEEELAEAEERLEALEAELDA 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1000 DVQKEEQQRLVLEKGFElktqayEKQIESLREEIKALKDERSQLhhqleegqvtsDRLKGEVARLskqaktisefEKEIE 1079
Cdd:COG4913 643 LQERREALQRLAEYSWD------EIDVASAEREIAELEAELERL-----------DASSDDLAAL----------EEQLE 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1080 LLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQK 1159
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERI 775
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1160 DCYEKEIEGLNFKVVHLSQEINHLQKLFREETDI----NESIRHEVTRLTSENmmIPDFKQQISEL-----ERQKQDLES 1230
Cdd:COG4913 776 DALRARLNRAEEELERAMRAFNREWPAETADLDAdlesLPEYLALLDRLEEDG--LPEYEERFKELlnensIEFVADLLS 853
|
410 420
....*....|....*....|...
gi 124486759 1231 RLKEQAEKIEGKLEEpfshLNRI 1253
Cdd:COG4913 854 KLRRAIREIKERIDP----LNDS 872
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
923-1115 |
9.38e-10 |
|
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: 60.71 E-value: 9.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 923 LEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELE-LQRERAEqmLQEKSEELKEKMDKLTRQLfDDV 1001
Cdd:COG1579 9 LLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEdLEKEIKR--LELEIEEVEARIKKYEEQL-GNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1002 QKEEQQrlvlekgfelktQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQ-AKTISEFEKEIEL 1080
Cdd:COG1579 86 RNNKEY------------EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAElEEKKAELDEELAE 153
|
170 180 190
....*....|....*....|....*....|....*
gi 124486759 1081 LQAQkidvEKHVQSQKREMRERMSEvtkQLLESYD 1115
Cdd:COG1579 154 LEAE----LEELEAEREELAAKIPP---ELLALYE 181
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
887-1336 |
1.45e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.16 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 887 LTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDT---VEERLSKLQK 963
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEydrVEKELSKLQR 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 964 HNAELELQRE---------RAEQMLQEKS---------------------------------------------EELKE- 988
Cdd:TIGR02169 491 ELAEAEAQARaseervrggRAVEEVLKASiqgvhgtvaqlgsvgeryataievaagnrlnnvvveddavakeaiELLKRr 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 989 -----------KMDKLTRQL-----------------FDD---------------VQKEE-------QQRLV------LE 1012
Cdd:TIGR02169 571 kagratflplnKMRDERRDLsilsedgvigfavdlveFDPkyepafkyvfgdtlvVEDIEaarrlmgKYRMVtlegelFE 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1013 K------------GFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQaktISEFEKEIEL 1080
Cdd:TIGR02169 651 KsgamtggsraprGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK---IGEIEKEIEQ 727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1081 LQAQkidvEKHVQSQKREMRERMSEvTKQLLESYD--IEDVRSRLS------------VEDLEHlNEDGELWFAYEGLKK 1146
Cdd:TIGR02169 728 LEQE----EEKLKERLEELEEDLSS-LEQEIENVKseLKELEARIEeleedlhkleeaLNDLEA-RLSHSRIPEIQAELS 801
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1147 ATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLtseNMMIPDFKQQISELERQKQ 1226
Cdd:TIGR02169 802 KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL---NGKKEELEEELEELEAALR 878
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1227 DLESRLKEqaekIEGKLEEPFSHLNRIREEERMQGRAVEAQSEMHPEGKERLvGAIHEPHEAIKFPKKQPEAEEEVESIL 1306
Cdd:TIGR02169 879 DLESRLGD----LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL-EALEEELSEIEDPKGEDEEIPEEELSL 953
|
570 580 590
....*....|....*....|....*....|
gi 124486759 1307 qqeasrlslekRDLEEELDMKDRMIRRLQD 1336
Cdd:TIGR02169 954 -----------EDVQAELQRVEEEIRALEP 972
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
849-1185 |
1.77e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.16 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 849 RYRKLLQEhkaviLQKYaRAWLARRRFQNIRRfvlniqltyRVQRLQKKLEDQNREnhglVEKLTslaalrvgdlEKVQK 928
Cdd:TIGR02169 212 RYQALLKE-----KREY-EGYELLKEKEALER---------QKEAIERQLASLEEE----LEKLT----------EEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 929 LEAELEKAATHRhsyEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELkEKMDKLTRQLFDDVQKEEQQR 1008
Cdd:TIGR02169 263 LEKRLEEIEQLL---EELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL-EDAEERLAKLEAEIDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1009 LVLEKgfelKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVarlskqaktiSEFEKEIELLQaQKIDV 1088
Cdd:TIGR02169 339 EELER----EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL----------KDYREKLEKLK-REINE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1089 EKHVQSQKREMRERMSEvtkqllesyDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLEShFQSQKDCYEKEIEG 1168
Cdd:TIGR02169 404 LKRELDRLQEELQRLSE---------ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ-LAADLSKYEQELYD 473
|
330
....*....|....*..
gi 124486759 1169 LNFKVVHLSQEINHLQK 1185
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQR 490
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
886-1343 |
2.81e-09 |
|
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: 62.44 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 886 QLTYRVQRLQKKLEDQNRenhgLVEKLTSLAALRVGDLE-KVQKLEAELEKAATHRhsyeekgRRYRDTVEERLSKLQKH 964
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNE----LHEKQKFYLRQSVIDLQtKLQEMQMERDAMADIR-------RRESQSQEDLRNQLQNT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 965 NAELELQRERAEQMLQEKSEELkekmDKLTRQLF--DDVQKEEQQRLVlekGFElktQAYEKQIESlreeikalKDERSQ 1042
Cdd:pfam15921 151 VHELEAAKCLKEDMLEDSNTQI----EQLRKMMLshEGVLQEIRSILV---DFE---EASGKKIYE--------HDSMST 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1043 LHHQ---------LEEGQVTSDRLKGEVARLSKQAKTI-SEFEKEIELLQAQKID-VEKHVQSQKRE---MRERMSEVTK 1108
Cdd:pfam15921 213 MHFRslgsaiskiLRELDTEISYLKGRIFPVEDQLEALkSESQNKIELLLQQHQDrIEQLISEHEVEitgLTEKASSARS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1109 QllesydIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVV-------------- 1174
Cdd:pfam15921 293 Q------ANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVlanseltearterd 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1175 HLSQEI----NHLQKLF----REETDIN---ESIRHEVTRLTSENMMIPDFKQQISELERQKQDLESRLK---------- 1233
Cdd:pfam15921 367 QFSQESgnldDQLQKLLadlhKREKELSlekEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKamksecqgqm 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1234 -EQAEKIEGK---LEEPFSHLNRIREEERMQGRAVE--AQSEMHPEGKER----LVGAIHEPHEAIKFPKKQPEAEEEVE 1303
Cdd:pfam15921 447 eRQMAAIQGKnesLEKVSSLTAQLESTKEMLRKVVEelTAKKMTLESSERtvsdLTASLQEKERAIEATNAEITKLRSRV 526
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 124486759 1304 SILQQEASRLSLEK---RDLEEELDM-------KDRMIRRLQDQVKTLTK 1343
Cdd:pfam15921 527 DLKLQELQHLKNEGdhlRNVQTECEAlklqmaeKDKVIEILRQQIENMTQ 576
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
894-1340 |
3.53e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.57 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 894 LQKKLEDQNRENHGLVEKLTSLAalrvgdlEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELElQRE 973
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQ-------QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIK-ELE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 974 RAEQMLQEKSEELK-EKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEK---QIESLREEIKALKDERSQLHHQLEE 1049
Cdd:TIGR04523 288 KQLNQLKSEISDLNnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQlneQISQLKKELTNSESENSEKQRELEE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1050 GQVTSDRLKGEvarlskqaktISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVE--- 1126
Cdd:TIGR04523 368 KQNEIEKLKKE----------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETiik 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1127 ------DLEhlNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHE 1200
Cdd:TIGR04523 438 nnseikDLT--NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1201 VTRLTSENMMIPDFKQQISELERQKQDLESRLKE-QAEKIEGKLEEPFSHLN-RIREEERMQGRAVEAQSEMHPEGKERL 1278
Cdd:TIGR04523 516 TKKISSLKEKIEKLESEKKEKESKISDLEDELNKdDFELKKENLEKEIDEKNkEIEELKQTQKSLKKKQEEKQELIDQKE 595
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486759 1279 VGAIHEPHEAIKFPKKQPEAEEEVESIlQQEASRLSLEKRDLEEELDMKDRMIRRLQDQVKT 1340
Cdd:TIGR04523 596 KEKKDLIKEIEEKEKKISSLEKELEKA-KKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKE 656
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
872-1113 |
3.82e-09 |
|
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: 61.68 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 872 RRRFQNIRRFVLNIQLTyRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEE-KGRRY 950
Cdd:pfam17380 359 KRELERIRQEEIAMEIS-RMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEaRQREV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 951 RDTVEERLSKLQKHNAElELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYekqiesLR 1030
Cdd:pfam17380 438 RRLEEERAREMERVRLE-EQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAM------IE 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1031 EEIKalkdeRSQLHHQLEEGQVTsdrlkgeVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKR---EMRERMSEVT 1107
Cdd:pfam17380 511 EERK-----RKLLEKEMEERQKA-------IYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERsrlEAMEREREMM 578
|
....*.
gi 124486759 1108 KQLLES 1113
Cdd:pfam17380 579 RQIVES 584
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
898-1342 |
4.44e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 61.73 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 898 LEDQN----RENHGLVEKLTSLAALRVGDLEKV---QKLEAELEKAATH---RHSYEEKGRRYRDTVEERL----SKLQK 963
Cdd:pfam01576 143 LEDQNsklsKERKLLEERISEFTSNLAEEEEKAkslSKLKNKHEAMISDleeRLKKEEKGRQELEKAKRKLegesTDLQE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 964 HNAELELQRERAEQMLQEKSEELKEKMDKLTR------QLFDDVQKEEQQRLVLEKGFELKTQA---YEKQIESLREEIK 1034
Cdd:pfam01576 223 QIAELQAQIAELRAQLAKKEEELQAALARLEEetaqknNALKKIRELEAQISELQEDLESERAArnkAEKQRRDLGEELE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1035 ALKDErsqlhhqLEEGQVTSdrlkgevarlSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESY 1114
Cdd:pfam01576 303 ALKTE-------LEDTLDTT----------AAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1115 DiEDVRSRLSVEDLEHL--NEDGELWFAYEGLKKAT-------RVLESH---FQSQKDCYEKEIEGLNFKVVHLSQEINH 1182
Cdd:pfam01576 366 E-QAKRNKANLEKAKQAleSENAELQAELRTLQQAKqdsehkrKKLEGQlqeLQARLSESERQRAELAEKLSKLQSELES 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1183 LQKLFREETDINESIRHEVTRLTSEnmmIPDFKQQISELERQKQDLESRLKEqaekiegkLEEPFSHLNRIREEERMQGR 1262
Cdd:pfam01576 445 VSSLLNEAEGKNIKLSKDVSSLESQ---LQDTQELLQEETRQKLNLSTRLRQ--------LEDERNSLQEQLEEEEEAKR 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1263 AVEAQSEMHPEGKERLVGAIHEPHEAIkfpkkqpEAEEEVESILQQEASRLSLEKRDLEEELDMKDRMIRRLQDQVKTLT 1342
Cdd:pfam01576 514 NVERQLSTLQAQLSDMKKKLEEDAGTL-------EALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLL 586
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
944-1322 |
5.39e-09 |
|
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: 61.50 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 944 EEKGRRYRDT-VEERLSKLQKHNAELELQREraeqMLQEKSEEL----KEKMDKLTRQLFDDVQKEEQqrlvlEKG-FEL 1017
Cdd:pfam15818 15 ELRMRREAETqYEEQIGKIIVETQELKWQKE----TLQNQKETLakqhKEAMAVFKKQLQMKMCALEE-----EKGkYQL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1018 KTQAYEKQIESLREEIKALkdersqlhhqleegqvtsdrlkgEVARLSKQaKTISEFEKEIELLQAQKIDVEKhvqsQKR 1097
Cdd:pfam15818 86 ATEIKEKEIEGLKETLKAL-----------------------QVSKYSLQ-KKVSEMEQKLQLHLLAKEDHHK----QLN 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1098 EMRERMSEVTKQL---------LESYDIEDVR--SRLSVedlehLNE--DGELWFAYEGLKKATRVL-ESHFQSQkdcYE 1163
Cdd:pfam15818 138 EIEKYYATITGQFglvkenhgkLEQNVQEAIQlnKRLSA-----LNKkqESEICSLKKELKKVTSDLiKSKVTCQ---YK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1164 KEIEGLNFKVVHlsQEINHLQKLFREETDINESIRHEVTRLTSENMMIPDFKQQISELERQKQDLESRLKeqaekiegkl 1243
Cdd:pfam15818 210 MGEENINLTIKE--QKFQELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEME---------- 277
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486759 1244 eepfSHLNRIREEERMQGRAVEAQSEMHPEGKERLVGAIHEPHEAIKFPKKQPEAEEEVESILQQEASRLSLEKRDLEE 1322
Cdd:pfam15818 278 ----AELKALKENNQTLERDNELQREKVKENEEKFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQE 352
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
892-1350 |
5.82e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 61.14 E-value: 5.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 892 QRLQKKLEDQNRENHGLVEKLTslaalrvgDLEKVQKLEAELEKAathrhsyeeKGRRYRDTVEERLSKLQKHNAELELQ 971
Cdd:TIGR00618 246 TQKREAQEEQLKKQQLLKQLRA--------RIEELRAQEAVLEET---------QERINRARKAAPLAAHIKAVTQIEQQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 972 RERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLV--LEKGFELKTQAYEKQIESLREEIKALKDERS--QLHHQL 1047
Cdd:TIGR00618 309 AQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLqtLHSQEIHIRDAHEVATSIREISCQQHTLTQHihTLQQQK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1048 EEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKR--EMRERMSEVTKQLLESYDIEDVRSRLSV 1125
Cdd:TIGR00618 389 TTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRyaELCAAAITCTAQCEKLEKIHLQESAQSL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1126 EDLEHLNEDGELWFAYEGLKKATR--VLESHFQSQKDCYEKEIEGLNFKVVHLSQEIN--HLQKLFREETDINESIRHEV 1201
Cdd:TIGR00618 469 KEREQQLQTKEQIHLQETRKKAVVlaRLLELQEEPCPLCGSCIHPNPARQDIDNPGPLtrRMQRGEQTYAQLETSEEDVY 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1202 TRLTSENMMIPDFKQQISELERQKQDLES---RLKEQAEKIEGKLEEPFSHLNRIREEERMQGRAVEAQSEMHPEGKERL 1278
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFSILTQcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQ 628
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486759 1279 VGAIHEPHEAIKFPKKQPEAEEEVESILQQEASRLSLEKRDLEEE-LDMKDRMIRRLQDQVKTLTKTTEKANH 1350
Cdd:TIGR00618 629 DVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKElLASRQLALQKMQSEKEQLTYWKEMLAQ 701
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
968-1340 |
8.56e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.44 E-value: 8.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 968 LELQRERA-------EQMLQEKSEELkekmDKLTRQLFDDVQKEEQQRLvlekgfelktQAYEKQIESLREEIKALKDER 1040
Cdd:PRK02224 164 LEEYRERAsdarlgvERVLSDQRGSL----DQLKAQIEEKEEKDLHERL----------NGLESELAELDEEIERYEEQR 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1041 SQLHHQLEEGQVTsdrlkgeVARLSKQAKTISEFEKEIELLQAQKIDVEKhvqsQKREMRERMSEVTKQLLE-SYDIEDV 1119
Cdd:PRK02224 230 EQARETRDEADEV-------LEEHEERREELETLEAEIEDLRETIAETER----EREELAEEVRDLRERLEElEEERDDL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1120 RSRLSVEDL--EHLNEDGElwfAYEGLKKATR-VLESHFQSQKDcYEKEIEGLNFKVVHLSQEINHLqklfREETDINES 1196
Cdd:PRK02224 299 LAEAGLDDAdaEAVEARRE---ELEDRDEELRdRLEECRVAAQA-HNEEAESLREDADDLEERAEEL----REEAAELES 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1197 irhevtRLTSENMMIPDFKQQISELERQKQDLESRLK---EQAEKIEGKLEEPFSHLNRIREEERMQGRAVEAQSEMHPE 1273
Cdd:PRK02224 371 ------ELEEAREAVEDRREEIEELEEEIEELRERFGdapVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE 444
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486759 1274 GKERLvgaihephEAIKFPK-KQP-EAEEEVESILQQEASRLSLEKR--DLEEELDMKDRMIRRLQDQVKT 1340
Cdd:PRK02224 445 AEALL--------EAGKCPEcGQPvEGSPHVETIEEDRERVEELEAEleDLEEEVEEVEERLERAEDLVEA 507
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
848-1239 |
1.56e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 848 RRYRKLLQEHKAV---ILQKYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRvgdlE 924
Cdd:COG4717 88 EEYAELQEELEELeeeLEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE----E 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 925 KVQKLEAELEKAATHRhsyEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQML---QEKSEELKEKMDKLTRQLFDDV 1001
Cdd:COG4717 164 ELEELEAELAELQEEL---EELLEQLSLATEEELQDLAEELEELQQRLAELEEELeeaQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1002 QKE---EQQRLVLEKGFELKTQAYEKQIESLREEIKA---------------LKDERSQLHHQLEEGQVTSDRLKGEVAR 1063
Cdd:COG4717 241 LEErlkEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1064 LSKQAKTIsEFEKEIELLQAQK-IDVEKHVQSQKREMRERMSEVTKQLLESyDIEDVRSRLSVEDLEHLNEDGELWFAYE 1142
Cdd:COG4717 321 LEELLAAL-GLPPDLSPEELLElLDRIEELQELLREAEELEEELQLEELEQ-EIAALLAEAGVEDEEELRAALEQAEEYQ 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1143 GLKKATRVLESHFQSQKDCYEKEIEGLNFKvvHLSQEINHLQKLFREETDINESIRHEVTRLTSENMMIPDfKQQISELE 1222
Cdd:COG4717 399 ELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELEQLEE-DGELAELL 475
|
410
....*....|....*..
gi 124486759 1223 RQKQDLESRLKEQAEKI 1239
Cdd:COG4717 476 QELEELKAELRELAEEW 492
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
980-1256 |
2.50e-08 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 57.62 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 980 QEKsEELKEKMDKLTRQLfDDVQKEEQQRLVLEKGFELKTQ-----------AYEKQIESLREEIKALKDERSQLHHQLE 1048
Cdd:pfam00038 1 NEK-EQLQELNDRLASYI-DKVRFLEQQNKLLETKISELRQkkgaepsrlysLYEKEIEDLRRQLDTLTVERARLQLELD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1049 EGQVTSDRLKgevARLSKQAKTISEFEKEIELLQAQ-------KIDVEKHVQS-------QKREMRERMSEVTKQLLESY 1114
Cdd:pfam00038 79 NLRLAAEDFR---QKYEDELNLRTSAENDLVGLRKDldeatlaRVDLEAKIESlkeelafLKKNHEEEVRELQAQVSDTQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1115 DIEDVRSRLSVEDLEHLNEdgeLWFAYEGL-KKATRVLESHFQSQkdcYEKeieglnfkvvhLSQEIN-HLQKLFREETD 1192
Cdd:pfam00038 156 VNVEMDAARKLDLTSALAE---IRAQYEEIaAKNREEAEEWYQSK---LEE-----------LQQAAArNGDALRSAKEE 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486759 1193 INESiRHEVTRLTSEnmmIPDFKQQISELERQKQDLESRLKEQAEKIEGKLEEPFSHLNRIREE 1256
Cdd:pfam00038 219 ITEL-RRTIQSLEIE---LQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQE 278
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
955-1315 |
2.86e-08 |
|
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: 58.68 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 955 EERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMD-KLT-----RQLFDDVQKEEQQRLVLEKGFE-LKTQAY--EKQ 1025
Cdd:pfam10174 337 EQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEeKSTlageiRDLKDMLDVKERKINVLQKKIEnLQEQLRdkDKQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1026 IESLREEIKALKDERSQ-------LHHQLEEGQVTSDRLKGEVARLSKQ--------AKTISEFEKEIELLQAQK----- 1085
Cdd:pfam10174 417 LAGLKERVKSLQTDSSNtdtalttLEEALSEKERIIERLKEQREREDRErleeleslKKENKDLKEKVSALQPELtekes 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1086 --IDVEKHVQSQKREM-----------------RERMSEVTKQLLESYDIE-------DVRSRLSVEDLE---HLNEDGE 1136
Cdd:pfam10174 497 slIDLKEHASSLASSGlkkdsklksleiaveqkKEECSKLENQLKKAHNAEeavrtnpEINDRIRLLEQEvarYKEESGK 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1137 LWFAYEGLKKATRVLEshfqSQKDCYEKEIEGLNFKVVHLSQEIN----HLQKLFREETDINESIRHEVTRLTsENMMIP 1212
Cdd:pfam10174 577 AQAEVERLLGILREVE----NEKNDKDKKIAELESLTLRQMKEQNkkvaNIKHGQQEMKKKGAQLLEEARRRE-DNLADN 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1213 DFKQQISEL----ERQKQDLESrLKEQAEKIEGKLEEPFSHLNRIREEERMQgraVEAQSEMHpegKERLVGAIHEPHEA 1288
Cdd:pfam10174 652 SQQLQLEELmgalEKTRQELDA-TKARLSSTQQSLAEKDGHLTNLRAERRKQ---LEEILEMK---QEALLAAISEKDAN 724
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 124486759 1289 IKF-----PKKQPEAEEE----------VESILQQEASRLSL 1315
Cdd:pfam10174 725 IALlelssSKKKKTQEEVmalkrekdrlVHQLKQQTQNRMKL 766
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
864-1232 |
2.92e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 58.60 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 864 KYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLE--DQNRENHGLVEKLTSLAALRvgDLEKVQKL-EAELEKAAThr 940
Cdd:pfam17380 259 RYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEkmEQERLRQEKEEKAREVERRR--KLEEAEKArQAEMDRQAA-- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 941 hSYEEKGRRYRDTvEERLSKLQKHNAELELQRERAEQMLQEKSeelkeKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQ 1020
Cdd:pfam17380 335 -IYAEQERMAMER-ERELERIRQEERKRELERIRQEEIAMEIS-----RMRELERLQMERQQKNERVRQELEAARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1021 AYEKQieslrEEIKALKDERSQLHHQLEEG-QVTSDRLKGEVAR-LSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKRE 1098
Cdd:pfam17380 408 EEERQ-----RKIQQQKVEMEQIRAEQEEArQREVRRLEEERAReMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1099 MRER--MSEVTKQLLESyDIEDVRSRLSVED-----LEHLNEDGELWFAYEglkKATRVLESHFQSQKDCYEKeiEGLNF 1171
Cdd:pfam17380 483 KRDRkrAEEQRRKILEK-ELEERKQAMIEEErkrklLEKEMEERQKAIYEE---ERRREAEEERRKQQEMEER--RRIQE 556
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486759 1172 KVVHLSQEINHLQKLFREETDI-----NESIRHEVTRLTSENMMIPDFKQQISELerQKQDLESRL 1232
Cdd:pfam17380 557 QMRKATEERSRLEAMEREREMMrqiveSEKARAEYEATTPITTIKPIYRPRISEY--QPPDVESHM 620
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
932-1306 |
2.98e-08 |
|
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: 58.83 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 932 ELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEK-----SEELKEKMDKLTRQLFDDVQKEEQ 1006
Cdd:pfam02463 157 EIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKkaleyYQLKEKLELEEEYLLYLDYLKLNE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1007 QRLVL------------EKGFELKTQAYEKQIESLREEIKALKDERSQ----LHHQLEEGQVTSDRLKGEVARLSKqakt 1070
Cdd:pfam02463 237 ERIDLlqellrdeqeeiESSKQEIEKEEEKLAQVLKENKEEEKEKKLQeeelKLLAKEEEELKSELLKLERRKVDD---- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1071 isefEKEIELLQAQKIDVEKHVQSQKREMRERmsevtKQLLESYDIEDVRSRLSVEDLEHLNEDGELwfAYEGLKKATRV 1150
Cdd:pfam02463 313 ----EEKLKESEKEKKKAEKELKKEKEEIEEL-----EKELKELEIKREAEEEEEEELEKLQEKLEQ--LEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1151 LESHFQSQKDCYEKEIEGLNFKVvhlsQEINHLQKLFREETDINESIRHEVTRLTSENMMIPDFKQQISELERQKQDLES 1230
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEE----KEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1231 RLK-------EQAEKIEGKLEEPFSHLNRIREEERMQGRAVEAQSEMHPEGKERL--VGAIHEPHEAIKFPKKQPEAEEE 1301
Cdd:pfam02463 458 LKLlkdelelKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLlaLIKDGVGGRIISAHGRLGDLGVA 537
|
....*
gi 124486759 1302 VESIL 1306
Cdd:pfam02463 538 VENYK 542
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
866-1335 |
3.23e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 866 ARAWLarrRFQNIRRFVLNIQLTYRvQRLQKKLEDQNRENHGLVEKLTSLAALRvgdlEKVQKLEAELEKAATHRHS--- 942
Cdd:PRK04863 271 AADYM---RHANERRVHLEEALELR-RELYTSRRQLAAEQYRLVEMARELAELN----EAESDLEQDYQAASDHLNLvqt 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 943 ---YEEKGRRYRDTVEERLSKLQKHNAELELQRERAEqMLQEKSEELKEKMDKLTRQLFDDVQK-EEQQRLVLEkgFELK 1018
Cdd:PRK04863 343 alrQQEKIERYQADLEELEERLEEQNEVVEEADEQQE-ENEARAEAAEEEVDELKSQLADYQQAlDVQQTRAIQ--YQQA 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1019 TQAYEKQ-----------------IESLREEIKALKDERSQLHHQLeegqvtsdrlkgevaRLSKQAKtiSEFEKEIELL 1081
Cdd:PRK04863 420 VQALERAkqlcglpdltadnaedwLEEFQAKEQEATEELLSLEQKL---------------SVAQAAH--SQFEQAYQLV 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1082 QAQKIDVEkhvqsqkremRERMSEVTKQLLESYdiedvrsrlsvEDLEHLNEDGElwfayeGLKKATRVLESHFQSQKDc 1161
Cdd:PRK04863 483 RKIAGEVS----------RSEAWDVARELLRRL-----------REQRHLAEQLQ------QLRMRLSELEQRLRQQQR- 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1162 yekeieglnfkVVHLSQEINhlQKLFREETDINE----SIRHEvTRLTSENMMIPDFKQQISELERQKQDLESRLkEQAE 1237
Cdd:PRK04863 535 -----------AERLLAEFC--KRLGKNLDDEDEleqlQEELE-ARLESLSESVSEARERRMALRQQLEQLQARI-QRLA 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1238 KIEGKLEEPFSHLNRIREeermqgraveaQSEMHPEGKERLVGAIhepheaikfpkkQPEAEEEVEsiLQQEASRLSLEK 1317
Cdd:PRK04863 600 ARAPAWLAAQDALARLRE-----------QSGEEFEDSQDVTEYM------------QQLLERERE--LTVERDELAARK 654
|
490
....*....|....*...
gi 124486759 1318 RDLEEEldmkdrmIRRLQ 1335
Cdd:PRK04863 655 QALDEE-------IERLS 665
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
893-1128 |
3.44e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 893 RLQKKLEDQNRENHGLVEKLtSLAALRVGDLE-KVQKLEAELEKAATHRHSYEEKGRRY---RDTVEERLSKLQkhnAEL 968
Cdd:TIGR02169 291 RVKEKIGELEAEIASLERSI-AEKERELEDAEeRLAKLEAEIDKLLAEIEELEREIEEErkrRDKLTEEYAELK---EEL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 969 ELQRERAEQM------LQEKSEELKEKMDKLTRQLFDdvQKEEQQRLVLEKgfelktQAYEKQIESLREEIKALKDERSQ 1042
Cdd:TIGR02169 367 EDLRAELEEVdkefaeTRDELKDYREKLEKLKREINE--LKRELDRLQEEL------QRLSEELADLNAAIAGIEAKINE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1043 LHHQLEEGQvtsDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRErmSEVTKQLLESYdiedVRSR 1122
Cdd:TIGR02169 439 LEEEKEDKA---LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE--AEAQARASEER----VRGG 509
|
....*.
gi 124486759 1123 LSVEDL 1128
Cdd:TIGR02169 510 RAVEEV 515
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
846-1115 |
3.82e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 846 ARRRYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNI-----QLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRV 920
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 921 GDLEKVQKLEAELEKA----ATHRHSYEEKGRRYRDT------VEERLSKLQKHNAELELQRERAEQMLQEKSE------ 984
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLkeelKALREALDELRAELTLLneeaanLRERLESLERRIAATERRLEDLEEQIEELSEdiesla 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 985 ----ELKEKMDKLTRQL---FDDVQKEEQQRLVLEKGFELKT---QAYEKQIESLREEIKALKDERSQLHHQLEEGQVTS 1054
Cdd:TIGR02168 859 aeieELEELIEELESELealLNERASLEEALALLRSELEELSeelRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1055 DRLKG-----------------------------EVARLSKQAK--------TISEFEKEIE---LLQAQKIDVEKHVQS 1094
Cdd:TIGR02168 939 DNLQErlseeysltleeaealenkieddeeearrRLKRLENKIKelgpvnlaAIEEYEELKErydFLTAQKEDLTEAKET 1018
|
330 340
....*....|....*....|.
gi 124486759 1095 QKREMRERMSEVTKQLLESYD 1115
Cdd:TIGR02168 1019 LEEAIEEIDREARERFKDTFD 1039
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
890-1232 |
4.99e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 890 RVQRLQKKLEDQNRENHGLVEKLTSLAAlrvgdlEKVQKLEAELEKAATHRHSYEEKGR--RYRDTVEERLSKLQKHNAE 967
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKA------EEAKKAEEAKIKAEELKKAEEEKKKveQLKKKEAEEKKKAEELKKA 1655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 968 LELQRERAEQmLQEKSEELKEKMDKLTRQLFDDVQKEEQqrlvlekgfeLKTQAYE-KQIESLREEIKALKDERSQLHHQ 1046
Cdd:PTZ00121 1656 EEENKIKAAE-EAKKAEEDKKKAEEAKKAEEDEKKAAEA----------LKKEAEEaKKAEELKKKEAEEKKKAEELKKA 1724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1047 LEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQsqkrEMRERMSEVTKqllESYDIEDVRSRLSVE 1126
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE----EIRKEKEAVIE---EELDEEDEKRRMEVD 1797
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1127 -DLEHLNEDGELwfAYEGLKKATRVLeshfQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLT 1205
Cdd:PTZ00121 1798 kKIKDIFDNFAN--IIEGGKEGNLVI----NDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFN 1871
|
330 340 350
....*....|....*....|....*....|.
gi 124486759 1206 SENMMIPDFKQQISELERQKQ----DLESRL 1232
Cdd:PTZ00121 1872 KEKDLKEDDEEEIEEADEIEKidkdDIEREI 1902
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
890-1269 |
5.15e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 57.60 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 890 RVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLE--KVQKLEAELEKAATHRH--SYEEKGRRYRDTVEErLSKLQKhn 965
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKEryKRDREQWERQRRELESRvaELKEELRQSREKHEE-LEEKYK-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 966 aelELQRERAEqMLQEKSEELKEKMDKLTR--QLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEikalKDERSQL 1043
Cdd:pfam07888 105 ---ELSASSEE-LSEEKDALLAQRAAHEARirELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE----EAERKQL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1044 HHQLEEGQVTSDRLKGE--VAR--LSKQAKTISEFEKEIELLQ-----AQKIDVE-KHVQSQKREMRER--MSEVTKQLL 1111
Cdd:pfam07888 177 QAKLQQTEEELRSLSKEfqELRnsLAQRDTQVLQLQDTITTLTqklttAHRKEAEnEALLEELRSLQERlnASERKVEGL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1112 ESyDIEDV---RSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFR 1188
Cdd:pfam07888 257 GE-ELSSMaaqRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1189 EETDINESIRHEVTRLTSENMMipdfkqQISELERQKQDLESRLK-EQAEKiEGKLEEPFSHLNRIRE-EERMQGRAVEA 1266
Cdd:pfam07888 336 EERMEREKLEVELGREKDCNRV------QLSESRRELQELKASLRvAQKEK-EQLQAEKQELLEYIRQlEQRLETVADAK 408
|
...
gi 124486759 1267 QSE 1269
Cdd:pfam07888 409 WSE 411
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
896-1112 |
5.67e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 5.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 896 KKLEDQNRENHGLVEKLTSLAALRVG---DLEKVQKLEAEL-----------EKAATHRHSYEEKGRRYRDTVEERLSKL 961
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSlkkELEKLEELKKKLaelekkldeleEELAELLKELEELGFESVEELEERLKEL 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 962 QK-HNAELELQRerAEQMLQEKSEELKEKMDKLTrQLFDDVQKEEQQRLVLEKGFELKTQAY--------EKQIESLREE 1032
Cdd:PRK03918 598 EPfYNEYLELKD--AEKELEREEKELKKLEEELD-KAFEELAETEKRLEELRKELEELEKKYseeeyeelREEYLELSRE 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1033 IKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLE 1112
Cdd:PRK03918 675 LAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEIASEIFE 754
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1071-1378 |
5.97e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1071 ISEFEKEIELLQAQKIDVEKHvqsqkREMRErmsevtkqllesyDIEDVRSRLSVEDLEHLNEdgELWFAYEGLKKATRV 1150
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERY-----KELKA-------------ELRELELALLVLRLEELRE--ELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1151 LESHfQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLF----REETDINESIRHEVTRLTSENMMIPDFKQQISELERQKQ 1226
Cdd:TIGR02168 255 LEEL-TAELQELEEKLEELRLEVSELEEEIEELQKELyalaNEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1227 DLESRLKEQAEKIEGKLEEpfshlnrireeermqgraVEAQSEMHPEGKERLVgaihEPHEAIKFPKKQPEAEEEVESIL 1306
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEE------------------LESLEAELEELEAELE----ELESRLEELEEQLETLRSKVAQL 391
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486759 1307 QQEASRLSLEKRDLEEELDMKDRMIRRLQDQVKTLTKTTEKANHVHLPSGSREYLGMLEYKKEDEGKLIQNL 1378
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL 463
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
884-1340 |
8.65e-08 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 57.06 E-value: 8.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 884 NIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLaalrvgdlekvQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQK 963
Cdd:pfam05557 50 NQELQKRIRLLEKREAEAEEALREQAELNRLK-----------KKYLEALNKKLNEKESQLADAREVISCLKNELSELRR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 964 --HNAELELQRERAE-QMLQEKSEELKEKMDKLTrQLFDDVQKEEQQRLVlekgFELKTQAYEKQIESLREEIKALKDER 1040
Cdd:pfam05557 119 qiQRAELELQSTNSElEELQERLDLLKAKASEAE-QLRQNLEKQQSSLAE----AEQRIKELEFEIQSQEQDSEIVKNSK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1041 SQLhHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQ----------AQKIDVEKHVQSQKREMRERMSEVTKQL 1110
Cdd:pfam05557 194 SEL-ARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKrklereekyrEEAATLELEKEKLEQELQSWVKLAQDTG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1111 LESYDIEDVRSR---LSVEDLEHLNEDGELWFAYEGLKKATRVLeshfQSQKDCYEKEIEGLNFKVVHLSQEINHLQK-- 1185
Cdd:pfam05557 273 LNLRSPEDLSRRieqLQQREIVLKEENSSLTSSARQLEKARREL----EQELAQYLKKIEDLNKKLKRHKALVRRLQRrv 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1186 -LFREETDINESIRHEVTRLTSENMMIPDFKQQISELERQKQDLESRLKEQAEKIEGKLEEPFSHLNRIREEER-MQGRA 1263
Cdd:pfam05557 349 lLLTKERDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLEReLQALR 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1264 VEAQsemhpegkerlvgaihepheaikfPKKQPEAEEEVESiLQQEASRLSLEKRDLEE-----ELDMKDRMIRRLQDQV 1338
Cdd:pfam05557 429 QQES------------------------LADPSYSKEEVDS-LRRKLETLELERQRLREqknelEMELERRCLQGDYDPK 483
|
..
gi 124486759 1339 KT 1340
Cdd:pfam05557 484 KT 485
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
848-1403 |
1.07e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.04 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 848 RRYRKLLQEHKAV----------ILQKYARAWLARRRFQNIRRFVLNIQltYRVQRLQKKLEDQNRENHGLVEKltSLAA 917
Cdd:pfam05483 78 RLYSKLYKEAEKIkkwkvsieaeLKQKENKLQENRKIIEAQRKAIQELQ--FENEKVSLKLEEEIQENKDLIKE--NNAT 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 918 LRVGDLEKvQKLEAELEKAATHRHSYEEKGRRYRDtVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQL 997
Cdd:pfam05483 154 RHLCNLLK-ETCARSAEKTKKYEYEREETRQVYMD-LNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEY 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 998 FDDVQ-KEEQQRLVL----EKGFELKTQAY------------EKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGE 1060
Cdd:pfam05483 232 KKEINdKEKQVSLLLiqitEKENKMKDLTFlleesrdkanqlEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1061 VARL------------------------SKQAKT-----ISEFEKEI----ELLQAQKIDVEKH----------VQSQKR 1097
Cdd:pfam05483 312 QKALeedlqiatkticqlteekeaqmeeLNKAKAahsfvVTEFEATTcsleELLRTEQQRLEKNedqlkiitmeLQKKSS 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1098 EMrERMSEVTKQllESYDIEDVRSRLSvEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQkdcyEKEIEGLNFKVV--- 1174
Cdd:pfam05483 392 EL-EEMTKFKNN--KEVELEELKKILA-EDEKLLDEKKQFEKIAEELKGKEQELIFLLQAR----EKEIHDLEIQLTaik 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1175 ----HLSQEINHLQKLFREETDINESIRHEVTRLTSENM-MIPDFKQQISELERQKQDL------ESRLKEQAEKIEGKL 1243
Cdd:pfam05483 464 tseeHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKeLTQEASDMTLELKKHQEDIinckkqEERMLKQIENLEEKE 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1244 EEPFSHLNRIREEERMQGRAVEAqsemhpegkerlvgaihepheaiKFPKKQPEAEEEVESILQQEASRLSLEKR--DLE 1321
Cdd:pfam05483 544 MNLRDELESVREEFIQKGDEVKC-----------------------KLDKSEENARSIEYEVLKKEKQMKILENKcnNLK 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1322 EELDMKDRMIRRLQDQVKTLTKTTEKAN-------------HVHLPSGSREYLGMLE-YKKEDEGKLI--QNLILDLKPR 1385
Cdd:pfam05483 601 KQIENKNKNIEELHQENKALKKKGSAENkqlnayeikvnklELELASAKQKFEEIIDnYQKEIEDKKIseEKLLEEVEKA 680
|
650
....*....|....*...
gi 124486759 1386 GVVVNMIPGLPAHILFMC 1403
Cdd:pfam05483 681 KAIADEAVKLQKEIDKRC 698
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
886-1073 |
1.46e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 886 QLTYRVQRLQKKLEDQNRENHGLVEKLTSL------AALRVGDLEK-VQKLEAELEKAATHRHSYEEKGRRYRDTVEERL 958
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALerriaaLARRIRALEQeLAALEAELAELEKEIAELRAELEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 959 SKLQKH----------NAELELQRERAEQMLQEKSEELKEKMDKLTRQLFD------DVQKEEQQRLVLEKGFELKTQAY 1022
Cdd:COG4942 111 RALYRLgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAElaalraELEAERAELEALLAELEEERAAL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 124486759 1023 EKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISE 1073
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
874-1245 |
1.75e-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: 56.50 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 874 RFQNIRRFVLNIQLTYRvQRLQKKLEDQNRENHGLVEKLTSLAALrvGDLEKvqKLEAELEKAATH--------RHsyEE 945
Cdd:COG3096 275 RHANERRELSERALELR-RELFGARRQLAEEQYRLVEMARELEEL--SARES--DLEQDYQAASDHlnlvqtalRQ--QE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 946 KGRRYRDTVEERLSKLQKHNAELElqrERAEQ--MLQEKSEELKEKMDKLTRQLfDDVQK--EEQQRLVLekgfelktqA 1021
Cdd:COG3096 348 KIERYQEDLEELTERLEEQEEVVE---EAAEQlaEAEARLEAAEEEVDSLKSQL-ADYQQalDVQQTRAI---------Q 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1022 YEKQIESLRE----------EIKALKDErsQLHHQLEEGQVTSDRLKGEvARLSKQAKTISEFEKEIELLQAQKIDVEK- 1090
Cdd:COG3096 415 YQQAVQALEKaralcglpdlTPENAEDY--LAAFRAKEQQATEEVLELE-QKLSVADAARRQFEKAYELVCKIAGEVERs 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1091 ------------------------HVQSQKREMRERMSEVTK--QLLESYDIEDVRSRLSVEDLEHLnedgelwfayegL 1144
Cdd:COG3096 492 qawqtarellrryrsqqalaqrlqQLRAQLAELEQRLRQQQNaeRLLEEFCQRIGQQLDAAEELEEL------------L 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1145 KKATRVLESHFQSQKDCYEKEIEgLNFKVVHLSQEINHLQK---LFREETDINESIRHEV-TRLTSENMMIpDFKQQISE 1220
Cdd:COG3096 560 AELEAQLEELEEQAAEAVEQRSE-LRQQLEQLRARIKELAArapAWLAAQDALERLREQSgEALADSQEVT-AAMQQLLE 637
|
410 420
....*....|....*....|....*
gi 124486759 1221 LERQKQDLESRLKEQAEKIEGKLEE 1245
Cdd:COG3096 638 REREATVERDELAARKQALESQIER 662
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
892-1115 |
2.28e-07 |
|
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: 55.80 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 892 QRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKV-----QKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNA 966
Cdd:pfam05667 246 TKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELlssfsGSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVET 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 967 ELELQRERAEQM--LQEKSEELKEKMDKLT----------RQLFDDVQKEEQQRLVLEKGFELKTQAY------EKQIES 1028
Cdd:pfam05667 326 EEELQQQREEELeeLQEQLEDLESSIQELEkeikklessiKQVEEELEELKEQNEELEKQYKVKKKTLdllpdaEENIAK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1029 LREEIKALKDERSQLHHQLEEGQVTsdrLKGEVARLsKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRErmsEVTK 1108
Cdd:pfam05667 406 LQALVDASAQRLVELAGQWEKHRVP---LIEEYRAL-KEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKE---ELYK 478
|
....*..
gi 124486759 1109 QLLESYD 1115
Cdd:pfam05667 479 QLVAEYE 485
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
888-1102 |
2.58e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 888 TYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAAthrhsyeekgRRYRDTvEERLSKLQKHNAE 967
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA----------RRIRAL-EQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 968 LELQRERAEQMLQEKSEELKEKMDKLTRQ--------LFDdvQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDE 1039
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLgrqpplalLLS--PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486759 1040 RSQLHHQLEEGQVTSDRLKGEVARLSKQ-----------AKTISEFEKEIELLQAQKIDVEKHVQSQKREMRER 1102
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALkaerqkllarlEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1022-1341 |
2.86e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1022 YEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVA--------RLSKQAKTISEFEKEIELLQAQKIDVEKHVQ 1093
Cdd:TIGR02169 168 FDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaeryqalLKEKREYEGYELLKEKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1094 SQKREMRERMSEVTKQLLESYDIEDVRSRLSvEDLEHLNEDgelwfayEGLKKATRVLESHFQ-----SQKDCYEKEIEG 1168
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQLLEELN-KKIKDLGEE-------EQLRVKEKIGELEAEiasleRSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1169 LNFKVVHLSQEINhlqKLFREETDINESIRHEVTRLTSENMMIPDFKQQISELERQKQDLESRLKEQAEKI---EGKLEE 1245
Cdd:TIGR02169 320 AEERLAKLEAEID---KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELkdyREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1246 PFSHLNRI-REEERMQGRAVEAQSEM--HPEGKERLVGAIHEPHEAIK-FPKKQPEAEEEVESI------LQQEASRLSL 1315
Cdd:TIGR02169 397 LKREINELkRELDRLQEELQRLSEELadLNAAIAGIEAKINELEEEKEdKALEIKKQEWKLEQLaadlskYEQELYDLKE 476
|
330 340
....*....|....*....|....*.
gi 124486759 1316 EKRDLEEELDMKDRMIRRLQDQVKTL 1341
Cdd:TIGR02169 477 EYDRVEKELSKLQRELAEAEAQARAS 502
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
955-1343 |
2.95e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 55.52 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 955 EERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLfddvqKEEQQRL-VLEKGFELKTQAYEKQIESLR--- 1030
Cdd:pfam05557 8 KARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRN-----QELQKRIrLLEKREAEAEEALREQAELNRlkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1031 ---EEIKALKDERSQlhhQLEEGQVTSDRLKGEVARLSKQAKtisefEKEIELlQAQKIDVEKhVQSQKREMRERMSEVT 1107
Cdd:pfam05557 83 kylEALNKKLNEKES---QLADAREVISCLKNELSELRRQIQ-----RAELEL-QSTNSELEE-LQERLDLLKAKASEAE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1108 K--QLLESYDIEDVRSRLSVEDLEHLNEDGELWfayeglKKATRVLESHFQSQKDcYEKEIEglnfkvvHLSQEINHLQK 1185
Cdd:pfam05557 153 QlrQNLEKQQSSLAEAEQRIKELEFEIQSQEQD------SEIVKNSKSELARIPE-LEKELE-------RLREHNKHLNE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1186 LFREETDINESIRHEVTRLTSENmmipDFKQQISELERQKQDLESRLKEQaEKIEGkleepfSHLNRIREEERMQGRAVE 1265
Cdd:pfam05557 219 NIENKLLLKEEVEDLKRKLEREE----KYREEAATLELEKEKLEQELQSW-VKLAQ------DTGLNLRSPEDLSRRIEQ 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1266 AQSE--MHPEGKERLVGaihephEAIKFPKKQPEaeeevesiLQQEASRLSLEKRDLEEELDMKDRMIRRLQDQVKTLTK 1343
Cdd:pfam05557 288 LQQReiVLKEENSSLTS------SARQLEKARRE--------LEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTK 353
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
896-1245 |
3.08e-07 |
|
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: 55.25 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 896 KKLEDQNRENHGLVEKLtslaalrvgdLEKVQKLEAELekaATHRHSYEEkgrrYRDTVEERLSKLQKHNAELE------ 969
Cdd:pfam06160 110 DELLESEEKNREEVEEL----------KDKYRELRKTL---LANRFSYGP----AIDELEKQLAEIEEEFSQFEeltesg 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 970 --LQRERAEQMLQEKSEELKEKMDKLTrQLFDDVQKEEQQRL---------VLEKGFELKTQAYEKQIESLREEIKALKd 1038
Cdd:pfam06160 173 dyLEAREVLEKLEEETDALEELMEDIP-PLYEELKTELPDQLeelkegyreMEEEGYALEHLNVDKEIQQLEEQLEENL- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1039 ersqlhHQLEEGQVtsDRLKGEVARLSKQAKTISE-FEKEIEllqAQKiDVEKHvQSQKREMRERMSEVTKQLLESYDIE 1117
Cdd:pfam06160 251 ------ALLENLEL--DEAEEALEEIEERIDQLYDlLEKEVD---AKK-YVEKN-LPEIEDYLEHAEEQNKELKEELERV 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1118 DVRSRLSVEDLEHlnedgelwfayeglkkaTRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINEsi 1197
Cdd:pfam06160 318 QQSYTLNENELER-----------------VRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEE-- 378
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 124486759 1198 RHEvtrltsenmmipDFKQQISELERQkqdlESRLKEQAEKIEGKLEE 1245
Cdd:pfam06160 379 EQE------------EFKESLQSLRKD----ELEAREKLDEFKLELRE 410
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
892-1338 |
3.55e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 892 QRLQKKLEDQNrENHGLVEKLTSLAALRVGDL--EKVQKLEAELEKAATHRhsyeekgrryrDTVEERLSKLQKHnaELE 969
Cdd:COG4913 262 ERYAAARERLA-ELEYLRAALRLWFAQRRLELleAELEELRAELARLEAEL-----------ERLEARLDALREE--LDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 970 LQRERAEQMLQEKsEELKEKMDKLTRQLfDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEE 1049
Cdd:COG4913 328 LEAQIRGNGGDRL-EQLEREIERLEREL-EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1050 GQvtsDRLKGEVARLSKQAKTIsefEKEIELLQAQKIDVEKHVQSQKREMRERMS------------------------- 1104
Cdd:COG4913 406 AL---AEAEAALRDLRRELREL---EAEIASLERRKSNIPARLLALRDALAEALGldeaelpfvgelievrpeeerwrga 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1105 ----------------EVTKQLLESYDIEDVRSRLSVEDLEHLNEDGEL---------------------W--------F 1139
Cdd:COG4913 480 iervlggfaltllvppEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERprldpdslagkldfkphpfraWleaelgrrF 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1140 AY------EGLKKATR----------------------VLESHF-----QSQKDCYEKEIEGLNFKVVHLSQEINHLQKL 1186
Cdd:COG4913 560 DYvcvdspEELRRHPRaitragqvkgngtrhekddrrrIRSRYVlgfdnRAKLAALEAELAELEEELAEAEERLEALEAE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1187 FREETDINESIRHeVTRLTSENMMIPDFKQQISELERQKQDLES------RLKEQAEKIEGKLEEPFSHLNRIREEERMQ 1260
Cdd:COG4913 640 LDALQERREALQR-LAEYSWDEIDVASAEREIAELEAELERLDAssddlaALEEQLEELEAELEELEEELDELKGEIGRL 718
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124486759 1261 GRAVEAQSEMHPEGKERLVGAihephEAIKFPKKQPEAEEEVESILQQEASRlsLEKRDLEEELDMKDRMIRRLQDQV 1338
Cdd:COG4913 719 EKELEQAEEELDELQDRLEAA-----EDLARLELRALLEERFAAALGDAVER--ELRENLEERIDALRARLNRAEEEL 789
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
895-1185 |
5.96e-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: 53.66 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 895 QKKLEDQNRenHGLVEKLTSLAALRVGDLEK-VQKLEAELEKAathrhsyEEKgrrYRDTVEERLSkLQKHNAELELQR- 972
Cdd:pfam15905 66 QKNLKESKD--QKELEKEIRALVQERGEQDKrLQALEEELEKV-------EAK---LNAAVREKTS-LSASVASLEKQLl 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 973 --ERAEQMLQEKSEE--LKEKMDKLTRQLF---DDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHH 1045
Cdd:pfam15905 133 elTRVNELLKAKFSEdgTQKKMSSLSMELMklrNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1046 QLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQllesydIEDVRSRLSV 1125
Cdd:pfam15905 213 EKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQ------IKDLNEKCKL 286
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1126 edLEHLNEDgelwfayeglkkatrvLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQK 1185
Cdd:pfam15905 287 --LESEKEE----------------LLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
891-1138 |
8.96e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.61 E-value: 8.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 891 VQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAEL----EKAATHRHSYEEKGRRYRDTVEERLS--KLQKH 964
Cdd:COG1340 38 LKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERdelnEKLNELREELDELRKELAELNKAGGSidKLRKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 965 NAELE--LQRE----RAEQMLQEKSEELKE------KMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEK------QI 1026
Cdd:COG1340 118 IERLEwrQQTEvlspEEEKELVEKIKELEKelekakKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEaqelheEM 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1027 ESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQaktISEFEKEIELLQAQKIDVEKhvQSQKREMRERMSEV 1106
Cdd:COG1340 198 IELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE---LRELRKELKKLRKKQRALKR--EKEKEELEEKAEEI 272
|
250 260 270
....*....|....*....|....*....|..
gi 124486759 1107 TKQLLESydiedvrSRLSVEDLEHLNEDGELW 1138
Cdd:COG1340 273 FEKLKKG-------EKLTTEELKLLQKSGLLE 297
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1018-1248 |
9.65e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 9.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1018 KTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKT----ISEFEKEIELLQAQKIDVEKHVQ 1093
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAleqeLAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1094 SQKREMRERMSEVTKQ--------LLESYDIEDVRSRLSVedLEHLNE-DGELWFAYEGLKKATRVLESHFQSQKDCYEK 1164
Cdd:COG4942 101 AQKEELAELLRALYRLgrqpplalLLSPEDFLDAVRRLQY--LKYLAPaRREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1165 EIEGlnfkvvhLSQEINHLQKLFREETDINESIRHEVTRLtsenmmipdfKQQISELERQKQDLESRLKEQAEKIEGKLE 1244
Cdd:COG4942 179 LLAE-------LEEERAALEALKAERQKLLARLEKELAEL----------AAELAELQQEAEELEALIARLEAEAAAAAE 241
|
....
gi 124486759 1245 EPFS 1248
Cdd:COG4942 242 RTPA 245
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
886-1243 |
9.94e-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: 53.82 E-value: 9.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 886 QLTYRVQRLQKKLEDQNRENHGLVEKLTSLAalrvgdlEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKhn 965
Cdd:TIGR00618 532 RGEQTYAQLETSEEDVYHQLTSERKQRASLK-------EQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK-- 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 966 aELELQRERAEQmLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLR--EEIKALKDERSQL 1043
Cdd:TIGR00618 603 -LSEAEDMLACE-QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALsiRVLPKELLASRQL 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1044 HHQLEEG---QVTSDR--LKGEVARLSKQAKTISEFEKEIELLQ----AQKIDVEK----HVQSQKREMRERmSEVTKQL 1110
Cdd:TIGR00618 681 ALQKMQSekeQLTYWKemLAQCQTLLRELETHIEEYDREFNEIEnassSLGSDLAAredaLNQSLKELMHQA-RTVLKAR 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1111 LESYDIEDVRSRLSV---EDLEHLNEDGELWF-AYEGLKKATRVLESHFQSQKDCYEKEiegLNFKVVHLSQEINHLQKL 1186
Cdd:TIGR00618 760 TEAHFNNNEEVTAALqtgAELSHLAAEIQFFNrLREEDTHLLKTLEAEIGQEIPSDEDI---LNLQCETLVQEEEQFLSR 836
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 124486759 1187 FREETDINESIRHEVTRLTSENMMIPDFKQQISELERQKQDLESRLKEQAEKIEGKL 1243
Cdd:TIGR00618 837 LEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDAL 893
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1071-1342 |
1.09e-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: 53.92 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1071 ISEFEKEIELLQAQKIDVEKH---VQSQKREMRERMSEVTKQLLESYDIEDVRSRL-SVEDLEHLNEdgelwfayeglKK 1146
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENierLDLIIDEKRQQLERLRREREKAERYQALLKEKrEYEGYELLKE-----------KE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1147 ATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFRE-ETDINESIRHEVTRLTSEnmmIPDFKQQISELERQK 1225
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEK---IGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1226 QDLESRLkeqaEKIEGKLEEPFSHLNRIREEERMQGRAVEAQSEMhpegKERLVGAIHEPHEAIKFPKKQPEAEEEVESI 1305
Cdd:TIGR02169 311 AEKEREL----EDAEERLAKLEAEIDKLLAEIEELEREIEEERKR----RDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
250 260 270
....*....|....*....|....*....|....*..
gi 124486759 1306 LQQEASRLSLEKRDLEEELDMKDRMIRRLQDQVKTLT 1342
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREINELKRELDRLQEELQRLS 419
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
886-1350 |
1.22e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.49 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 886 QLTYRVQRLQKKLEdqNRENhglveKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHN 965
Cdd:TIGR04523 37 QLEKKLKTIKNELK--NKEK-----ELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 966 AELELQREraeQMLQEKSEelkekMDKLTRQLfddVQKEEQQRLVLEKGFELKTQAYE--KQIESLREEIKALKDERSQL 1043
Cdd:TIGR04523 110 SEIKNDKE---QKNKLEVE-----LNKLEKQK---KENKKNIDKFLTEIKKKEKELEKlnNKYNDLKKQKEELENELNLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1044 HHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRL 1123
Cdd:TIGR04523 179 EKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1124 SVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSqkdcYEKEIEGLNfkvvhlSQEINHLQKLFREE-TDINESIRHEVT 1202
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQ----LKSEISDLN------NQKEQDWNKELKSElKNQEKKLEEIQN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1203 RLTSENMMIPDFKQQISELERQKQDLES-------RLKEQAEKIEGKLEEPFSHLNRIREEERmQGRAVEAQSEMHPEGK 1275
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKKELTNSESensekqrELEEKQNEIEKLKKENQSYKQEIKNLES-QINDLESKIQNQEKLN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1276 ERLVGAIHepheaiKFPKKQPEAEEEVESILQQ------EASRLSLEKRDLEEELDMKDRMIRRLQDQVKTLTKTTEKAN 1349
Cdd:TIGR04523 408 QQKDEQIK------KLQQEKELLEKEIERLKETiiknnsEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
.
gi 124486759 1350 H 1350
Cdd:TIGR04523 482 Q 482
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
890-1347 |
1.41e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.37 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 890 RVQRLQKKLEDQNRENHGLVEKLTSLAALrvgdLEKVQKLEAELEKAATHRHSYEEKGRRYRDtVEERLSKLQkhNAELE 969
Cdd:PRK01156 219 EIERLSIEYNNAMDDYNNLKSALNELSSL----EDMKNRYESEIKTAESDLSMELEKNNYYKE-LEERHMKII--NDPVY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 970 LQRERAEQMLQEKSEelKEKMDKLTRQLFDDVQKEEQQRLVLEkgfelktqayekQIESLREEIKALKDERSQLHHQLEE 1049
Cdd:PRK01156 292 KNRNYINDYFKYKND--IENKKQILSNIDAEINKYHAIIKKLS------------VLQKDYNDYIKKKSRYDDLNNQILE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1050 GQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLE-SYDIE--DVRSRLSVE 1126
Cdd:PRK01156 358 LEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDiSSKVSslNQRIRALRE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1127 DLEHLNEDGELWFAYE---------GLKKATRVLEsHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKL--FREETDINE 1195
Cdd:PRK01156 438 NLDELSRNMEMLNGQSvcpvcgttlGEEKSNHIIN-HYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRkeYLESEEINK 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1196 SIrHEVTRLTSENMMIPDFKQQISELeRQKQDLESRLKEQAEKIE-GKLEEPF-SHLNRIREEERMQGRAVEAQSEmhpE 1273
Cdd:PRK01156 517 SI-NEYNKIESARADLEDIKIKINEL-KDKHDKYEEIKNRYKSLKlEDLDSKRtSWLNALAVISLIDIETNRSRSN---E 591
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124486759 1274 GKERLVGAIHEPHE-AIKFPKKQPEAEEEVESIlQQEASRLSLEKRDLEEeldmKDRMIRRLQDQVKTLTKTTEK 1347
Cdd:PRK01156 592 IKKQLNDLESRLQEiEIGFPDDKSYIDKSIREI-ENEANNLNNKYNEIQE----NKILIEKLRGKIDNYKKQIAE 661
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
952-1245 |
1.41e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 952 DTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLfdDVQKEEQQRLVLEKgfelktQAYEKQIESLRE 1031
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEEL--EQLREELEQAREEL------EQLEEELEQARS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1032 EIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKT----ISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVT 1107
Cdd:COG4372 74 ELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEElqeeLEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1108 KQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAyEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLF 1187
Cdd:COG4372 154 ELEEQLESLQEELAALEQELQALSEAEAEQALD-ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 124486759 1188 REETDINESIRHEVTRLTSENMMIPDFKQQISELERQKQDLESRLKEQAEKIEGKLEE 1245
Cdd:COG4372 233 LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
847-1325 |
2.31e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.66 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 847 RRRYRKLLQEHKAVILQKYARA------------WLARRRFQNIRRFVLNIQLtyRVQRLQKKLEDQNRENHGLVEKLTS 914
Cdd:TIGR00618 97 TRSHRKTEQPEQLYLEQKKGRGrilaakkseteeVIHDLLKLDYKTFTRVVLL--PQGEFAQFLKAKSKEKKELLMNLFP 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 915 L-----AALRVGDLEKVQKLEAELEKAathRHSYEEkgrryrDTVEERLSKLQKHNAELElqreRAEQMLQEKSEELKEK 989
Cdd:TIGR00618 175 LdqytqLALMEFAKKKSLHGKAELLTL---RSQLLT------LCTPCMPDTYHERKQVLE----KELKHLREALQQTQQS 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 990 MDKLTRQLFDDVQKEEQQRLVLEKGFELKT-QAYEKQIESLREEI-------------KALKDERSQLHHQLEEGQVTSD 1055
Cdd:TIGR00618 242 HAYLTQKREAQEEQLKKQQLLKQLRARIEElRAQEAVLEETQERInrarkaaplaahiKAVTQIEQQAQRIHTELQSKMR 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1056 RLKGEVARLSKQAKTISEFEKEIELLQA-----QKIDVEKHVQSQKREMRERMSEVT---KQLLESYDIEDVRSRLSVED 1127
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQRRLLQTlhsqeIHIRDAHEVATSIREISCQQHTLTqhiHTLQQQKTTLTQKLQSLCKE 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1128 LEHLNEdgelwfayEGLKKATRVL-ESHFQSQKDCYEKEIEglnfkvvhLSQEINHLQKLFREEtdinesirhEVTRLTS 1206
Cdd:TIGR00618 402 LDILQR--------EQATIDTRTSaFRDLQGQLAHAKKQQE--------LQQRYAELCAAAITC---------TAQCEKL 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1207 ENMMIPDFKQQISELERQKQDLESRLKEQAEKieGKLEEPFshLNRIREEER-MQGR----AVEAQSEMHPEGKERLVGA 1281
Cdd:TIGR00618 457 EKIHLQESAQSLKEREQQLQTKEQIHLQETRK--KAVVLAR--LLELQEEPCpLCGScihpNPARQDIDNPGPLTRRMQR 532
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 124486759 1282 IHEPHeaikfpKKQPEAEEEVESILQQEASRLSLEKRDLEEELD 1325
Cdd:TIGR00618 533 GEQTY------AQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ 570
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
764-1334 |
2.53e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 764 QKHVRGWLQRRKFLRERQAALTIQRyfRGQQTVRKAITAT--ALKEAWAAIILQKYCRGYLVRNLYQLIRVATITIQAHT 841
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAEL--EELEAELEELEAElaELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 842 RGflaRRRYRKLLQEHKAVILQKYARawLARRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVG 921
Cdd:COG1196 302 QD---IARLEERRRELEERLEELEEE--LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 922 DLEKVQKL---EAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLF 998
Cdd:COG1196 377 AEEELEELaeeLLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 999 DDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEI 1078
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1079 E------LLQAQKIDVEKHVQSQKREM----RERMSEVTKQLLesyDIEDVRSRLSVEDLEHLNEDGELWFAYEglkkat 1148
Cdd:COG1196 537 EaaleaaLAAALQNIVVEDDEVAAAAIeylkAAKAGRATFLPL---DKIRARAALAAALARGAIGAAVDLVASD------ 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1149 rvleshfqsQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINE--SIRHEVTRLTSENMMIPDFKQQISELERQKQ 1226
Cdd:COG1196 608 ---------LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRlrEVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1227 DLESRLKEQAEKIEGKLEEpfsHLNRIREEERMQGRAVEAQSEMHPEGKERLVGAIHEPHEAIKfpKKQPEAEEEVESIL 1306
Cdd:COG1196 679 AELEELAERLAEEELELEE---ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE--ELLEEEELLEEEAL 753
|
570 580
....*....|....*....|....*...
gi 124486759 1307 QQEASRLSLEkrDLEEELDMKDRMIRRL 1334
Cdd:COG1196 754 EELPEPPDLE--ELERELERLEREIEAL 779
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1021-1316 |
3.52e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.68 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1021 AYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIellqaqkidvekhvQSQKREMR 1100
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDEL--------------NEKVKELK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1101 ERMSEVTKQLLESYD-IEDVRSRLSVEDLEHLNEDgelwfayeGLKKATRVLESHFQSQKDCYEKEIEglnfkvvhLSQE 1179
Cdd:COG1340 78 EERDELNEKLNELREeLDELRKELAELNKAGGSID--------KLRKEIERLEWRQQTEVLSPEEEKE--------LVEK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1180 INHLQKLFREETDINEsIRHEVTRLTSEnmmIPDFKQQISELERQKQDlesrLKEQAEKIEGKLEEPFSHLNRIREE-ER 1258
Cdd:COG1340 142 IKELEKELEKAKKALE-KNEKLKELRAE---LKELRKEAEEIHKKIKE----LAEEAQELHEEMIELYKEADELRKEaDE 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486759 1259 MQGRAVEAQSEMHPEGKE------------RLVGAIHEPHEAIKFPKKQPEAEEEVESILQ--QEASRLSLE 1316
Cdd:COG1340 214 LHKEIVEAQEKADELHEEiielqkelrelrKELKKLRKKQRALKREKEKEELEEKAEEIFEklKKGEKLTTE 285
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
895-1270 |
4.00e-06 |
|
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: 51.50 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 895 QKKLEDQNRENHGLVEKLTSLAAlRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRER 974
Cdd:COG5185 208 KESETGNLGSESTLLEKAKEIIN-IEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANN 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 975 AEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIkalKDERSQLHHQLEEGQVTS 1054
Cdd:COG5185 287 LIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEI---EQGQESLTENLEAIKEEI 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1055 DRLKGEVaRLSKQAKTISEFEKEIEllqAQKIDVEKHVQSQKREMRERMSEVTKQLlesydiedvrsRLSVEDLEHLNED 1134
Cdd:COG5185 364 ENIVGEV-ELSKSSEELDSFKDTIE---STKESLDEIPQNQRGYAQEILATLEDTL-----------KAADRQIEELQRQ 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1135 gelwfayegLKKATRVLEShFQSQKDCYEKEIEglnfKVVHLSQEiNHLQKLFREETDINESIRHEVTRLTSENMMIpdf 1214
Cdd:COG5185 429 ---------IEQATSSNEE-VSKLLNELISELN----KVMREADE-ESQSRLEEAYDEINRSVRSKKEDLNEELTQI--- 490
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 124486759 1215 KQQISELERQKQDLESRLKEQAEKIEGKLEEPFSHLNrirEEERMQGRAVEAQSEM 1270
Cdd:COG5185 491 ESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLK---DFMRARGYAHILALEN 543
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
922-1109 |
4.85e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 922 DLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEE-------LKEKMDKLT 994
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEiaelraeLEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 995 RQLFDDVQKEEQQRLVLEKGFELKTQAYeKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEF 1074
Cdd:COG4942 108 ELLRALYRLGRQPPLALLLSPEDFLDAV-RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190
....*....|....*....|....*....|....*
gi 124486759 1075 EKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQ 1109
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
873-1373 |
6.40e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 873 RRFQNIRRfvlnIQLTYRVQRLQKKLEDQNRENHGLVEKltSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRD 952
Cdd:PTZ00121 1146 RKAEDAKR----VEIARKAEDARKAEEARKAEDAKKAEA--ARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARK 1219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 953 TVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLF---------------DDVQKEEQQRLVLE----- 1012
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFarrqaaikaeearkaDELKKAEEKKKADEakkae 1299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1013 ---KGFELKTQAYE-KQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQ---K 1085
Cdd:PTZ00121 1300 ekkKADEAKKKAEEaKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEakkK 1379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1086 IDVEKHVQSQKR---EMRERMSEVTKQLLESYDIEDVRSRlsVEDLEHLNEdgELWFAYEGLKKATRVLESHFQSQKDCY 1162
Cdd:PTZ00121 1380 ADAAKKKAEEKKkadEAKKKAEEDKKKADELKKAAAAKKK--ADEAKKKAE--EKKKADEAKKKAEEAKKADEAKKKAEE 1455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1163 EKEIEGLNfKVVHLSQEINHLQKLFREETDINESIR--HEVTRLTSENMMIPDFKQQISEL---ERQKQDLESRLKEQAE 1237
Cdd:PTZ00121 1456 AKKAEEAK-KKAEEAKKADEAKKKAEEAKKADEAKKkaEEAKKKADEAKKAAEAKKKADEAkkaEEAKKADEAKKAEEAK 1534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1238 KI-EGKLEEPFSHLNRIREEERMQGRAVEAQSEMHPEGKERLVGAIHEPHEAIKFPKKQPEAE---EEVESILQQEASRL 1313
Cdd:PTZ00121 1535 KAdEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklYEEEKKMKAEEAKK 1614
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1314 SLEKRDLEEELDMKDRMIRRLQDQVKTLTKTTEKANHVHLPSGSREYLGMLEYKKEDEGK 1373
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1016-1238 |
6.50e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 6.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1016 ELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQaktISEFEKEIELLQAQkidvekhVQSQ 1095
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE---IDKLQAEIAEAEAE-------IEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1096 KREMRERMSEVTKQ---------LLESYDIEDVRSRLSVedLEHLNE-DGELwfaYEGLKKATRVLEshfqSQKDCYEKE 1165
Cdd:COG3883 85 REELGERARALYRSggsvsyldvLLGSESFSDFLDRLSA--LSKIADaDADL---LEELKADKAELE----AKKAELEAK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486759 1166 IEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLtsenmmipdfKQQISELERQKQDLESRLKEQAEK 1238
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA----------EAQLAELEAELAAAEAAAAAAAAA 218
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
859-1043 |
6.85e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 859 AVILQKYARAWLARRRFQNIRRFVLNIQ-LTYRVQRLQKKLEDQN------RENHGLV--EKLTSLAALRVGDLE-KVQK 928
Cdd:COG3206 151 AAVANALAEAYLEQNLELRREEARKALEfLEEQLPELRKELEEAEaaleefRQKNGLVdlSEEAKLLLQQLSELEsQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 929 LEAELEKAATHRHSYEEKGRRYRDTVEE-----RLSKLQKHNAELELQRERAEQMLQEKS---EELKEKMDKLTRQLFDD 1000
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPEllqspVIQQLRAQLAELEAELAELSARYTPNHpdvIALRAQIAALRAQLQQE 310
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 124486759 1001 VQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQL 1043
Cdd:COG3206 311 AQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL 353
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
878-1101 |
7.08e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 7.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 878 IRRFVLNIQLTY-RVQRLQKKLEDQNReNHGLVEKltslAALRVGDLEKVQKLEAELEKAAT---------HRHSYEEKG 947
Cdd:COG4913 213 VREYMLEEPDTFeAADALVEHFDDLER-AHEALED----AREQIELLEPIRELAERYAAARErlaeleylrAALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 948 RRYrDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKE-----------KMDKLTRQLfDDVQKEEQQRlvlekgfE 1016
Cdd:COG4913 288 RRL-ELLEAELEELRAELARLEAELERLEARLDALREELDEleaqirgnggdRLEQLEREI-ERLERELEER-------E 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1017 LKTQAYEKQIESL--------------REEIKALKDERSQLHHQLEEGQvtsDRLKGEVARLSKQAKTIsefEKEIELLQ 1082
Cdd:COG4913 359 RRRARLEALLAALglplpasaeefaalRAEAAALLEALEEELEALEEAL---AEAEAALRDLRRELREL---EAEIASLE 432
|
250
....*....|....*....
gi 124486759 1083 AQKIDVEKHVQSQKREMRE 1101
Cdd:COG4913 433 RRKSNIPARLLALRDALAE 451
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
924-1156 |
7.17e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 924 EKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQM------LQEKSEELKEKMDKLTRQL 997
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAqeelesLQEEAEELQEELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 998 fDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEegQVTSDRLKGEVARLSKQAKTISEFEKE 1077
Cdd:COG4372 125 -QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ--ALSEAEAEQALDELLKEANRNAEKEEE 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486759 1078 IELLQaQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRsrlSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQ 1156
Cdd:COG4372 202 LAEAE-KLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE---LEEDKEELLEEVILKEIEELELAILVEKDTEEE 276
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
924-1077 |
1.02e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 50.24 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 924 EKVQKLEAELEKAATHRHSYEEKGRRYRDTVEErlskLQKHNAELELQRERAEQMLQEKSEELKEKmdkltrqlfddvqK 1003
Cdd:COG2433 392 EEEPEAEREKEHEERELTEEEEEIRRLEEQVER----LEAEVEELEAELEEKDERIERLERELSEA-------------R 454
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486759 1004 EEQQRLVLEkgfelktqayEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKgEVARLSKQ-----AKTISEFEKE 1077
Cdd:COG2433 455 SEERREIRK----------DREISRLDREIERLERELEEERERIEELKRKLERLK-ELWKLEHSgelvpVKVVEKFTKE 522
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
958-1343 |
1.42e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 958 LSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLfDDVQKEEQQRLVLEKGFElktqAYEKQIESLREEIKALK 1037
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKE-EEYAELQEELEELEEELE----ELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1038 DERsQLHHQLEEGQVTSDRLKGEVAR---LSKQAKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESY 1114
Cdd:COG4717 123 KLL-QLLPLYQELEALEAELAELPERleeLEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1115 D------------IEDVRSRLSV--EDLEHLNEDGELWFAYEGLKKATRVLE------SHFQSQKDCYEKEIEGLNFKVV 1174
Cdd:COG4717 202 EelqqrlaeleeeLEEAQEELEEleEELEQLENELEAAALEERLKEARLLLLiaaallALLGLGGSLLSLILTIAGVLFL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1175 HLSQEINHLQKLFREETDINESI-------------RHEVTRLTSENMMIPDFK-----------QQISELERQKQDLES 1230
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAeelqalpaleeleEEELEELLAALGLPPDLSpeellelldriEELQELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1231 RLKEQAEKIE----------GKLEEPFSHLNRIREEERMQGRAVEAQSEMHPEGKERLVGAIHEPHEAIK-----FPKKQ 1295
Cdd:COG4717 362 ELQLEELEQEiaallaeagvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEeeleeLEEEL 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 124486759 1296 PEAEEEVESiLQQEASRLSLEKRDLEE--ELDMKDRMIRRLQDQVKTLTK 1343
Cdd:COG4717 442 EELEEELEE-LREELAELEAELEQLEEdgELAELLQELEELKAELRELAE 490
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
949-1343 |
1.73e-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: 50.05 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 949 RYRDTVEERLSKLQKHNAELelqreraeQMLQEKSEELKEKMDKLTRQlfdDVQKEEQQRLVlekgfelktQAYEKQIES 1028
Cdd:TIGR00606 190 TLRQVRQTQGQKVQEHQMEL--------KYLKQYKEKACEIRDQITSK---EAQLESSREIV---------KSYENELDP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1029 LREEIKALKDERSQLhHQLEEGQVTSDRLKGEVARLSKQAKTIseFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTK 1108
Cdd:TIGR00606 250 LKNRLKEIEHNLSKI-MKLDNEIKALKSRKKQMEKDNSELELK--MEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQR 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1109 QlLESYDIEdvRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKdcYEKEIEGLNfKVVHLSQEINHLQKLFR 1188
Cdd:TIGR00606 327 E-LEKLNKE--RRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLA--TRLELDGFE-RGPFSERQIKNFHTLVI 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1189 E-ETDINESIRHEVTRLTSENMMIpdfKQQISELERQKQDLESRLKEQAEKIEGKLEEpfshlnriREEERMQGRAVEAQ 1267
Cdd:TIGR00606 401 ErQEDEAKTAAQLCADLQSKERLK---QEQADEIRDEKKGLGRTIELKKEILEKKQEE--------LKFVIKELQQLEGS 469
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486759 1268 SEMHPEGKERLVGAIHEPHEAIKFPKKQPEAEEEVEsiLQQEASRLSLEKRDLEEELDMKDRMIRRLQdQVKTLTK 1343
Cdd:TIGR00606 470 SDRILELDQELRKAERELSKAEKNSLTETLKKEVKS--LQNEKADLDRKLRKLDQEMEQLNHHTTTRT-QMEMLTK 542
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
971-1190 |
1.99e-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: 48.99 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 971 QRERAEQmLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKgFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEG 1050
Cdd:COG4942 18 QADAAAE-AEAELEQLQQEIAELEKELAALKKEEKALLKQLAA-LERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1051 QVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKI-DVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVEDLE 1129
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFlDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486759 1130 H---LNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREE 1190
Cdd:COG4942 176 LealLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
924-1084 |
2.05e-05 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 46.87 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 924 EKVQKLEAELEKAAthrhsyeekgRRYRDTVEERLSKLQKH-NAELELQRERAE-------QMLQEKSEELKEKMDKLTR 995
Cdd:pfam01442 11 TYAEELQEQLGPVA----------QELVDRLEKETEALRERlQKDLEEVRAKLEpyleelqAKLGQNVEELRQRLEPYTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 996 QLFDDVQK--EEQQRLVLEKGFELKTQAyEKQIESLREEIKALKDE-RSQLHHQLEEGQVTSDRLKGEV-ARLSKQAKTI 1071
Cdd:pfam01442 81 ELRKRLNAdaEELQEKLAPYGEELRERL-EQNVDALRARLAPYAEElRQKLAERLEELKESLAPYAEEVqAQLSQRLQEL 159
|
170
....*....|....
gi 124486759 1072 SE-FEKEIELLQAQ 1084
Cdd:pfam01442 160 REkLEPQAEDLREK 173
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
993-1138 |
2.33e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.09 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 993 LTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKT-- 1070
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERRei 461
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124486759 1071 -----ISEFEKEIELLQAQKIDVEKHVQSQKREMrERMSEVTKqLLESYDIEDVR--SRLSVEDLEHLNEDGELW 1138
Cdd:COG2433 462 rkdreISRLDREIERLERELEEERERIEELKRKL-ERLKELWK-LEHSGELVPVKvvEKFTKEAIRRLEEEYGLK 534
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
896-1256 |
2.65e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.06 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 896 KKLEDQNRENHGLVEKLtslaalrvgdLEKVQKLEAELekaATHRHSYeekGRRYrDTVEERLSKLQKHNAELE------ 969
Cdd:PRK04778 129 QELLESEEKNREEVEQL----------KDLYRELRKSL---LANRFSF---GPAL-DELEKQLENLEEEFSQFVeltesg 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 970 --LQRERAEQMLQEKSEELKEKMDKLTrQLFDDVQKEEQQRL---------VLEKGFELKTQAYEKQIESLREEIKALKD 1038
Cdd:PRK04778 192 dyVEAREILDQLEEELAALEQIMEEIP-ELLKELQTELPDQLqelkagyreLVEEGYHLDHLDIEKEIQDLKEQIDENLA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1039 ERSQLhhqleegqvtsdrlkgEVARLSKQAKTISE--------FEKEIEllqAQKiDVEKHvQSQKREMRERMSEVTKQL 1110
Cdd:PRK04778 271 LLEEL----------------DLDEAEEKNEEIQEridqlydiLEREVK---ARK-YVEKN-SDTLPDFLEHAKEQNKEL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1111 L-------ESY-----DIEDVRSRLsvEDLEHLNEDgelwfayegLKKATRVLESH---FQSQKDCYEKEIEGLnfKVVH 1175
Cdd:PRK04778 330 KeeidrvkQSYtlnesELESVRQLE--KQLESLEKQ---------YDEITERIAEQeiaYSELQEELEEILKQL--EEIE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1176 LSQE--INHLQKLFREETDINESIRHEVTRLTS-----ENMMIP----DFKQQISELERQKQDLESRLKEQ---AEKIEG 1241
Cdd:PRK04778 397 KEQEklSEMLQGLRKDELEAREKLERYRNKLHEikrylEKSNLPglpeDYLEMFFEVSDEIEALAEELEEKpinMEAVNR 476
|
410
....*....|....*
gi 124486759 1242 KLEEPFSHLNRIREE 1256
Cdd:PRK04778 477 LLEEATEDVETLEEE 491
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
897-1118 |
2.74e-05 |
|
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: 47.79 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 897 KLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAE 976
Cdd:pfam06008 41 QIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 977 QMLQEKSEELKEKMDklTRQLFDDVQKEEQQrlvLEKGFELKTQAyEKQIESLREEIKALKDersQLHHQLEEgqvTSDR 1056
Cdd:pfam06008 121 SRMLAEAQRMLGEIR--SRDFGTQLQNAEAE---LKAAQDLLSRI-QTWFQSPQEENKALAN---ALRDSLAE---YEAK 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486759 1057 LKGEVARLSK-QAKTisefeKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIED 1118
Cdd:pfam06008 189 LSDLRELLREaAAKT-----RDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKTARDSLD 246
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
895-1278 |
2.77e-05 |
|
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: 48.95 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 895 QKKLEDQNRENHGLVEKLTSLAALRVGDLE----KVQKLEAELEKAATHRHSYEEKGRRYRDTVE-ERL--SKLQKHNAE 967
Cdd:pfam05483 417 DEKLLDEKKQFEKIAEELKGKEQELIFLLQarekEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEkEKLknIELTAHCDK 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 968 LELQRERAEQMLQEKSEELKEKMDKLtrqlfDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDErsqLHHQL 1047
Cdd:pfam05483 497 LLLENKELTQEASDMTLELKKHQEDI-----INCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDE---VKCKL 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1048 EEGQVTSDRLKGEVARLSKQAKTI----SEFEKEIEllqaQKIDVEKHVQSQKREMRERMSEVTKQlLESYDIEDVRSRL 1123
Cdd:pfam05483 569 DKSEENARSIEYEVLKKEKQMKILenkcNNLKKQIE----NKNKNIEELHQENKALKKKGSAENKQ-LNAYEIKVNKLEL 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1124 SVEDLEHlnedgelwfayeglkkatrvlesHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFRE----ETDINESIRH 1199
Cdd:pfam05483 644 ELASAKQ-----------------------KFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEavklQKEIDKRCQH 700
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1200 EVTRLTSenmMIPDFKQQISEL-ERQKQDL---ESRLKEQAEkIEGKLEEPFSHLnrireeeRMQGRAVEAQSEMHPEGK 1275
Cdd:pfam05483 701 KIAEMVA---LMEKHKHQYDKIiEERDSELglyKNKEQEQSS-AKAALEIELSNI-------KAELLSLKKQLEIEKEEK 769
|
...
gi 124486759 1276 ERL 1278
Cdd:pfam05483 770 EKL 772
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
721-1109 |
2.83e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 721 LHRLIQDSNQYQFGRTKIFFRAGQVAYLEKLRLDKLRQDCIMIQKHVRGWLQRRKFLRERQAALT--IQRYFRGQQTVRK 798
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEeeLEEAQEELEELEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 799 AITATAlKEAWAAIILQKycrgyLVRNLYQLIRVATITIQAHTRGFLARRRYR--KLLQEHKAVILqkYARAWLARRRFQ 876
Cdd:COG4717 228 ELEQLE-NELEAAALEER-----LKEARLLLLIAAALLALLGLGGSLLSLILTiaGVLFLVLGLLA--LLFLLLAREKAS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 877 NIRRFvLNIQLTYRVQRLQKKLEDQNRENHGLVEKLT-SLAALRVGDLEKVQKLEAELEKAathrhsyeEKGRRYRDTVE 955
Cdd:COG4717 300 LGKEA-EELQALPALEELEEEELEELLAALGLPPDLSpEELLELLDRIEELQELLREAEEL--------EEELQLEELEQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 956 ERLSKLQKHNAELELQRERAEQMLQEKsEELKEKMDKLTRQLfddvqkEEQQRLVLEKGFELKTQAYEKQIESLREEIKA 1035
Cdd:COG4717 371 EIAALLAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQL------EELLGELEELLEALDEEELEEELEELEEELEE 443
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486759 1036 LKDERSQLHHQLEEgqvtsdrLKGEVARLSKQaKTISEFEKEIELLQAQKIDVEKHVQSQK--REMRERMSEVTKQ 1109
Cdd:COG4717 444 LEEELEELREELAE-------LEAELEQLEED-GELAELLQELEELKAELRELAEEWAALKlaLELLEEAREEYRE 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
846-1049 |
4.24e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 846 ARRRYRKLLQEH-KAVILQKYARAWLARRRFQNIRRFVLNIQ-----LTYRVQRLQKKLEDQNRENHGLVEKLTSLAALR 919
Cdd:COG4913 260 LAERYAAARERLaELEYLRAALRLWFAQRRLELLEAELEELRaelarLEAELERLEARLDALREELDELEAQIRGNGGDR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 920 VGDLEK-VQKLEAELEKAATHRHSYEEKGRRYRDTVEERLsklqkhnAELELQRERAEQMLQEKSEELKEkmdkLTRQLF 998
Cdd:COG4913 340 LEQLEReIERLERELEERERRRARLEALLAALGLPLPASA-------EEFAALRAEAAALLEALEEELEA----LEEALA 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 124486759 999 DDVQKEEQQRlvlekgfelktqayeKQIESLREEIKALKDERSQLHHQLEE 1049
Cdd:COG4913 409 EAEAALRDLR---------------RELRELEAEIASLERRKSNIPARLLA 444
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
890-1009 |
4.68e-05 |
|
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: 45.42 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 890 RVQRLQKKLEDQNR-----ENHGLVEKLTSLAAlrvgdlEKVQKLEAELEKAATHRH-SYEEKGRRYRDTVEERLSKLQK 963
Cdd:pfam05672 21 RQAREQREREEQERlekeeEERLRKEELRRRAE------EERARREEEARRLEEERRrEEEERQRKAEEEAEEREQREQE 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 124486759 964 HNAELELQRERAEQMLQEKSEELKEKMDKLTrqlfddvQKEEQQRL 1009
Cdd:pfam05672 95 EQERLQKQKEEAEAKAREEAERQRQEREKIM-------QQEEQERL 133
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
627-652 |
5.51e-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: 45.41 E-value: 5.51e-05
10 20
....*....|....*....|....*.
gi 124486759 627 KFRSSLYLLMETLNATTPHYVRCIKP 652
Cdd:cd01363 145 IINESLNTLMNVLRATRPHFVRCISP 170
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
845-1383 |
6.11e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.04 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 845 LARRRYRKLLQEHKAVILQKYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLaalrvgdLE 924
Cdd:pfam02463 185 LAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIES-------SK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 925 KVQKLEAELEKaatHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKE 1004
Cdd:pfam02463 258 QEIEKEEEKLA---QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1005 EQ--QRLVLEKGFELKTQAYEKQIESLREEIKAL---KDERSQLHHQLEEGQVTSDRLKGEVarLSKQAKTISEFEKEIE 1079
Cdd:pfam02463 335 EEieELEKELKELEIKREAEEEEEEELEKLQEKLeqlEEELLAKKKLESERLSSAAKLKEEE--LELKSEEEKEAQLLLE 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1080 LLQAQKIDVEKHVQSQKREmrermSEVTKQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQK 1159
Cdd:pfam02463 413 LARQLEDLLKEEKKEELEI-----LEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1160 dcyEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTSENMMIPDFKQQISELERQKQDLESRLKEQAEKI 1239
Cdd:pfam02463 488 ---LLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1240 EGKLEEPFSHLNRIREEERMQGRAVEAQSEMHPEGKERLVGAIHEPHEAIKFPKKQPEAEEEVESILQQEASRLSLEKRD 1319
Cdd:pfam02463 565 KLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAK 644
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124486759 1320 LEEELDMKDRMIRRLQDQ-VKTLTKTTEKANHVHLPSGSREYLGMLEYKKEDEGKLIQNLILDLK 1383
Cdd:pfam02463 645 ESGLRKGVSLEEGLAEKSeVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREK 709
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
975-1258 |
6.81e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.54 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 975 AEQMLQ---EKSEELKEKMDKLtrqlfddVQKEEQQRL----VLEKGFELKTQ------AYEKQIESLREEIKALKDERS 1041
Cdd:pfam06160 91 IEELLDdieEDIKQILEELDEL-------LESEEKNREeveeLKDKYRELRKTllanrfSYGPAIDELEKQLAEIEEEFS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1042 QLHHQLEEGQVTS-----DRLKGEVARLSKQAKTISEFEKEI---------EL------LQAQKIDVE-KHVQSQKREMR 1100
Cdd:pfam06160 164 QFEELTESGDYLEarevlEKLEEETDALEELMEDIPPLYEELktelpdqleELkegyreMEEEGYALEhLNVDKEIQQLE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1101 ERMSEvTKQLLESYDIEDVRsrlsvEDLEHLNED-GELWFAYEGLKKATRVLESHFQSQKDcYEKEIEGLNFkvvHLSQE 1179
Cdd:pfam06160 244 EQLEE-NLALLENLELDEAE-----EALEEIEERiDQLYDLLEKEVDAKKYVEKNLPEIED-YLEHAEEQNK---ELKEE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1180 INHLQKLFR---EETDINESIRHEVTRLTSENMMIpdfkqqISELERQKQ---DLESRLKE---QAEKIEGKLEEPFSHL 1250
Cdd:pfam06160 314 LERVQQSYTlneNELERVRGLEKQLEELEKRYDEI------VERLEEKEVaysELQEELEEileQLEEIEEEQEEFKESL 387
|
....*...
gi 124486759 1251 NRIREEER 1258
Cdd:pfam06160 388 QSLRKDEL 395
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
986-1240 |
7.92e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.61 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 986 LKEKMDKLTRQL-------FDDVqKEEQQRLVLEKGFELKTQAYEK--QIESLREEIKALKDERSQLHHQLEEgqvtsDR 1056
Cdd:PRK05771 14 LKSYKDEVLEALhelgvvhIEDL-KEELSNERLRKLRSLLTKLSEAldKLRSYLPKLNPLREEKKKVSVKSLE-----EL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1057 LKGEVARLSKQAKTISEFEKEIELLQaqkidvekhvqSQKREMRERMSEVTKqlLESYDIedvrsrlsveDLEHLNeDGE 1136
Cdd:PRK05771 88 IKDVEEELEKIEKEIKELEEEISELE-----------NEIKELEQEIERLEP--WGNFDL----------DLSLLL-GFK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1137 LWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFrEETDINESIRHEVTRLTSENMMIPDFKQ 1216
Cdd:PRK05771 144 YVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVE-EELKKLGFERLELEEEGTPSELIREIKE 222
|
250 260
....*....|....*....|....
gi 124486759 1217 QISELERQKQDLESRLKEQAEKIE 1240
Cdd:PRK05771 223 ELEEIEKERESLLEELKELAKKYL 246
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
976-1231 |
8.55e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 8.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 976 EQMLQEKS-----EELKEKMDKLTRqLFDDVQKEEQQRLVLEkgfELKTQAyeKQIESLREEIKALKDERSQLhhQLEEG 1050
Cdd:COG4913 215 EYMLEEPDtfeaaDALVEHFDDLER-AHEALEDAREQIELLE---PIRELA--ERYAAARERLAELEYLRAAL--RLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1051 QVTSDRLKGEVARLskqaktisefEKEIELLQAQKidveKHVQSQKREMRERMSEVTKQLLESydiedvrsrlSVEDLEH 1130
Cdd:COG4913 287 QRRLELLEAELEEL----------RAELARLEAEL----ERLEARLDALREELDELEAQIRGN----------GGDRLEQ 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1131 LNEDgelwfayegLKKATRVLESHFQSQKDcYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTSENMM 1210
Cdd:COG4913 343 LERE---------IERLERELEERERRRAR-LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA 412
|
250 260
....*....|....*....|..
gi 124486759 1211 -IPDFKQQISELERQKQDLESR 1231
Cdd:COG4913 413 aLRDLRRELRELEAEIASLERR 434
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
867-1170 |
8.93e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.64 E-value: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 867 RAWLARRRFQNIRRFVLNIQltYRVQRLQKKLEDQNRENHGLVEKLTS--------LAALR--------VGDLEKVQ-KL 929
Cdd:COG3096 286 RALELRRELFGARRQLAEEQ--YRLVEMARELEELSARESDLEQDYQAasdhlnlvQTALRqqekieryQEDLEELTeRL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 930 EAE---LEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQ-----EKSEEL--------------- 986
Cdd:COG3096 364 EEQeevVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQavqalEKARALcglpdltpenaedyl 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 987 ---KEKMDKLTRQLFDDVQK---EEQQRLVLEKGFEL---------KTQAYEKQIESLRE--EIKALKDERSQLHHQL-- 1047
Cdd:COG3096 444 aafRAKEQQATEEVLELEQKlsvADAARRQFEKAYELvckiageveRSQAWQTARELLRRyrSQQALAQRLQQLRAQLae 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1048 ----EEGQVTSDRLKGEVA-RLSKQAKTISEFEKEIELLQAQKIDVEKHV----------QSQKREMRERMSEVTKQLLE 1112
Cdd:COG3096 524 leqrLRQQQNAERLLEEFCqRIGQQLDAAEELEELLAELEAQLEELEEQAaeaveqrselRQQLEQLRARIKELAARAPA 603
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486759 1113 SYDIEDVRSRLSVEDLEHLNEDGELWFAYEGL---KKATRVLESHFQSQKDCYEKEIEGLN 1170
Cdd:COG3096 604 WLAAQDALERLREQSGEALADSQEVTAAMQQLlerEREATVERDELAARKQALESQIERLS 664
|
|
| Mpp10 |
COG5384 |
U3 small nucleolar ribonucleoprotein component [Translation, ribosomal structure and ... |
930-1349 |
9.24e-05 |
|
U3 small nucleolar ribonucleoprotein component [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227674 [Multi-domain] Cd Length: 569 Bit Score: 47.38 E-value: 9.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 930 EAELEKAAThrhSYEEKGRRYRDTVE------ERLSKLQKHNAElELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQK 1003
Cdd:COG5384 94 ESELEEAES---VFKEKQMLSADVSEieeqsnDSLSENDEEPSM-DDEKTSAEAAREEFAEEKRIPDPYGINDKFFDLEK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1004 EEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEfEKEIELLQA 1083
Cdd:COG5384 170 FNRDTLAAEDSNEASEGSEDEDIDYFQDMPSDDEEEEAIYYEDFFDKPTKEPVKKHSDVKDPKEDEELDE-EEHDSAMDK 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1084 QKIDVEKHVQSQKREmrERMSEVTKQLLESYDIEDVRSRLSVEDLEHLNEDGELWfAYEGLKKATRVLESHFQSqkdcye 1163
Cdd:COG5384 249 VKLDLFADEEDEPNA--EGVGEASDKNLSSFEKQQIEMDEQIEELEKELVAPKEW-KYAGEVSAKKRPKNSLLA------ 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1164 keiEGLNFKV------VHLSQEINHLQKLFREET------DINESIRHEVTRLT-SENMMIPDFKQQISELERQKQDL-- 1228
Cdd:COG5384 320 ---EELEFKQgakpvpVSTKEDTESLEDIILQRIregtfdDHAYRIREEVTIADeIPEFELLESKSILSLAEEYEGDLmq 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1229 ---ESRLKEQAEKIEGKLEEPFSHLNRIREEErmqgraveaqSEMH---PEGKERLVGAIHEPheAIKFPKKQPEAEEEV 1302
Cdd:COG5384 397 ivdESALSEELDKGHNEIFVLDSEIRMVLDTL----------KSLHsvpKPGAKSLEIIKNVP--TLKMEDAQPLYMSNA 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 124486759 1303 ESILQQEASRLSLEKRDLE-----------EELDMKDRMIRRLQDQVKTLTKTTEKAN 1349
Cdd:COG5384 465 SSLAPQEIYNVGKAEKDGEirlkngvamskEELTREDKNRLRRALKRKRSKANLPNVN 522
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
966-1270 |
1.03e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 47.16 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 966 AELELQRERaeqmLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEI-----------K 1034
Cdd:PLN03229 432 RELEGEVEK----LKEQILKAKESSSKPSELALNEMIEKLKKEIDLEYTEAVIAMGLQERLENLREEFskansqdqlmhP 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1035 ALKDERSQLHHQL-----EEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLqaqKIDVEKHVQS--QKREMRERM---- 1103
Cdd:PLN03229 508 VLMEKIEKLKDEFnkrlsRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKL---KAEINKKFKEvmDRPEIKEKMealk 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1104 SEVTKQLLESYDIEDvrsRLSVEDLEHLNEDGELWFAyEGLKKATRVLESHFQSQKDCYEKEI-EGLNFKVVHLSQEINH 1182
Cdd:PLN03229 585 AEVASSGASSGDELD---DDLKEKVEKMKKEIELELA-GVLKSMGLEVIGVTKKNKDTAEQTPpPNLQEKIESLNEEINK 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1183 LQKLFREETDIN---ESIRHEVTRLTSEnmmiPDF--KQQISELERQ-KQDL-----ESRLKEQAEKIEGKL---EEPFS 1248
Cdd:PLN03229 661 KIERVIRSSDLKskiELLKLEVAKASKT----PDVteKEKIEALEQQiKQKIaealnSSELKEKFEELEAELaaaRETAA 736
|
330 340
....*....|....*....|...
gi 124486759 1249 HLN-RIREEERMQGRAVEAQSEM 1270
Cdd:PLN03229 737 ESNgSLKNDDDKEEDSKEDGSRV 759
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
910-1086 |
1.04e-04 |
|
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: 47.06 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 910 EKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYE-EKGRRYRDTVEERLSKLQKHNAELELQRERAEQmlQEKSEELKE 988
Cdd:pfam09731 283 DDLNSLIAHAHREIDQLSKKLAELKKREEKHIERAlEKQKEELDKLAEELSARLEEVRAADEAQLRLEF--EREREEIRE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 989 KMDKLTRQLFDDVQKEEQQRLvlekGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEgqvtsdrLKGEVARLSKQA 1068
Cdd:pfam09731 361 SYEEKLRTELERQAEAHEEHL----KDVLVEQEIELQREFLQDIKEKVEEERAGRLLKLNE-------LLANLKGLEKAT 429
|
170
....*....|....*...
gi 124486759 1069 KTISEFEKEIelLQAQKI 1086
Cdd:pfam09731 430 SSHSEVEDEN--RKAQQL 445
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1129-1349 |
1.15e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.81 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1129 EHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLqklfREETDINESIRHEVTRLTSEn 1208
Cdd:pfam07888 38 ECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQS----REKHEELEEKYKELSASSEE- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1209 mmipdFKQQISELERQKQDLESRLKEQAEKIEGKLEEPfshLNRIREEERMQGRAVEAQSEMHPEGKERlvgaihephea 1288
Cdd:pfam07888 113 -----LSEEKDALLAQRAAHEARIRELEEDIKTLTQRV---LERETELERMKERAKKAGAQRKEEEAER----------- 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486759 1289 ikfpkKQPEAEEEVEsilQQEASRLSLEKRDLEEELDMKDRMIRRLQDQVKTLTKTTEKAN 1349
Cdd:pfam07888 174 -----KQLQAKLQQT---EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH 226
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
704-1359 |
1.20e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 704 TQQELSLSDKKEvcKVVLH--RLIQDSNQYQFGRTKIFFRagqvayleKLRLDKLRQDCIMIQKHVRGWLQRRKFLRERQ 781
Cdd:TIGR00618 282 TQERINRARKAA--PLAAHikAVTQIEQQAQRIHTELQSK--------MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLH 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 782 AALTIQRYFRGQQTVRKAITATALKE-----AWAAIIlqkycrgYLVRNLYQLIRVATITIQAHTRGFLARRRYRKLLQE 856
Cdd:TIGR00618 352 SQEIHIRDAHEVATSIREISCQQHTLtqhihTLQQQK-------TTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQG 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 857 HKAVI-----LQKYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEA 931
Cdd:TIGR00618 425 QLAHAkkqqeLQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPC 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 932 ELEKAATHRH-----SYE---------------EKGRRYRDTVEERLSKLQKHNAELELQRERA---EQMLQEKSEELKE 988
Cdd:TIGR00618 505 PLCGSCIHPNparqdIDNpgpltrrmqrgeqtyAQLETSEEDVYHQLTSERKQRASLKEQMQEIqqsFSILTQCDNRSKE 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 989 KMDKLtRQLFDDVQKEEQQRLVLEKgfelkTQAYEKQIESLREEIKALKDERSQLHHQLEEgqvtsdRLKGEVARLSKQA 1068
Cdd:TIGR00618 585 DIPNL-QNITVRLQDLTEKLSEAED-----MLACEQHALLRKLQPEQDLQDVRLHLQQCSQ------ELALKLTALHALQ 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1069 KTISEfEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSvEDLEHLnedGELWfayeglkkat 1148
Cdd:TIGR00618 653 LTLTQ-ERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLR-ELETHI---EEYD---------- 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1149 rvleSHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREetdinesirhevtrltsenmmipdfKQQISELERQKQDL 1228
Cdd:TIGR00618 718 ----REFNEIENASSSLGSDLAAREDALNQSLKELMHQART-------------------------VLKARTEAHFNNNE 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1229 ESRLKEQAEKIEGKLEEPFSHLNRIREEERMQGRAVEAQSEMH-PEGKERLVGAIHepheaikfpkKQPEAEEEVESILQ 1307
Cdd:TIGR00618 769 EVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEiPSDEDILNLQCE----------TLVQEEEQFLSRLE 838
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 124486759 1308 QEASRLSLEKRDLEEELDMKDRMIRRLQDQVKtLTKTTEKANHVHLPSGSRE 1359
Cdd:TIGR00618 839 EKSATLGEITHQLLKYEECSKQLAQLTQEQAK-IIQLSDKLNGINQIKIQFD 889
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
976-1347 |
1.56e-04 |
|
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: 46.64 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 976 EQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLE---KGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEG-Q 1051
Cdd:pfam05483 62 QEGLKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEaelKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEiQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1052 VTSDRLKGEVArlskqaktisefekeiellqaqkidvEKHVQSQKREMRERMSEVTKQllesYDIEDVRSRLSVEDLEHL 1131
Cdd:pfam05483 142 ENKDLIKENNA--------------------------TRHLCNLLKETCARSAEKTKK----YEYEREETRQVYMDLNNN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1132 NEDGELWFAYEGLKKATRVLESHFQSQKDcYEKeieglnfkvvhlsqeINHLQKLFREETDINES-IRHEVTRLTSENMM 1210
Cdd:pfam05483 192 IEKMILAFEELRVQAENARLEMHFKLKED-HEK---------------IQHLEEEYKKEINDKEKqVSLLLIQITEKENK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1211 IPDFKQQISELERQKQDLESRLKEQAEKIEgKLEEPFSHLNRIREEERMQ-GRAVEAQSEMhpegKERLVGAIHEPHEAI 1289
Cdd:pfam05483 256 MKDLTFLLEESRDKANQLEEKTKLQDENLK-ELIEKKDHLTKELEDIKMSlQRSMSTQKAL----EEDLQIATKTICQLT 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 124486759 1290 KFPKKQPEAEEEVESILQQEASRLSLEKRDLEEELDMKDRMIRRLQDQVKTLTKTTEK 1347
Cdd:pfam05483 331 EEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQK 388
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
870-1255 |
1.66e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.76 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 870 LARRRFQNIRRFVlnIQLTYRVQRLQKKLEDQ-NRENHGLVEKLTSLAA-LRVGDLEKVQKLEAELEKAATHRhsyEEKG 947
Cdd:pfam12128 643 FARTALKNARLDL--RRLFDEKQSEKDKKNKAlAERKDSANERLNSLEAqLKQLDKKHQAWLEEQKEQKREAR---TEKQ 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 948 RRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLtrqlfdDVqkEEQQRLVLEKGFELKTQAYEkQIE 1027
Cdd:pfam12128 718 AYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASL------GV--DPDVIAKLKREIRTLERKIE-RIA 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1028 SLREEIKALKD--------ERSQLHHQLEEGQVTSDRLKGEVARLSKQAKT-ISEFEKEIELLQAQKIDVEKHVQSQKRE 1098
Cdd:pfam12128 789 VRRQEVLRYFDwyqetwlqRRPRLATQLSNIERAISELQQQLARLIADTKLrRAKLEMERKASEKQQVRLSENLRGLRCE 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1099 MR------------ERMSEVTKQLLESYDIEDVRSRLSvEDLEHLNEDgelwFAYEGLKKATRVLESHFQSqkdcYEKEI 1166
Cdd:pfam12128 869 MSklatlkedanseQAQGSIGERLAQLEDLKLKRDYLS-ESVKKYVEH----FKNVIADHSGSGLAETWES----LREED 939
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1167 EGLNFKVVHLsqeiNHLQKLFREETDINESIRHEVTRLTSENMMIpdFKQQISELERQKQDLESRLKEQAEKIEGKLEEP 1246
Cdd:pfam12128 940 HYQNDKGIRL----LDYRKLVPYLEQWFDVRVPQSIMVLREQVSI--LGVDLTEFYDVLADFDRRIASFSRELQREVGEE 1013
|
....*....
gi 124486759 1247 fSHLNRIRE 1255
Cdd:pfam12128 1014 -AFFEGVSE 1021
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1004-1264 |
2.05e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1004 EEQQRLvlekgfeLKTQAYEKQIESLREEIKALKDERsqlhhqleegqvtsDRLKGEVARLSKQaktISEFEKEIELLQA 1083
Cdd:COG1579 4 EDLRAL-------LDLQELDSELDRLEHRLKELPAEL--------------AELEDELAALEAR---LEAAKTELEDLEK 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1084 QKIDVEKHVQsqkrEMRERMSEVTKQLLEsydiedVRSRLSVEDLEHlnedgELwfayEGLKKATRVLEshfqsqkdcyE 1163
Cdd:COG1579 60 EIKRLELEIE----EVEARIKKYEEQLGN------VRNNKEYEALQK-----EI----ESLKRRISDLE----------D 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1164 KEIEglnfkvvhLSQEINHLQKLFREETDINESIRHEVTRLTSEnmmipdFKQQISELERQKQDLESRLKEQAEKIEGKL 1243
Cdd:COG1579 111 EILE--------LMERIEELEEELAELEAELAELEAELEEKKAE------LDEELAELEAELEELEAEREELAAKIPPEL 176
|
250 260
....*....|....*....|.
gi 124486759 1244 eepFSHLNRIReeERMQGRAV 1264
Cdd:COG1579 177 ---LALYERIR--KRKNGLAV 192
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
884-1351 |
2.07e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.35 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 884 NIQLTYRVQRLQKKLEDQNRENHGLVEKLTS-------LAALRVGDLEKVQKLEAELEKAATH----RHSYEEKGRRY-- 950
Cdd:pfam10174 69 NQHLQLTIQALQDELRAQRDLNQLLQQDFTTspvdgedKFSTPELTEENFRRLQSEHERQAKElfllRKTLEEMELRIet 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 951 -------RD-TVEERLSKLQ----------------KHNAELELQRERAEQMLQEKSEELKEKMDKLTR--QLFDDVQKE 1004
Cdd:pfam10174 149 qkqtlgaRDeSIKKLLEMLQskglpkksgeedwertRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRrnQLQPDPAKT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1005 EQQRLVLEKGfELKTQAYEKQIESLREEIKALK-------DERSQLHHQLEEGQVTSDRLKGEVARL----SKQAKTISE 1073
Cdd:pfam10174 229 KALQTVIEMK-DTKISSLERNIRDLEDEVQMLKtngllhtEDREEEIKQMEVYKSHSKFMKNKIDQLkqelSKKESELLA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1074 FEKEIELLQAQKIDVEKHV-----------------QSQKREMRERMSEV-------TKQLLE--------SYDIEDVRS 1121
Cdd:pfam10174 308 LQTKLETLTNQNSDCKQHIevlkesltakeqraailQTEVDALRLRLEEKesflnkkTKQLQDlteekstlAGEIRDLKD 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1122 RLSVEDLEhlnedgelwfaYEGLKKATRVLeshfQSQKDCYEKEIEGLNFKVVHLSQEINH-------LQKLFREETDIN 1194
Cdd:pfam10174 388 MLDVKERK-----------INVLQKKIENL----QEQLRDKDKQLAGLKERVKSLQTDSSNtdtalttLEEALSEKERII 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1195 ESIRHEVTRLTSENM-MIPDFKQQISELERQKQDLESRLKEQAEKIEgKLEEPFSHLNRIREEERMQGRAVEAQSEMHPE 1273
Cdd:pfam10174 453 ERLKEQREREDRERLeELESLKKENKDLKEKVSALQPELTEKESSLI-DLKEHASSLASSGLKKDSKLKSLEIAVEQKKE 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1274 GKERLVGAIHEPHEAIKFPKKQPEAEEEVeSILQQEASRLSLEK--------------RDLEEELDMKDRMIRRLQD--- 1336
Cdd:pfam10174 532 ECSKLENQLKKAHNAEEAVRTNPEINDRI-RLLEQEVARYKEESgkaqaeverllgilREVENEKNDKDKKIAELESltl 610
|
570
....*....|....*.
gi 124486759 1337 -QVKTLTKTTEKANHV 1351
Cdd:pfam10174 611 rQMKEQNKKVANIKHG 626
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
890-1399 |
2.11e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.37 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 890 RVQRLQKKLEDQNRENHGLVEklTSLAALRvGDL----EKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQkhn 965
Cdd:pfam12128 280 ERQETSAELNQLLRTLDDQWK--EKRDELN-GELsaadAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQ--- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 966 AELELQRER------AEQMLQEKSEELKEKMD-KLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKA--- 1035
Cdd:pfam12128 354 SELENLEERlkaltgKHQDVTAKYNRRRSKIKeQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAgkl 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1036 -LKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKhVQSQKREMRERMSEVTKQL-LES 1113
Cdd:pfam12128 434 eFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVER-LQSELRQARKRRDQASEALrQAS 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1114 YDIEDVRSRLsvEDLEHLnedgelwfayegLKKATRVLESHFQSQKDCYEKEIEGLnfkvvhLSQEINHLQKLFREETDi 1193
Cdd:pfam12128 513 RRLEERQSAL--DELELQ------------LFPQAGTLLHFLRKEAPDWEQSIGKV------ISPELLHRTDLDPEVWD- 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1194 nESIRHEVT----RLTSENMMIPDFKQQISELERQKQDLESRLKEQAEKIEgKLEEPFSHLN-RIREEERMQGRAVEAQs 1268
Cdd:pfam12128 572 -GSVGGELNlygvKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQA-AAEEQLVQANgELEKASREETFARTAL- 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1269 emhpEGKERLVGAIHEPHEAIKFPKKQPEAEEE--VESILQQEASRLSLEKRDLEEELDMKDRMIRRLQDQVKTLTKTTE 1346
Cdd:pfam12128 649 ----KNARLDLRRLFDEKQSEKDKKNKALAERKdsANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVE 724
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 124486759 1347 KANHVHLPSGSREYLGMLEYKKEDEGKLIQNLILDLKPRGVVVNMIPGLPAHI 1399
Cdd:pfam12128 725 GALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREI 777
|
|
| Myo5p-like_CBD_Rasip1 |
cd15472 |
cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 ... |
1396-1675 |
2.14e-04 |
|
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: 45.73 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1396 PAHILFMCVRYADSLNDANMLKSLMNSAINGIKHVV----KE----HFE-----------------DLEMLSFWLSNT-- 1448
Cdd:cd15472 25 PAFLLCLCIQHSATHFEPGHFGKLLLKIAKRIQEIVwektKElaekQPEhqdpaslsllsiaelapDLQPLLFWMSNSie 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1449 --CHFLNCLKQYSGE-EEFMKYNSPQQNKNCLNNfDLTEYRQILSDVAIRIYHQFIIVMENNLQPIIvPGMLE------- 1518
Cdd:cd15472 105 llYFIQQKVPLYEQSmEEELDVGSKESLLSSTLT-ASEEAMTVLEEVIMYTFQQCVYYLTKTLYVAL-PALLDsnpftae 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1519 -YESLQGISGLkPTGFRKrsssiddtdaytMTSILQ---QLSyfysTMCQngLDPEIVRQAVKQLFYLVGAVTLNSLLLR 1594
Cdd:cd15472 183 eRESWSGGSRL-PEGVRR------------VLEIYQatlDLL----RQYQ--VHPEIASQMFAYLFFFSNASLFNQLMEK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1595 KDMCSC---RKGMQIRCNISFLEEWLKDKNVqSSLAKETLEPLSQAAWLLQVKKTTDSDAKEIAQCCT--SLSAVQIIKI 1669
Cdd:cd15472 244 GSGGGFfqwSRGVQIRANLDLLLDWLQGAGL-GDLAEEFFRKLSSTVNLLATPKEQLLQMSWSSLRAEfpALNPAQLHHL 322
|
....*.
gi 124486759 1670 LNSYTP 1675
Cdd:cd15472 323 LRQYQL 328
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
924-1082 |
2.56e-04 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 43.77 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 924 EKVQKLEAELEKAATHRHSY-EEKGRRYRDTVEERLSKLQKHNAEL-ELQRERAE--QMLQEKSEELKEKMDKLTRQlfd 999
Cdd:pfam08614 21 AENAKLQSEPESVLPSTSSSkLSKASPQSASIQSLEQLLAQLREELaELYRSRGElaQRLVDLNEELQELEKKLRED--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1000 dvqkeeqqrlvlekgfelktqayEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVA----RLSKQAKTISEFE 1075
Cdd:pfam08614 98 -----------------------ERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELValqlQLNMAEEKLRKLE 154
|
....*...
gi 124486759 1076 KE-IELLQ 1082
Cdd:pfam08614 155 KEnRELVE 162
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1195-1302 |
2.60e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1195 ESIRHEVTRLTSEnmmipdFKQQISELERQKQDLESRLKEQAEKI--EGKlEEPFSHLNRIREEERMQGRAVEAQ--SEM 1270
Cdd:PRK00409 540 EALLKEAEKLKEE------LEEKKEKLQEEEDKLLEEAEKEAQQAikEAK-KEADEIIKELRQLQKGGYASVKAHelIEA 612
|
90 100 110
....*....|....*....|....*....|..
gi 124486759 1271 HpegkeRLVGAIHEPHEAIKFPKKQPEAEEEV 1302
Cdd:PRK00409 613 R-----KRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
922-1129 |
2.70e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.29 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 922 DLEKVQKLEAELEKAATHRHSY----EEKGRRYRDTVEERlsklqKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQL 997
Cdd:pfam13868 4 NSDELRELNSKLLAAKCNKERDaqiaEKKRIKAEEKEEER-----RLDEMMEEERERALEEEEEKEEERKEERKRYRQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 998 FDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREE----IKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQA-KTIS 1072
Cdd:pfam13868 79 EEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEdqaeAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEdERIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 124486759 1073 EFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYD-IEDVRSRLSVEDLE 1129
Cdd:pfam13868 159 EYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAeRDELRAKLYQEEQE 216
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
875-1251 |
2.71e-04 |
|
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: 46.20 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 875 FQNIRRFVLNIQLTYR-VQRLQKKLED--QNRENHGLVEKLTSLAALRvGDLEKVQKLEAELEKAATHRHSYEEKGRRYR 951
Cdd:TIGR01612 1442 FKNADENNENVLLLFKnIEMADNKSQHilKIKKDNATNDHDFNINELK-EHIDKSKGCKDEADKNAKAIEKNKELFEQYK 1520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 952 DTVEERLSKLqkhnAELELQ------RERAEQMLQE----------KSEELKEKMDKLTRQLF---DDVQKEEQQ----- 1007
Cdd:TIGR01612 1521 KDVTELLNKY----SALAIKnkfaktKKDSEIIIKEikdahkkfilEAEKSEQKIKEIKKEKFrieDDAAKNDKSnkaai 1596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1008 --RLVLEKgFE---LKTQAYEKQIESLREEIKALKDERSQL-----HHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKE 1077
Cdd:TIGR01612 1597 diQLSLEN-FEnkfLKISDIKKKINDCLKETESIEKKISSFsidsqDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKE 1675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1078 IELLQAQ----KIDVEKHVQSQKREMRERMSEV----------TKQLLESyDIEDVRSRLSVEDLEHLNEDGElwfayeg 1143
Cdd:TIGR01612 1676 LDELDSEiekiEIDVDQHKKNYEIGIIEKIKEIaiankeeiesIKELIEP-TIENLISSFNTNDLEGIDPNEK------- 1747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1144 lkkatrvLESHFQSQKDCYEKEIEGLNFKVvhlsqeiNHLQKLFREETDINEsIRHevTRLTSENmmipDFKQQISELER 1223
Cdd:TIGR01612 1748 -------LEEYNTEIGDIYEEFIELYNIIA-------GCLETVSKEPITYDE-IKN--TRINAQN----EFLKIIEIEKK 1806
|
410 420
....*....|....*....|....*...
gi 124486759 1224 QKQDLESRLKEQAEKIEGKLEEPFSHLN 1251
Cdd:TIGR01612 1807 SKSYLDDIEAKEFDRIINHFKKKLDHVN 1834
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
924-1049 |
2.73e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 42.63 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 924 EKVQKLEAELEKAATHRHSYEEKGRRYRDTVEE--RLSK---------LQKHNAEL-ELQRERAE-QMLQEKSEELKEKM 990
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKqaEIAReaqqnyereLVLHAEDIkALQALREElNELKAEIAELKAEA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 124486759 991 DKLTRQLfddvqkeeqqrLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEE 1049
Cdd:pfam07926 81 ESAKAEL-----------EESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQLES 128
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
988-1122 |
2.76e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.84 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 988 EKMDKLTRQLfdDVQKEEQQRLVLEKgfelkTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQ 1067
Cdd:COG0542 411 EELDELERRL--EQLEIEKEALKKEQ-----DEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQR 483
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 124486759 1068 AKTISEFEKEIELLQAQKIDVEKHVQsqkremrermSEVTKQllesyDIEDVRSR 1122
Cdd:COG0542 484 YGKIPELEKELAELEEELAELAPLLR----------EEVTEE-----DIAEVVSR 523
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
924-1109 |
2.79e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 924 EKVQKLEAELEKAathrhsyEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQmLQEKSEELKEKMDKLTRQLFD---D 1000
Cdd:COG3883 23 KELSELQAELEAA-------QAELDALQAELEELNEEYNELQAELEALQAEIDK-LQAEIAEAEAEIEERREELGErarA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1001 VQKEEQQRLVLE-----KGFE--------LKT--QAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLS 1065
Cdd:COG3883 95 LYRSGGSVSYLDvllgsESFSdfldrlsaLSKiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 124486759 1066 KQaktISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQ 1109
Cdd:COG3883 175 AQ---QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
885-1349 |
2.87e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.94 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 885 IQLTYRVQRLQKKLEDQNRENHGLVEKLTSLaalrVGDLEKVQKLEAELEKAathRHSYEEKGRRYRDTVEERLSKLQ-K 963
Cdd:pfam01576 639 LSLARALEEALEAKEELERTNKQLRAEMEDL----VSSKDDVGKNVHELERS---KRALEQQVEEMKTQLEELEDELQaT 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 964 HNAELEL---------QRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQR---LVLEKGFELKTQAYEKQIESL-- 1029
Cdd:pfam01576 712 EDAKLRLevnmqalkaQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRaqaVAAKKKLELDLKELEAQIDAAnk 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1030 -REE-IKALKDERSQ---LHHQLEEGQVTSDRLKGEVARLSKQAKTIsefekEIELLQAQKI-----DVEKHVQSQKREM 1099
Cdd:pfam01576 792 gREEaVKQLKKLQAQmkdLQRELEEARASRDEILAQSKESEKKLKNL-----EAELLQLQEDlaaseRARRQAQQERDEL 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1100 RErmsEVTKQLLESYDIEDVRSRLS--VEDLEHLNEDgelwfayeglkkatrvLESHFQSQKDCYEK---EIEGLNfkvV 1174
Cdd:pfam01576 867 AD---EIASGASGKSALQDEKRRLEarIAQLEEELEE----------------EQSNTELLNDRLRKstlQVEQLT---T 924
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1175 HLSQEINHLQKlfreetdiNESIRhevtrltsenmmipdfkqqiSELERQKQDLESRLKEQAEKIEGKLEEPFSHLnrir 1254
Cdd:pfam01576 925 ELAAERSTSQK--------SESAR--------------------QQLERQNKELKAKLQEMEGTVKSKFKSSIAAL---- 972
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1255 eeermQGRAVEAQSEMHPEGKERLVGA--IHEPHEAIKFPKKQPEAE----EEVESILQQEASRLSLEKRDLEEELDMKD 1328
Cdd:pfam01576 973 -----EAKIAQLEEQLEQESRERQAANklVRRTEKKLKEVLLQVEDErrhaDQYKDQAEKGNSRMKQLKRQLEEAEEEAS 1047
|
490 500
....*....|....*....|....
gi 124486759 1329 RMI---RRLQDQVKTLTKTTEKAN 1349
Cdd:pfam01576 1048 RANaarRKLQRELDDATESNESMN 1071
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
924-1100 |
2.95e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 924 EKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELelqRERAEQMLQEKSEELKEKMDKLTRQLfddvqk 1003
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL---LEEAEKEAQQAIKEAKKEADEIIKEL------ 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1004 eeqQRLVLEKGFELKTQAYE---KQIESLREEIKALKDERSQLHHQLEEGQ---VTSDRLKGEVARLSKQAKTISEF--- 1074
Cdd:PRK00409 594 ---RQLQKGGYASVKAHELIearKRLNKANEKKEKKKKKQKEKQEELKVGDevkYLSLGQKGEVLSIPDDKEAIVQAgim 670
|
170 180 190
....*....|....*....|....*....|.
gi 124486759 1075 -----EKEIELLQAQKIDVEKHVQSQKREMR 1100
Cdd:PRK00409 671 kmkvpLSDLEKIQKPKKKKKKKPKTVKPKPR 701
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
881-1043 |
3.91e-04 |
|
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: 44.80 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 881 FVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKAathrHSYEEKGRRYR---DTVEER 957
Cdd:pfam15905 176 MAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITEL----SCVSEQVEKYKldiAQLEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 958 LSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLtrqlfddvqKEEQQRLVLEkgFELKTQAYEKQIESLREEIKALK 1037
Cdd:pfam15905 252 LKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLL---------ESEKEELLRE--YEEKEQTLNAELEELKEKLTLEE 320
|
....*.
gi 124486759 1038 DERSQL 1043
Cdd:pfam15905 321 QEHQKL 326
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
961-1030 |
4.25e-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: 44.11 E-value: 4.25e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124486759 961 LQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLFDD-----VQKEEQQRLVLEKGFELKTQAYEKQIESLR 1030
Cdd:cd16269 217 LEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEqeralESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
955-1341 |
4.35e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 955 EERLSKLQKHNAELELQRERAEQMLQEKSEE---LKEKMDKLTrQLFDDVQkEEQQRLVLEKG-FELKTQAYEKQIESLR 1030
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEknaLQEQLQAET-ELCAEAE-EMRARLAARKQeLEEILHELESRLEEEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1031 EEIKALKDERSQLHH-------QLEEGQVTSDRLKGEvaRLSKQAKtISEFEKEIELLQAQKIDVEKhvqsQKREMRERM 1103
Cdd:pfam01576 89 ERSQQLQNEKKKMQQhiqdleeQLDEEEAARQKLQLE--KVTTEAK-IKKLEEDILLLEDQNSKLSK----ERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1104 SEVTKQLLESYDIEDVRSRLS------VEDLE-HLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHL 1176
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKnkheamISDLEeRLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1177 SQEINHLQKLFREETDINESIRHEVTRLTSENM-MIPDF---KQQISELERQKQDLESRLKEQAEKIE------------ 1240
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISeLQEDLeseRAARNKAEKQRRDLGEELEALKTELEdtldttaaqqel 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1241 -GKLEEPFSHLNRIREEErmqGRAVEAQ-SEMhpegKERLVGAIHEPHEAIKFPKKQPEAEEEVESILQQEASRLSLEKR 1318
Cdd:pfam01576 322 rSKREQEVTELKKALEEE---TRSHEAQlQEM----RQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELR 394
|
410 420
....*....|....*....|...
gi 124486759 1319 DLEEELDMKDRMIRRLQDQVKTL 1341
Cdd:pfam01576 395 TLQQAKQDSEHKRKKLEGQLQEL 417
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
984-1335 |
5.48e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 984 EELKEKMDKLTRQLFDDvQKEEQQRL--VL----EKGFEL--KTQAYeKQIESLREEIKalkdersqlHHQLEEGQVTSD 1055
Cdd:COG4913 158 RALKARLKKQGVEFFDS-FSAYLARLrrRLgigsEKALRLlhKTQSF-KPIGDLDDFVR---------EYMLEEPDTFEA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1056 rlkgeVARLSKQAKTISEFEKEIELLQAQKidvekhvqsqkremrermsEVTKQLLESYD-IEDVRSRLSVedLEHLNED 1134
Cdd:COG4913 227 -----ADALVEHFDDLERAHEALEDAREQI-------------------ELLEPIRELAErYAAARERLAE--LEYLRAA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1135 GELWFAYEGLKKATRVLESHfqsqkdcyEKEIEGLNFKVVHLSQEINHLQklfREETDINESIR-HEVTRLTsenmmipD 1213
Cdd:COG4913 281 LRLWFAQRRLELLEAELEEL--------RAELARLEAELERLEARLDALR---EELDELEAQIRgNGGDRLE-------Q 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1214 FKQQISELERQKQDLESRLKEQAEKIEG-KLEEPFShlnriREE-ERMQGRAVEAQsemhpegkerlvgaihepheaikf 1291
Cdd:COG4913 343 LEREIERLERELEERERRRARLEALLAAlGLPLPAS-----AEEfAALRAEAAALL------------------------ 393
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 124486759 1292 pkkqpEAEEEVESILQQEASRLSLEKRDLEEELDMKDRMIRRLQ 1335
Cdd:COG4913 394 -----EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
924-1347 |
5.88e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 924 EKVQKLEAELEKAATHRHSYEEKGR-----RYRDTVEERLSKLQKHNAELELQRERAEQMLQEKseelKEKMDKLTRqlF 998
Cdd:TIGR00606 478 QELRKAERELSKAEKNSLTETLKKEvkslqNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT----KDKMDKDEQ--I 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 999 DDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEI 1078
Cdd:TIGR00606 552 RKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDV 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1079 ELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLS-------------------VEDLEH--LNEDGEL 1137
Cdd:TIGR00606 632 CGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqrvfqteaelqefISDLQSklRLAPDKL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1138 WFAYEGLKKATR------VLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHL---------------------------- 1183
Cdd:TIGR00606 712 KSTESELKKKEKrrdemlGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLkndieeqetllgtimpeeesakvcltdv 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1184 ---QKLFREETDINESIRHEVTRLTSEnmmipDFKQQISELERQKQDLESRLKEQAEKIE------GKLEEPFSHLNRIR 1254
Cdd:TIGR00606 792 timERFQMELKDVERKIAQQAAKLQGS-----DLDRTVQQVNQEKQEKQHELDTVVSKIElnrkliQDQQEQIQHLKSKT 866
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1255 EE---ERMQGRAVEAQSEMHPEGKERLVGAIHEPHEAIKFPKKQPEAEEEVESILQQEASRLSLEKRDLEEELDMKDRMI 1331
Cdd:TIGR00606 867 NElksEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDI 946
|
490
....*....|....*.
gi 124486759 1332 RRLQDQVKTLTKTTEK 1347
Cdd:TIGR00606 947 KEKVKNIHGYMKDIEN 962
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
954-1109 |
5.96e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 954 VEERLSKLQKHNAE------LELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEKQIE 1027
Cdd:PRK12704 24 VRKKIAEAKIKEAEeeakriLEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1028 SLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEiellQAQKIDVEKhvqsQKREMRERMSEVT 1107
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE----EAKEILLEK----VEEEARHEAAVLI 175
|
..
gi 124486759 1108 KQ 1109
Cdd:PRK12704 176 KE 177
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
960-1131 |
6.30e-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: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 960 KLQKHNAELELQRERAEQMLQEkSEELKEKMDKLtrqlfDDVQKEEQQRLVlekgfelktqAYEKQIESLREEIKALKDE 1039
Cdd:smart00787 120 QLVKTFARLEAKKMWYEWRMKL-LEGLKEGLDEN-----LEGLKEDYKLLM----------KELELLNSIKPKLRDRKDA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1040 RSQLHHQLEEG-----QVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQS---QKREMRERMSEVTKQLL 1111
Cdd:smart00787 184 LEEELRQLKQLedeleDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDltnKKSELNTEIAEAEKKLE 263
|
170 180
....*....|....*....|...
gi 124486759 1112 ES--YDIEDVRS-RLSVEDLEHL 1131
Cdd:smart00787 264 QCrgFTFKEIEKlKEQLKLLQSL 286
|
|
| MyosinXI_CBD |
cd15475 |
cargo binding domain of myosin XI; Class XI myosins are a plant specific group, homologous to ... |
1550-1702 |
7.80e-04 |
|
cargo binding domain of myosin XI; Class XI myosins are a plant specific group, homologous to class V myosins. C-terminal domain of Arabidopsis myosin XI has been shown to be homologous to the cargo-binding domain of yeast myosin V myo2p, which targets myosin to vacuole- and mitochondria, as well as secretory vesicle.
Pssm-ID: 271259 Cd Length: 326 Bit Score: 43.72 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1550 SILQQLSYFYSTMCQNGLDPEIVRQAVKQLFYLVGAVTLNSLLLRKDMCSCRKGMQIRCNISFLEEW---LKDKNVQSSL 1626
Cdd:cd15475 154 SIIKSLNSLLSTLKENHVPPFLVQKIFTQVFSFINVQLFNSLLLRRECCSFSNGEYVKAGLAELELWcsqATEEYAGSSW 233
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124486759 1627 akETLEPLSQAAWLLQVKKTTDSDAKEIAQ-CCTSLSAVQIIKILNSYTpIDDFEKR-VNPSFVRKVQALLNNRGDSA 1702
Cdd:cd15475 234 --DELKHIRQAVGFLVIHQKSRKSYDEITNdLCPVLSVQQLYRICTMYW-DDKYGTQsVSPEVISSMRVLMTEDSNNA 308
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
921-1112 |
8.17e-04 |
|
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: 44.17 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 921 GDLEKVQKLEAELEKAATHRHSYEEKGRRYR---DTVEERLSKLQKHNAELELQR-------ERAEQMLQEKSEELKEKM 990
Cdd:pfam15709 307 GNMESEEERSEEDPSKALLEKREQEKASRDRlraERAEMRRLEVERKRREQEEQRrlqqeqlERAEKMREELELEQQRRF 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 991 D--KLTRQLFDDvqkEEQQRLVLEKGFELKTQAYE----KQIESLREEIKALKDERSQlhHQLEEGQVTSDRLKGEVARL 1064
Cdd:pfam15709 387 EeiRLRKQRLEE---ERQRQEEEERKQRLQLQAAQerarQQQEEFRRKLQELQRKKQQ--EEAERAEAEKQRQKELEMQL 461
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 124486759 1065 SKQAKTISEFEKEIEL-LQAQKIDVEKHVQSQKREMRERMSEVTKQLLE 1112
Cdd:pfam15709 462 AEEQKRLMEMAEEERLeYQRQKQEAEEKARLEAEERRQKEEEAARLALE 510
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
890-1342 |
9.53e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 9.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 890 RVQRLQKKLEDQNRENHGLVEKLTSLAalrvgdlekvQKLEAELE---KAATHRHSYEEKGRRYRDTV---EERLSKLQK 963
Cdd:pfam01576 20 RQQKAESELKELEKKHQQLCEEKNALQ----------EQLQAETElcaEAEEMRARLAARKQELEEILhelESRLEEEEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 964 HNAELELQRERAEQMLQEKSEELKEKMDklTRqlfddvQKEEQQRLVLE---KGFELKTQAYEKQIESLREEIKALKDER 1040
Cdd:pfam01576 90 RSQQLQNEKKKMQQHIQDLEEQLDEEEA--AR------QKLQLEKVTTEakiKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1041 SQLHHQLEEGQ-----VTSDRLKGEVA------RLSKQAKTISEFEKEIELLQAQKIDvekhVQSQKREMRERMSEVTKQ 1109
Cdd:pfam01576 162 SEFTSNLAEEEekaksLSKLKNKHEAMisdleeRLKKEEKGRQELEKAKRKLEGESTD----LQEQIAELQAQIAELRAQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1110 LLESYD-IEDVRSRLSVEDLEHLNedgelwfayegLKKATRVLESH-------FQSQKDCYEK----------EIEGLNF 1171
Cdd:pfam01576 238 LAKKEEeLQAALARLEEETAQKNN-----------ALKKIRELEAQiselqedLESERAARNKaekqrrdlgeELEALKT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1172 KV--------------VHLSQEINHLQKLFREETDINES------IRHEvTRLTSENMMIPDFKQQISELERQKQDLESR 1231
Cdd:pfam01576 307 ELedtldttaaqqelrSKREQEVTELKKALEEETRSHEAqlqemrQKHT-QALEELTEQLEQAKRNKANLEKAKQALESE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1232 LKE-QAE----------------KIEGKLEEPFSHLNRI-REEERMQGRAVEAQSEMhpegkERLVGAIHEPH-EAIKFP 1292
Cdd:pfam01576 386 NAElQAElrtlqqakqdsehkrkKLEGQLQELQARLSESeRQRAELAEKLSKLQSEL-----ESVSSLLNEAEgKNIKLS 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486759 1293 KKQPEAE---EEVESILQQEA-SRLSL---------EKRDLEEELDMKDRMIRRLQDQVKTLT 1342
Cdd:pfam01576 461 KDVSSLEsqlQDTQELLQEETrQKLNLstrlrqledERNSLQEQLEEEEEAKRNVERQLSTLQ 523
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
891-1042 |
9.72e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 891 VQRLQKKLEDQNRENHGLVEKLTSLAAlRVGDLE-KVQKLEAELEKAAthRHSYEEKGRRyrDTVE-------------- 955
Cdd:COG3883 46 LEELNEEYNELQAELEALQAEIDKLQA-EIAEAEaEIEERREELGERA--RALYRSGGSV--SYLDvllgsesfsdfldr 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 956 -ERLSKLQKHNAEL--ELQRERAE-----QMLQEKSEELKEKMDKLTRQLFD-DVQKEEQQRLVleKGFELKTQAYEKQI 1026
Cdd:COG3883 121 lSALSKIADADADLleELKADKAEleakkAELEAKLAELEALKAELEAAKAElEAQQAEQEALL--AQLSAEEAAAEAQL 198
|
170
....*....|....*.
gi 124486759 1027 ESLREEIKALKDERSQ 1042
Cdd:COG3883 199 AELEAELAAAEAAAAA 214
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
890-1060 |
1.15e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 890 RVQRLQKKLED--QNRENH--GLVEKLTSLAALRvgdlEKVQKLEAELE---KAATHRHSYEEKGRRYR----------- 951
Cdd:PRK02224 510 RIERLEERREDleELIAERreTIEEKRERAEELR----ERAAELEAEAEekrEAAAEAEEEAEEAREEVaelnsklaelk 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 952 ------DTVEERLSKLQKHNAELELQRERAEQmLQEKSEELKEKMDKL---TRQLFDDVQ-------KEEQQRL------ 1009
Cdd:PRK02224 586 erieslERIRTLLAAIADAEDEIERLREKREA-LAELNDERRERLAEKrerKRELEAEFDearieeaREDKERAeeyleq 664
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486759 1010 VLEKGFELKTQAYE------------KQIESLREEIKALKDERSQL---HHQLEEGQVTSDRLKGE 1060
Cdd:PRK02224 665 VEEKLDELREERDDlqaeigavenelEELEELRERREALENRVEALealYDEAEELESMYGDLRAE 730
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
852-1166 |
1.21e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.88 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 852 KLLQEHKAVILQKYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEA 931
Cdd:TIGR00606 785 KVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKS 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 932 ELEKAATHRHSYEEKGRR---YRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRqlfddvqKEEQQR 1008
Cdd:TIGR00606 865 KTNELKSEKLQIGTNLQRrqqFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISS-------KETSNK 937
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1009 LVlekgfelktqayEKQIESLREEIKALKDERSQLHHQLEEGQvtSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDV 1088
Cdd:TIGR00606 938 KA------------QDKVNDIKEKVKNIHGYMKDIENKIQDGK--DDYLKQKETELNTVNAQLEECEKHQEKINEDMRLM 1003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1089 EKHVQSQKREMRERMSEVTKQLLESyDIEDVRSRLSVEDLEhLNEDG--ELWFAYEGLKKATRVL---ESHFQSQKDCYE 1163
Cdd:TIGR00606 1004 RQDIDTQKIQERWLQDNLTLRKREN-ELKEVEEELKQHLKE-MGQMQvlQMKQEHQKLEENIDLIkrnHVLALGRQKGYE 1081
|
...
gi 124486759 1164 KEI 1166
Cdd:TIGR00606 1082 KEI 1084
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
971-1330 |
1.24e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.32 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 971 QRERAEQMLQEKSEELKEKMDkltrqlfDDVQKEEQQRLVLEKGFELKTQAYEKQIESLREEIKALKDERSQlhhQLEEG 1050
Cdd:pfam02029 13 RRAREERRRQKEEEEPSGQVT-------ESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQK---RLQEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1051 QvtsDRLKGEVARLSKQAKTISEFEKEIELLQAQkiDVEKHVQSQKREMRERmsevtkqllesydiEDVRSRLSVEDLEH 1130
Cdd:pfam02029 83 L---ERQKEFDPTIADEKESVAERKENNEEEENS--SWEKEEKRDSRLGRYK--------------EEETEIREKEYQEN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1131 LNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEGLNFK---------VVHLSQEINHL-QKLFREETDINESIRHE 1200
Cdd:pfam02029 144 KWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKkekkvkyesKVFLDQKRGHPeVKSQNGEEEVTKLKVTT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1201 VTRLTSENMMIPDFK---------QQISELERQKQDLESrlkEQAEKIEGKLEEP---FSHLNRIREEERmqgRAVEaqs 1268
Cdd:pfam02029 224 KRRQGGLSQSQEREEeaevfleaeQKLEELRRRRQEKES---EEFEKLRQKQQEAeleLEELKKKREERR---KLLE--- 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486759 1269 emhpEGKERlvgaihepheaikfpKKQPEAEEEVesilqqeasRLSLEKRDLEEELDmKDRM 1330
Cdd:pfam02029 295 ----EEEQR---------------RKQEEAERKL---------REEEEKRRMKEEIE-RRRA 327
|
|
| K-box |
pfam01486 |
K-box region; The K-box region is commonly found associated with SRF-type transcription ... |
973-1048 |
1.31e-03 |
|
K-box region; The K-box region is commonly found associated with SRF-type transcription factors see pfam00319. The K-box is a possible coiled-coil structure. Possible role in multimer formation.
Pssm-ID: 460228 [Multi-domain] Cd Length: 91 Bit Score: 39.37 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 973 ERAEQMLQEKSEELKEKMDKLTRQL------------FDDVQKEEQQrlvLEKGF----ELKTQAYEKQIESLREEIKAL 1036
Cdd:pfam01486 3 ENEQENWQQEAAKLKKEIENLQRSQrqllgedlsslsLKELQQLEQQ---LEKSLkrirSRKNQLLLEQIEELKKKERIL 79
|
90
....*....|..
gi 124486759 1037 KDERSQLHHQLE 1048
Cdd:pfam01486 80 QEENKELRKKLE 91
|
|
| TBCA |
pfam02970 |
Tubulin binding cofactor A; |
1144-1241 |
1.50e-03 |
|
Tubulin binding cofactor A;
Pssm-ID: 460769 [Multi-domain] Cd Length: 99 Bit Score: 39.80 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1144 LKKATRVLEsHFQSQKDCYEKEIEglnfkvvhlsQEINHLQKLFREETDINEsIRHEVTRLTSENMMIPDFKQQISEler 1223
Cdd:pfam02970 6 LKIKTGVVK-RLVKEEASYEKELE----------EQEARLEKLKADGADEYD-LKKQEEVLEETKAMIPDLKKRLEE--- 70
|
90
....*....|....*...
gi 124486759 1224 QKQDLESRLKEQAEKIEG 1241
Cdd:pfam02970 71 AVEDLEEFLEEEEDLGAD 88
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
924-1085 |
1.71e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 924 EKVQKLEAELEKaathrhsyeekgrryrdTVEERLSKLQKhnaeLELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQK 1003
Cdd:PRK12704 64 EEIHKLRNEFEK-----------------ELRERRNELQK----LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1004 EEQqrlVLEKGFELKtQAYEKQIESLrEEIKAL-KDE-RSQLHHQLEEgqvtsdRLKGEVARLskqaktISEFEKEIElL 1081
Cdd:PRK12704 123 QQE---LEKKEEELE-ELIEEQLQEL-ERISGLtAEEaKEILLEKVEE------EARHEAAVL------IKEIEEEAK-E 184
|
....
gi 124486759 1082 QAQK 1085
Cdd:PRK12704 185 EADK 188
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
884-1110 |
1.72e-03 |
|
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: 42.03 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 884 NIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLaalrvgdlekvqKLEAELEKAATHRhsyeeKGRRYRDtVEERLSKLQK 963
Cdd:pfam17078 19 NLQLTVQSQNLLSKLEIAQQKESKFLENLASL------------KHENDNLSSMLNR-----KERRLKD-LEDQLSELKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 964 HNAELELQ----RERAEQmLQEKSEELKEKMDKLTRQLfdDVQKEEQQRLvlekgfelkTQAYEKQIESLREEIKALKDE 1039
Cdd:pfam17078 81 SYEELTESnkqlKKRLEN-SSASETTLEAELERLQIQY--DALVDSQNEY---------KDHYQQEINTLQESLEDLKLE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1040 rsqLHHQLEE-GQVTSDRLKGEVARLS------KQAKTISEfEKEIELLQ-----AQKIDVEKHVQSQKrEMRERMSEVT 1107
Cdd:pfam17078 149 ---NEKQLENyQQRISSNDKDIDTKLDsynnkfKNLDNIYV-NKNNKLLTkldslAQLLDLPSWLNLYP-ESRNKILEYA 223
|
...
gi 124486759 1108 KQL 1110
Cdd:pfam17078 224 EKM 226
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
887-1060 |
1.82e-03 |
|
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: 43.17 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 887 LTYRVQRLQKKLEDQNRENHGLVEKLTSLAA-LRVGDLeKVQKLEAELEKAathRHSYEEKGRRYRDTVEER-------L 958
Cdd:pfam05483 599 LKKQIENKNKNIEELHQENKALKKKGSAENKqLNAYEI-KVNKLELELASA---KQKFEEIIDNYQKEIEDKkiseeklL 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 959 SKLQKHNA----ELELQRErAEQMLQEKSEELKEKMDKLTRQlFDDVQKEEQQRLVLEKGfelKTQAYEKQIESLREEIK 1034
Cdd:pfam05483 675 EEVEKAKAiadeAVKLQKE-IDKRCQHKIAEMVALMEKHKHQ-YDKIIEERDSELGLYKN---KEQEQSSAKAALEIELS 749
|
170 180
....*....|....*....|....*.
gi 124486759 1035 ALKDERSQLHHQLEEGQVTSDRLKGE 1060
Cdd:pfam05483 750 NIKAELLSLKKQLEIEKEEKEKLKME 775
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
952-1062 |
1.85e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 952 DTVEERLSKLQKHNAELELQRERA----EQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKTQAYEK--Q 1025
Cdd:COG0542 407 DSKPEELDELERRLEQLEIEKEALkkeqDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRygK 486
|
90 100 110
....*....|....*....|....*....|....*..
gi 124486759 1026 IESLREEIKALKDERSQLHHQLEEgQVTSDrlkgEVA 1062
Cdd:COG0542 487 IPELEKELAELEEELAELAPLLRE-EVTEE----DIA 518
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
887-1110 |
2.00e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 42.75 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 887 LTYRVQRLQKKLEDQNRENHGLVEKLTSLAALrvgdlekVQKLEAELEKAATHRHSYEEKGRRYR---DTVEERLSKLQK 963
Cdd:pfam19220 88 LVARLAKLEAALREAEAAKEELRIELRDKTAQ-------AEALERQLAAETEQNRALEEENKALReeaQAAEKALQRAEG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 964 HNAELELQRERAEQ---MLQEKSEELKEKMDKLTRQLFDDVQKEEQQR---LVLEKGFELKTQAYEKQIESLREEIKALK 1037
Cdd:pfam19220 161 ELATARERLALLEQenrRLQALSEEQAAELAELTRRLAELETQLDATRarlRALEGQLAAEQAERERAEAQLEEAVEAHR 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1038 DERSQLHHQLEEGQ---VTSDRLKGEVA---------------RLSKQAKTISEFEKEIELLQAQKIDVE---KHVQSQK 1096
Cdd:pfam19220 241 AERASLRMKLEALTaraAATEQLLAEARnqlrdrdeairaaerRLKEASIERDTLERRLAGLEADLERRTqqfQEMQRAR 320
|
250
....*....|....
gi 124486759 1097 REMRERMSEVTKQL 1110
Cdd:pfam19220 321 AELEERAEMLTKAL 334
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
852-1127 |
2.01e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.11 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 852 KLLQEHKAVILQKYA--RAWL------ARRRFQNIRRFVLNIqltyrvqrLQKKLEDQNRENHGLVEKLTSLAALRVGDL 923
Cdd:PTZ00108 980 DILKEFYLVRLDLYKkrKEYLlgklerELARLSNKVRFIKHV--------INGELVITNAKKKDLVKELKKLGYVRFKDI 1051
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 924 EKVQK---LEAELEKAATHRHSYEEKGRRYRDTVEE------------RLSKLQKHNAELELQRERAEQMLQEKSEEL-K 987
Cdd:PTZ00108 1052 IKKKSekiTAEEEEGAEEDDEADDEDDEEELGAAVSydyllsmpiwslTKEKVEKLNAELEKKEKELEKLKNTTPKDMwL 1131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 988 EKMDKLTRQLFDDVQKEEQQRLVLEKgFELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRlKGEVARLSKQ 1067
Cdd:PTZ00108 1132 EDLDKFEEALEEQEEVEEKEIAKEQR-LKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSK-RVDSDEKRKL 1209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1068 AKTISEFEKEIELLQAQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRSRLSVED 1127
Cdd:PTZ00108 1210 DDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEG 1269
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1217-1347 |
2.11e-03 |
|
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: 43.13 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1217 QISELERQKQDLESRLKEQAEKIEgKLEEPFSHLNRiREEERMQGRAVEAQSEMHpegkeRLVGAIHEPHEAIKFPKKQP 1296
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLE-EIEQLLEELNK-KIKDLGEEEQLRVKEKIG-----ELEAEIASLERSIAEKEREL 317
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 124486759 1297 EAEEEVESILQQEASRLSLEKRDLEEELDMKDRMIRRLQDQVKTLTKTTEK 1347
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED 368
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
895-1350 |
2.16e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 895 QKKLEDQNRE------NHGLVE-KLTSLAALRVGDL-EKVQKLEAELEKaathrhSYEEKGRRYrdTVEErlSKLQKHNA 966
Cdd:pfam12128 353 QSELENLEERlkaltgKHQDVTaKYNRRRSKIKEQNnRDIAGIKDKLAK------IREARDRQL--AVAE--DDLQALES 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 967 ELELQRERAEQMLQEKSEELKEKMDKLTRQLfDDVQKEEQQRLVLEKGFELKTQAYEKQiESLREEIKALKDERSQL--- 1043
Cdd:pfam12128 423 ELREQLEAGKLEFNEEEYRLKSRLGELKLRL-NQATATPELLLQLENFDERIERAREEQ-EAANAEVERLQSELRQArkr 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1044 ------HHQLEEGQVtsDRLKGEVAR----LSKQAKTISEF-EKEIEL-------------------------------- 1080
Cdd:pfam12128 501 rdqaseALRQASRRL--EERQSALDElelqLFPQAGTLLHFlRKEAPDweqsigkvispellhrtdldpevwdgsvggel 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1081 ------LQAQKIDVEKHVQSQKrEMRERMSEVTKQLLESYD-IEDVRSRLSVEDLEHLNEDGELWFAYEGLKKAT---RV 1150
Cdd:pfam12128 579 nlygvkLDLKRIDVPEWAASEE-ELRERLDKAEEALQSAREkQAAAEEQLVQANGELEKASREETFARTALKNARldlRR 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1151 LESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQK-LFREETDINESIRHEVTRLTSENMmipdfkQQISELERQKQDLE 1229
Cdd:pfam12128 658 LFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKqLDKKHQAWLEEQKEQKREARTEKQ------AYWQVVEGALDAQL 731
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1230 SRLKEQAEKIEGKLEEPFSHLNRIREEErMQGRAVEaqsemhPEGKERLVGAIHEPHEAIKFPKKQPEAEEEVESILQ-- 1307
Cdd:pfam12128 732 ALLKAAIAARRSGAKAELKALETWYKRD-LASLGVD------PDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQet 804
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 124486759 1308 --QEASRLSLEKRDLEEELDMKDRMIRRLQDQVKTLTKTTEKANH 1350
Cdd:pfam12128 805 wlQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERK 849
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1005-1337 |
2.51e-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: 42.50 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1005 EQQRLVLEKgfelkTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSD--------------RLKGEVARLSKQ--- 1067
Cdd:pfam10174 60 EQYRVTQEE-----NQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEdkfstpelteenfrRLQSEHERQAKElfl 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1068 -AKTISEFEKEIEL----LQAQKIDVEK---HVQSQ---------KREMRERMSEVTKQ------LLESYDIEDVRSRLS 1124
Cdd:pfam10174 135 lRKTLEEMELRIETqkqtLGARDESIKKlleMLQSKglpkksgeeDWERTRRIAEAEMQlghlevLLDQKEKENIHLREE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1125 VEDLEHLNEDGELWFAYE-----------GLKKATRVLESHFQSQK-----DCYEKEIEGLNFKVVH-----LSQEINHL 1183
Cdd:pfam10174 215 LHRRNQLQPDPAKTKALQtviemkdtkisSLERNIRDLEDEVQMLKtngllHTEDREEEIKQMEVYKshskfMKNKIDQL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1184 -QKLFREETDInESIRHEVTRLTSENmmiPDFKQQISELERQKQDLESR---LKEQAEKIEGKLEEPFSHLN-------R 1252
Cdd:pfam10174 295 kQELSKKESEL-LALQTKLETLTNQN---SDCKQHIEVLKESLTAKEQRaaiLQTEVDALRLRLEEKESFLNkktkqlqD 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1253 IREEERMQGRAVEAQSEMHpEGKERLVGAIHEP----HEAIKFPKKQPEAEEEVESILQQEASRLSLEKRDLEEELDMKD 1328
Cdd:pfam10174 371 LTEEKSTLAGEIRDLKDML-DVKERKINVLQKKienlQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKE 449
|
....*....
gi 124486759 1329 RMIRRLQDQ 1337
Cdd:pfam10174 450 RIIERLKEQ 458
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
979-1185 |
2.57e-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: 41.29 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 979 LQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEkgfelktQAYEKQIESLREEIKALKDERSQLHHQLEEGQvtsdrlk 1058
Cdd:pfam14988 9 LAKKTEEKQKKIEKLWNQYVQECEEIERRRQELA-------SRYTQQTAELQTQLLQKEKEQASLKKELQALR------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1059 gEVARLSKQAktisefEKEIELLQAQKIDVEKHVQSQKREMRERMSEvTKQLLESyDIEDVRSRLSVEDLEHlnedgELW 1138
Cdd:pfam14988 75 -PFAKLKESQ------EREIQDLEEEKEKVRAETAEKDREAHLQFLK-EKALLEK-QLQELRILELGERATR-----ELK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 124486759 1139 FAYEGLK-KATRVLESHFQSQKdcyeKEIEGLNFKVVHLSQEINHLQK 1185
Cdd:pfam14988 141 RKAQALKlAAKQALSEFCRSIK----RENRQLQKELLQLIQETQALEA 184
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
983-1084 |
2.93e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 983 SEEL--KEK-MDKLTRQLfddvqKEEQQRLVLEKgfeLKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKG 1059
Cdd:PRK09039 45 SREIsgKDSaLDRLNSQI-----AELADLLSLER---QGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEG 116
|
90 100
....*....|....*....|....*....
gi 124486759 1060 EVARLSKQ---AKTIS-EFEKEIELLQAQ 1084
Cdd:PRK09039 117 RAGELAQEldsEKQVSaRALAQVELLNQQ 145
|
|
| IQ |
pfam00612 |
IQ calmodulin-binding motif; Calmodulin-binding motif. |
831-851 |
3.18e-03 |
|
IQ calmodulin-binding motif; Calmodulin-binding motif.
Pssm-ID: 459869 Cd Length: 21 Bit Score: 36.53 E-value: 3.18e-03
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
747-1069 |
3.26e-03 |
|
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: 42.27 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 747 YLEKLRLDKLRQDCIMIQKHVRGWLQRRKFLRERQAALTIQRYFRGQQTVRKAITATALKEAWAAIILQKYCRGYLVRNL 826
Cdd:pfam02463 695 LRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEK 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 827 YqLIRVATITIQAHTRGFLARRRYRKLLQEHKAVILQKYARAWLarRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENH 906
Cdd:pfam02463 775 E-LAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL--EEEQLLIEQEEKIKEEELEELALELKEEQKLEKL 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 907 GLVEKLTSLAALRVGDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQE----- 981
Cdd:pfam02463 852 AEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEaeill 931
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 982 ----KSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFELKtqayEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRL 1057
Cdd:pfam02463 932 kyeeEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEEL----GKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKL 1007
|
330
....*....|..
gi 124486759 1058 KGEVARLSKQAK 1069
Cdd:pfam02463 1008 IRAIIEETCQRL 1019
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
921-1311 |
3.43e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 921 GDLEKVQKLEAELEKAATHRHSYEEKGRRYRDTVEERLsKLQKHNAElELQRERAE-------------------QMLQE 981
Cdd:PRK01156 360 GYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEIL-KIQEIDPD-AIKKELNEinvklqdisskvsslnqriRALRE 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 982 KSEELKEKMDKLTRQ-----LFDDVQKEEQQRLVleKGFELKTQAYEKQIESLREEIKALKDERSQL---HHQLEEGQVt 1053
Cdd:PRK01156 438 NLDELSRNMEMLNGQsvcpvCGTTLGEEKSNHII--NHYNEKKSRLEEKIREIEIEVKDIDEKIVDLkkrKEYLESEEI- 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1054 sDRLKGEVARLSKQAKTISEFEKEIELLqAQKIDVEKHVQSQKREM-----RERMSEVTKQL--LESYDIEDVRSRlSVE 1126
Cdd:PRK01156 515 -NKSINEYNKIESARADLEDIKIKINEL-KDKHDKYEEIKNRYKSLkledlDSKRTSWLNALavISLIDIETNRSR-SNE 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1127 DLEHLNEdgelwfayegLKKATRVLESHFQSQKDCYEKEIEGLNFKVVHLSQEINHLQKLFREETDINESIRHEVTRLTS 1206
Cdd:PRK01156 592 IKKQLND----------LESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAE 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1207 ENMMIPDFKqqisELERQKQDLESRLKeqaeKIEGKLEEPFSHLNRIREEERMQGRAVEAQSEMHPEGKERLvGAIHEPH 1286
Cdd:PRK01156 662 IDSIIPDLK----EITSRINDIEDNLK----KSRKALDDAKANRARLESTIEILRTRINELSDRINDINETL-ESMKKIK 732
|
410 420
....*....|....*....|....*..
gi 124486759 1287 EAIKFPKKQPEA--EEEVESILQQEAS 1311
Cdd:PRK01156 733 KAIGDLKRLREAfdKSGVPAMIRKSAS 759
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
830-851 |
3.54e-03 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 36.53 E-value: 3.54e-03
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
924-1053 |
3.63e-03 |
|
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: 39.13 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 924 EKVQKLEAELEKAATHRHSYEEKGRRYrdtvEERLSKLQKHNAELELQRERAEQMlQEKSEELKEKmdkltrqlfddvQK 1003
Cdd:pfam20492 13 ERLKQYEEETKKAQEELEESEETAEEL----EEERRQAEEEAERLEQKRQEAEEE-KERLEESAEM------------EA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 124486759 1004 EEQQRLvlekgfELKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVT 1053
Cdd:pfam20492 76 EEKEQL------EAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREE 119
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
995-1373 |
3.98e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 995 RQLFDDVQKEEQQRLVLEKgfelktqayekqieslreEIKALKDERSQlhhQLEEGQvtsdrlKGEVARLSKQAKTISEF 1074
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEK------------------EEKAREVERRR---KLEEAE------KARQAEMDRQAAIYAEQ 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1075 EKeiellqaQKIDVEKHVQSQKREMRERMSEVTKQLLESYDIEDVRsrlsveDLEHLNedgelwfaYEGLKKATRVlesh 1154
Cdd:pfam17380 340 ER-------MAMERERELERIRQEERKRELERIRQEEIAMEISRMR------ELERLQ--------MERQQKNERV---- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1155 fqsqkdcyEKEIEGLNfKVVHLSQEinhLQKLFREETDINESIRhevtrltsenmmipdfKQQISELERQKQDLESRLKE 1234
Cdd:pfam17380 395 --------RQELEAAR-KVKILEEE---RQRKIQQQKVEMEQIR----------------AEQEEARQREVRRLEEERAR 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1235 QAEKIEGKLEEPFSHLNRIREEERMQGRAV-------EAQSEMHPEGKERLVGAIHEPHEAIKFPKK-----QPEAEEEV 1302
Cdd:pfam17380 447 EMERVRLEEQERQQQVERLRQQEEERKRKKlelekekRDRKRAEEQRRKILEKELEERKQAMIEEERkrkllEKEMEERQ 526
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486759 1303 ESILQQEASRLSLEKRDLEEEldMKDRmiRRLQDQVKtltKTTEKANHVHLPSGSREylgMLEYKKEDEGK 1373
Cdd:pfam17380 527 KAIYEEERRREAEEERRKQQE--MEER--RRIQEQMR---KATEERSRLEAMERERE---MMRQIVESEKA 587
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
896-1202 |
5.05e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 896 KKLEDQNRENHGLVEKLTSLAAlrvgDLEKVQKL--------------------EAELEKAATHR-------HSYEEKGR 948
Cdd:PRK04863 786 KRIEQLRAEREELAERYATLSF----DVQKLQRLhqafsrfigshlavafeadpEAELRQLNRRRveleralADHESQEQ 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 949 RYR---DTVEERLSKLQKHNAELELQrerAEQMLQEKSEELKEKMDKLtrqlfddvqkEEQQRLVLEKGFELktQAYEKQ 1025
Cdd:PRK04863 862 QQRsqlEQAKEGLSALNRLLPRLNLL---ADETLADRVEEIREQLDEA----------EEAKRFVQQHGNAL--AQLEPI 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1026 IESLR---EEIKALKDERSQLHHQLEEGQVTSDRLKGEVARL-----SKQAKTISEFEKEIELLQAQkidvEKHVQSQKR 1097
Cdd:PRK04863 927 VSVLQsdpEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRahfsyEDAAEMLAKNSDLNEKLRQR----LEQAEQERT 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1098 EMRERMSEVTKQLLEsYD--IEDVRSRLSV-EDL--EHLNEDGELWFAY-EGLKKATRVLE-------SHFQSQKDCYEK 1164
Cdd:PRK04863 1003 RAREQLRQAQAQLAQ-YNqvLASLKSSYDAkRQMlqELKQELQDLGVPAdSGAEERARARRdelharlSANRSRRNQLEK 1081
|
330 340 350
....*....|....*....|....*....|....*...
gi 124486759 1165 EIeglnfkvVHLSQEINHLQKLFREETDINESIRHEVT 1202
Cdd:PRK04863 1082 QL-------TFCEAEMDNLTKKLRKLERDYHEMREQVV 1112
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
904-1036 |
6.52e-03 |
|
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: 39.80 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 904 ENHGLVEKLTSLAALrvgDLEKVQKLEAELEKaathRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKS 983
Cdd:pfam06785 66 EKSFLEEKEAKLTEL---DAEGFKILEETLEE----LQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFR 138
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 124486759 984 EELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFElKTQAYEKQIESLREEIKAL 1036
Cdd:pfam06785 139 LESEEQLAEKQLLINEYQQTIEEQRSVLEKRQD-QIENLESKVRDLNYEIKTL 190
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
884-1058 |
6.93e-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: 41.35 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 884 NIQLTYRVQRLQKKL---EDQNRENHGLVEKLtsLAALRVGDLEKVQKLE--AELEKAATHRHSYEEKGRRYRDTVEERL 958
Cdd:pfam10174 553 NPEINDRIRLLEQEVaryKEESGKAQAEVERL--LGILREVENEKNDKDKkiAELESLTLRQMKEQNKKVANIKHGQQEM 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 959 SKlqKHNAELELQRERAEQM----LQEKSEELKEKMDKlTRQLFDDVQKE---EQQRLV----------------LEKGF 1015
Cdd:pfam10174 631 KK--KGAQLLEEARRREDNLadnsQQLQLEELMGALEK-TRQELDATKARlssTQQSLAekdghltnlraerrkqLEEIL 707
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1016 ELKTQAYEKQI-----------------ESLREEIKALKDERSQLHHQLEegQVTSDRLK 1058
Cdd:pfam10174 708 EMKQEALLAAIsekdaniallelssskkKKTQEEVMALKREKDRLVHQLK--QQTQNRMK 765
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
896-1079 |
7.77e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 896 KKLEDQNRENHGLVEKLTSLAALRvgdLEKVQKLEAELEKAathrhsyEEKGRRYRDTVEERLSKLQKHNAELELQRera 975
Cdd:TIGR04523 499 KKLNEEKKELEEKVKDLTKKISSL---KEKIEKLESEKKEK-------ESKISDLEDELNKDDFELKKENLEKEIDE--- 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 976 eqmLQEKSEELKEKMDKLTR---QLFDDVQKEEQQRLVLEKGFELKtqayEKQIESLREEIKALKDERSQLHHQLEEGQV 1052
Cdd:TIGR04523 566 ---KNKEIEELKQTQKSLKKkqeEKQELIDQKEKEKKDLIKEIEEK----EKKISSLEKELEKAKKENEKLSSIIKNIKS 638
|
170 180
....*....|....*....|....*..
gi 124486759 1053 TSDRLKGEVARLSKQAKTISEFEKEIE 1079
Cdd:TIGR04523 639 KKNKLKQEVKQIKETIKEIRNKWPEII 665
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
780-1129 |
7.91e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 41.05 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 780 RQAALTIQRYFRGQQT---VRKAITATALKEAWAAIILQKYCRGYLVRNLYQLIRVATITIQAHTRGFLARRRYRKLLQE 856
Cdd:COG5278 135 LEAALALVRSGEGKALmdeIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 857 HKAVILQKYARAWLARRRFQNIRRFVLNIQLTYRVQRLQKKLEDQNRENHGLVEKLTSLAALRVGDLEKVQKLEAELEKA 936
Cdd:COG5278 215 AAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 937 ATHRHSYEEKGRRYRDTVEERLSKLQKHNAELELQRERAEQMLQEKSEELKEKMDKLTRQLFDDVQKEEQQRLVLEKGFE 1016
Cdd:COG5278 295 EALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALA 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1017 LKTQAYEKQIESLREEIKALKDERSQLHHQLEEGQVTSDRLKGEVARLSKQAKTISEFEKEIELLQAQKIDVEKHVQSQK 1096
Cdd:COG5278 375 GLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGA 454
|
330 340 350
....*....|....*....|....*....|...
gi 124486759 1097 REMRERMSEVTKQLLESYDIEDVRSRLSVEDLE 1129
Cdd:COG5278 455 ALALAAAEALAEELAAVAALAALAAAAAALAEA 487
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1188-1390 |
8.06e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1188 REETDINESIRHEVTRLTSENMMIPDFKQQISELERQKQDLESRLKEQAEKIEgKLEEpfsHLNRIREEERMQGRAveaq 1267
Cdd:COG2433 392 EEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIE-RLER---ELSEARSEERREIRK---- 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1268 semhpegkerlvgaihepheaikfpkkqpeaEEEVeSILQQEASRLsleKRDLEEELDMKDRMIRRLqDQVKTLTKTTEK 1347
Cdd:COG2433 464 -------------------------------DREI-SRLDREIERL---ERELEEERERIEELKRKL-ERLKELWKLEHS 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 124486759 1348 ANHV---HLPSGSREYLGMLE----YKKED---------EGKLIQNLILDLKPRGVVVN 1390
Cdd:COG2433 508 GELVpvkVVEKFTKEAIRRLEeeygLKEGDvvylrdasgAGRSTAELLAEAGPRAVIVP 566
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1097-1240 |
8.20e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1097 REMRERMSEVTKQLLESYDIEDVRSR----LSVED-LEHLNEDGElwfayEGLKKATRVLESHFQSQKDCYEKEIEGLNF 1171
Cdd:COG2433 346 DAYKNKFERVEKKVPPDVDRDEVKARvirgLSIEEaLEELIEKEL-----PEEEPEAEREKEHEERELTEEEEEIRRLEE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1172 KVVHLSQEINHLQ-----------------KLFREETDINESIRHEVTRLTSEnmmipdfkqqISELERQKQDLESRLKE 1234
Cdd:COG2433 421 QVERLEAEVEELEaeleekderierlerelSEARSEERREIRKDREISRLDRE----------IERLERELEEERERIEE 490
|
....*.
gi 124486759 1235 QAEKIE 1240
Cdd:COG2433 491 LKRKLE 496
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1220-1339 |
8.56e-03 |
|
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: 37.98 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486759 1220 ELERQKQDLESRLK---EQAEKIEGKLEEpfsHLNRIRE-EERMQgravEAQsemhpegkerlvgaihepHEAIKFPKKQ 1295
Cdd:pfam20492 3 EAEREKQELEERLKqyeEETKKAQEELEE---SEETAEElEEERR----QAE------------------EEAERLEQKR 57
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 124486759 1296 PEAEEEVESiLQQEASRLSLEKRDLEEELDMKDRMIRRLQDQVK 1339
Cdd:pfam20492 58 QEAEEEKER-LEESAEMEAEEKEQLEAELAEAQEEIARLEEEVE 100
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
926-995 |
9.23e-03 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 37.95 E-value: 9.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486759 926 VQKLEAELEKAATHRHSYEEKGRRYRDTV--EERLSK-LQKHNAELElqreRAEQMLQEKSEELKEKMDKLTR 995
Cdd:pfam18595 49 LAKLEEAKKKLKELRDALEEKEIELRELErrEERLQRqLENAQEKLE----RLREQAEEKREAAQARLEELRE 117
|
|
| |
