|
Name |
Accession |
Description |
Interval |
E-value |
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
2-1691 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 1400.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 2 TGGQSCSSNMIVWIPDEKEVFVKGELMSTDINKNKFTGQEEQIGIvhPLDSTEVSNLVQVRIsdvfpvNPSTFDKVENMS 81
Cdd:COG5022 1 MSTTNAEVGSGCWIPDEEKGWIWAEIIKEAFNKGKVTEEGKKEDG--ESVSVKKKVLGNDRI------KLPKFDGVDDLT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 82 ELTHLNEPSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKHnrlsksrldensHEKLPPHIFAIAE 161
Cdd:COG5022 73 ELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKN------------RLELEPHVFAIAE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 162 EAYENLLSEGKDQSILVTGESGAGKTENTKKILQYLASITSGSpsniapvsgSSIVESFEMKILQSNPILESFGNAQTVR 241
Cdd:COG5022 141 EAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSS---------TVEISSIEKQILATNPILEAFGNAKTVR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 242 NNNSSRFGKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGlDDSELKNLRLkSRNVKDYKILSNS 321
Cdd:COG5022 212 NDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAG-DPEELKKLLL-LQNPKDYIYLSQG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 322 NQDIIPGINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAEQASFKND--VSAICSNLGVDEKDFQ 399
Cdd:COG5022 290 GCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRNGAAIFSDNsvLDKACYLLGIDPSLFV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 400 TAILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENNSFEQL 479
Cdd:COG5022 370 KWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQL 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 480 CINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIESKGPPtGVLPLLDEEAVLPKSTDESFYSKLI 559
Cdd:COG5022 450 CINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY-FDNQPCIDLIEKKNPL-GILSLLDEECVMPHATDESFTSKLA 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 560 STWDQNSS-KFKRSRLK-NGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQpegeksssagVEAN 637
Cdd:COG5022 528 QRLNKNSNpKFKKSRFRdNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFD----------DEEN 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 638 ISNQevkksartSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGY 717
Cdd:COG5022 598 IESK--------GRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGF 669
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 718 PNRIAFQEFFQRYRILYPENSTTTTFSSklKASTKQNCEFLLTSLQLDTKVYKIGNTKLFFKAGVLADLEKQKDVKLNNI 797
Cdd:COG5022 670 PSRWTFDEFVQRYRILSPSKSWTGEYTW--KEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNI 747
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 798 MIKLTATIRGYTVRKEITYHLQKLKKTRVIGNTFRLYnRLVKEDPWFNLFIRIKPLLTSSNDMTRTKKFNEQINKLKNdl 877
Cdd:COG5022 748 ATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLR-RLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQK-- 824
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 878 qemeskkkflEEKNQKTVNElentqdllNQEKENLRKNESLLNRVkTSSETLQKQFDDLvsEKDEISrekLEVAQNLEEA 957
Cdd:COG5022 825 ----------TIKREKKLRE--------TEEVEFSLKAEVLIQKF-GRSLKAKKRFSLL--KKETIY---LQSAQRVELA 880
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 958 HQKIQGLQETIREreatLEKLHSKNNELIKQISDLNCDISKeqssqSLIKESKLKLEnEIKRLKDVINSkeeeiksfndk 1037
Cdd:COG5022 881 ERQLQELKIDVKS----ISSLKLVNLELESEIIELKKSLSS-----DLIENLEFKTE-LIARLKKLLNN----------- 939
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1038 lSSSEEDLDIKLVTLEkncniamsRLQSLVTENSDLRSKNENFKkekaALNNQLKNKESELLKMKEKIDNHKKELATFSK 1117
Cdd:COG5022 940 -IDLEEGPSIEYVKLP--------ELNKLHEVESKLKETSEEYE----DLLKKSTILVREGNKANSELKNFKKELAELSK 1006
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1118 QRdDAVSEHgkiTAELKETRIQLTEYKSNYQKIKEEYSNFQRETKEQEqkkrnslVESLNDSKIKELEARLsqeislnqy 1197
Cdd:COG5022 1007 QY-GALQES---TKQLKELPVEVAELQSASKIISSESTELSILKPLQK-------LKGLLLLENNQLQARY--------- 1066
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1198 lnkrisgnsvetnisstrrstsySDDPLDKEDiiKKYYDLQLAFTEITRNLENEIEEKKnlisrLRFTETRLASSSFEDQ 1277
Cdd:COG5022 1067 -----------------------KALKLRREN--SLLDDKQLYQLESTENLLKTINVKD-----LEVTNRNLVKPANVLQ 1116
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1278 KIKAQMKKLkKLIQDMDPSIPLDsilnepLDNCPDKESDINKLMLEVDYLKRQLDIETRAHYDAENAISalhskfrkiqg 1357
Cdd:COG5022 1117 FIVAQMIKL-NLLQEISKFLSQL------VNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALS----------- 1178
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1358 ESSLSSSDIYKLKFEASEERVKSLEDKLKTMPLRDRTNLPVGDiiKNRDSISkyeeEIRYYKLENYKLQEILNesngklS 1437
Cdd:COG5022 1179 EKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFSGWPRGD--KLKKLIS----EGWVPTEYSTSLKGFNN------L 1246
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1438 QLTLDLRQSKSKEALLSeQLDRLQKDLESTERQKELLSSTIKQQKQQfencMDDLQGNELRLREHIHALKQAEEDVKNma 1517
Cdd:COG5022 1247 NKKFDTPASMSNEKLLS-LLNSIDNLLSSYKLEEEVLPATINSLLQY----INVGLFNALRTKASSLRWKSATEVNYN-- 1319
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1518 siieklktqnkQKEKLIWEREMERNDSDMQLQetllELKRVQDVKKILSDDLAHLKERLSAVedRSQYTDEINRLKEELN 1597
Cdd:COG5022 1320 -----------SEELDDWCREFEISDVDEELE----ELIQAVKVLQLLKDDLNKLDELLDAC--YSLNPAEIQNLKSRYD 1382
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1598 CSLKaETNLKKEFatlKYKLETSTNDSEAKISDLLKQlDHYTKVVEMLNNEKDAISLaEKELYQKYEALNTECEslkgki 1677
Cdd:COG5022 1383 PADK-ENNLPKEI---LKKIEALLIKQELQLSLEGKD-ETEVHLSEIFSEEKSLISL-DRNSIYKEEVLSSLSA------ 1450
|
1690
....*....|....
gi 6321812 1678 vSLTKIKQELESDL 1691
Cdd:COG5022 1451 -LLTKEKIALLDRK 1463
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
89-779 |
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: 1069.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKHNrlsksrldenshEKLPPHIFAIAEEAYENLL 168
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRR------------EEMPPHIFAIADNAYRNML 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNIAPVSGSSiveSFEMKILQSNPILESFGNAQTVRNNNSSRF 248
Cdd:cd01377 69 QDRENQSILITGESGAGKTENTKKVIQYLASVAASSKKKKESGKKKG---TLEDQILQANPILEAFGNAKTVRNNNSSRF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 249 GKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLkSRNVKDYKILSNSNQDIiPG 328
Cdd:cd01377 146 GKFIRIHFGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLL-TGDPSYYFFLSQGELTI-DG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 329 INDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAE-QASFKNDVSA--ICSNLGVDEKDFQTAILRP 405
Cdd:cd01377 224 VDDAEEFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREeQAELDGTEEAdkAAHLLGVNSSDLLKALLKP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 406 RSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENNSFEQLCINYTN 485
Cdd:cd01377 304 RIKVGREWVTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 486 EKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIESkgPPTGVLPLLDEEAVLPKSTDESFYSKLISTWDQN 565
Cdd:cd01377 384 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEK--PNMGILSILDEECVFPKATDKTFVEKLYSNHLGK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 566 SS---KFKRSRLKNGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQPEGEKSSSAGveanisnqe 642
Cdd:cd01377 462 SKnfkKPKPKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGGG--------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 643 vKKSARTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYPNRIA 722
Cdd:cd01377 533 -KKKKKGGSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRII 611
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 6321812 723 FQEFFQRYRILYPENSTTTTFSSklkastKQNCEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd01377 612 FAEFKQRYSILAPNAIPKGFDDG------KAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
77-779 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 995.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 77 VENMSELTHLNEPSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKHnrlsksrldensHEKLPPHI 156
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKR------------RGELPPHI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 157 FAIAEEAYENLLSEGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNIapvsgssiVESFEMKILQSNPILESFGN 236
Cdd:pfam00063 69 FAIADEAYRSMLQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN--------VGRLEEQILQSNPILEAFGN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 237 AQTVRNNNSSRFGKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKsrNVKDYK 316
Cdd:pfam00063 141 AKTVRNNNSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT--NPKDYH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 317 ILSNSNQDIIPGINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRA-EQASFKND--VSAICSNLGV 393
Cdd:pfam00063 219 YLSQSGCYTIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNdEQAVPDDTenLQKAASLLGI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 394 DEKDFQTAILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHG-SATLNYIGLLDIAGFEIFE 472
Cdd:pfam00063 299 DSTELEKALCKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKtIEKASFIGVLDIYGFEIFE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 473 NNSFEQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGkDLQLTIDLIESKgpPTGVLPLLDEEAVLPKSTDE 552
Cdd:pfam00063 379 KNSFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQ 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 553 SFYSKLISTWDqNSSKFKRSRL--KNGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQPEGEKSS 630
Cdd:pfam00063 456 TFLDKLYSTFS-KHPHFQKPRLqgETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAES 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 631 SAgveANISNQEVKKSARTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGI 710
Cdd:pfam00063 535 AA---ANESGKSTPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGI 611
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321812 711 RLAREGYPNRIAFQEFFQRYRILYPENsttttfSSKLKASTKQNCEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:pfam00063 612 RIRRAGFPNRITFQEFVQRYRILAPKT------WPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
70-791 |
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: 928.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 70 NPSTFDKVENMSELTHLNEPSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKHnrlsksrldensH 149
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKS------------R 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 150 EKLPPHIFAIAEEAYENLLSEGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSniapvsgssiVESFEMKILQSNP 229
Cdd:smart00242 69 GELPPHVFAIADNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTE----------VGSVEDQILESNP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 230 ILESFGNAQTVRNNNSSRFGKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKS 309
Cdd:smart00242 139 ILEAFGNAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 310 rnVKDYKILSNSNQDIIPGINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAEQAS----FKNDVS 385
Cdd:smart00242 219 --PEDYRYLNQGGCLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAstvkDKEELS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 386 AICSNLGVDEKDFQTAILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDI 465
Cdd:smart00242 297 NAAELLGVDPEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 466 AGFEIFENNSFEQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGkDLQLTIDLIESKgpPTGVLPLLDEEAV 545
Cdd:smart00242 377 YGFEIFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEKK--PPGILSLLDEECR 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 546 LPKSTDESFYSKLISTWDQNSSKFKRSRL-KNGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQP 624
Cdd:smart00242 454 FPKGTDQTFLEKLNQHHKKHPHFSKPKKKgRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 625 EGEKSSSagveanisnqevkksarTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCN 704
Cdd:smart00242 534 GVSNAGS-----------------KKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYL 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 705 GVLEGIRLAREGYPNRIAFQEFFQRYRILYPEnsttttFSSKLKASTKQNCEFLLTSLQLDTKVYKIGNTKLFFKAGVLA 784
Cdd:smart00242 597 GVLENIRIRRAGFPYRLPFDEFLQRYRVLLPD------TWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLA 670
|
....*..
gi 6321812 785 DLEKQKD 791
Cdd:smart00242 671 ELEELRE 677
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
89-779 |
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: 764.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksrldeNSHEKLPPHIFAIAEEAYENLL 168
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGK-----------GRSADLPPHVFAVADAAYRAML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEGKDQSILVTGESGAGKTENTKKILQYLASItSGSPSNIAPVSGSSIVEsfemKILQSNPILESFGNAQTVRNNNSSRF 248
Cdd:cd00124 70 RDGQNQSILISGESGAGKTETTKLVLKYLAAL-SGSGSSKSSSSASSIEQ----QILQSNPILEAFGNAKTVRNDNSSRF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 249 GKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSR--NVKDYKILSNSNQDII 326
Cdd:cd00124 145 GKFIELQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLlsYYYLNDYLNSSGCDRI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 327 PGINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAEQASF-----KNDVSAICSNLGVDEKDFQTA 401
Cdd:cd00124 225 DGVDDAEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEDSSaevadDESLKAAAKLLGVDAEDLEEA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 402 ILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNL--DHGSATLNYIGLLDIAGFEIFENNSFEQL 479
Cdd:cd00124 305 LTTRTIKVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALspTDAAESTSFIGILDIFGFENFEVNSFEQL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 480 CINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIEskGPPTGVLPLLDEEAVLPKSTDESFYSKLI 559
Cdd:cd00124 385 CINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIE--GKPLGILSLLDEECLFPKGTDATFLEKLY 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 560 STWDQNSSKFKRSRLKNG-FILKHYAGDVEYTVEGWLSKNKDPLNDNllsllsssqndiISKLFQpegeksssagveani 638
Cdd:cd00124 462 SAHGSHPRFFSKKRKAKLeFGIKHYAGDVTYDADGFLEKNKDTLPPD------------LVDLLR--------------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 639 snqevkksartstfktTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYP 718
Cdd:cd00124 515 ----------------SGSQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYP 578
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321812 719 NRIAFQEFFQRYRILYPEnsttttFSSKLKASTKQNCEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd00124 579 VRLPFDEFLKRYRILAPG------ATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
89-779 |
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: 673.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYdCD--LIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlSKSRLDensheklpPHIFAIAEEAYEN 166
Cdd:cd01380 1 PAVLHNLKVRF-CQrnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQ----NMGELD--------PHIFAIAEEAYRQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 167 LLSEGKDQSILVTGESGAGKTENTKKILQYLASitsgspsniapVSGSSIVES-FEMKILQSNPILESFGNAQTVRNNNS 245
Cdd:cd01380 68 MARDEKNQSIIVSGESGAGKTVSAKYAMRYFAT-----------VGGSSSGETqVEEKVLASNPIMEAFGNAKTTRNDNS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 246 SRFGKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSrnVKDYKILSNSNQDI 325
Cdd:cd01380 137 SRFGKYIEILFDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGS--AEDFFYTNQGGSPV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 326 IPGINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAEQASFKNDVSAI---CSNLGVDEKDFQTAI 402
Cdd:cd01380 215 IDGVDDAAEFEETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLqiaCELLGIDESQLAKWL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 403 LRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSAT--LNYIGLLDIAGFEIFENNSFEQLC 480
Cdd:cd01380 295 CKRKIVTRSEVIVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEkqHSFIGVLDIYGFETFEVNSFEQFC 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 481 INYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIESKgppTGVLPLLDEEAVLPKSTDESFYSKLIS 560
Cdd:cd01380 375 INYANEKLQQQFNQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGK---LGILDLLDEECRLPKGSDENWAQKLYN 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 561 TWDQNSSK-FKRSRLKNG-FILKHYAGDVEYTVEGWLSKNKDPLNDNllsllsssQNDIIsklfqpegeKSSsagveani 638
Cdd:cd01380 451 QHLKKPNKhFKKPRFSNTaFIVKHFADDVEYQVEGFLEKNRDTVSEE--------HLNVL---------KAS-------- 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 639 snqevkksarTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYP 718
Cdd:cd01380 506 ----------KNRKKTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFP 575
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321812 719 NRIAFQEFFQRYRILYPENSTTTTfssklkaSTKQNCEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd01380 576 SRWTYEEFFSRYRVLLPSKEWLRD-------DKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
90-779 |
0e+00 |
|
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: 660.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksrldeNSHEkLPPHIFAIAEEAYENLLS 169
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGK-----------KRHE-MPPHIYAISESAYRCMLQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 170 EGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNiapvSGSSIVESFEMKILQSNPILESFGNAQTVRNNNSSRFG 249
Cdd:cd14920 70 DREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGR----KDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 250 KFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSRNvkDYKILSNSNQDIiPGI 329
Cdd:cd14920 146 KFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFN--NYRFLSNGYIPI-PGQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 330 NDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDR-AEQASFKNDVSA--ICSNLGVDEKDFQTAILRPR 406
Cdd:cd14920 223 QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERnTDQASMPENTVAqkLCHLLGMNVMEFTRAILTPR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 407 SKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSAT-LNYIGLLDIAGFEIFENNSFEQLCINYTN 485
Cdd:cd14920 303 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 486 EKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIESKGPPTGVLPLLDEEAVLPKSTDESFYSKLIStwDQN 565
Cdd:cd14920 383 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQ--EQG 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 566 S-SKFKRSRLKNG---FILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQPE-----GEKSSSAGVEA 636
Cdd:cd14920 461 ShSKFQKPRQLKDkadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdrivgLDQVTGMTETA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 637 NISNQEVKKsartSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREG 716
Cdd:cd14920 541 FGSAYKTKK----GMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQG 616
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321812 717 YPNRIAFQEFFQRYRILYPeNSTTTTFssklkASTKQNCEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14920 617 FPNRIVFQEFRQRYEILTP-NAIPKGF-----MDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
90-779 |
0e+00 |
|
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: 643.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksrldeNSHEkLPPHIFAIAEEAYENLLS 169
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGI-----------KRHE-VPPHVFAITDSAYRNMLG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 170 EGKDQSILVTGESGAGKTENTKKILQYLASITSGSP--SNIAPVSGSS---IVESFEMKILQSNPILESFGNAQTVRNNN 244
Cdd:cd14911 70 DREDQSILCTGESGAGKTENTKKVIQFLAYVAASKPkgSGAVPHPAVNpavLIGELEQQLLQANPILEAFGNAKTVKNDN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 245 SSRFGKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKsrNVKDYKILSNSNQd 324
Cdd:cd14911 150 SSRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD--DVKSYAFLSNGSL- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 325 IIPGINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDR-AEQASFKNDVSA--ICSNLGVDEKDFQTA 401
Cdd:cd14911 227 PVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERnNDQATLPDNTVAqkIAHLLGLSVTDMTRA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 402 ILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSAT-LNYIGLLDIAGFEIFENNSFEQLC 480
Cdd:cd14911 307 FLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSFEQLC 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 481 INYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIESkgpPTGVLPLLDEEAVLPKSTDESFYSKLIS 560
Cdd:cd14911 387 INYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDK---PGGIMALLDEECWFPKATDKTFVDKLVS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 561 TWDQNsSKFKRSRLKN--GFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQpegEKSSSAGVEANI 638
Cdd:cd14911 464 AHSMH-PKFMKTDFRGvaDFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWK---DAEIVGMAQQAL 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 639 SNQEVKKSARTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYP 718
Cdd:cd14911 540 TDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFP 619
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321812 719 NRIAFQEFFQRYRILYPeNSTTTTFSSKLKAstkqnCEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14911 620 NRIPFQEFRQRYELLTP-NVIPKGFMDGKKA-----CEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
90-779 |
0e+00 |
|
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: 610.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksrldeNSHEkLPPHIFAIAEEAYENLLS 169
Cdd:cd14932 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGK-----------KRHE-MPPHIYAITDTAYRSMMQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 170 EGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNIAPVSGSSIVESFEMKILQSNPILESFGNAQTVRNNNSSRFG 249
Cdd:cd14932 70 DREDQSILCTGESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 250 KFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSRNvkDYKILSNSNQdIIPGI 329
Cdd:cd14932 150 KFIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYS--KYRFLSNGNV-TIPGQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 330 NDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDR-AEQASFKNDVSA--ICSNLGVDEKDFQTAILRPR 406
Cdd:cd14932 227 QDKELFAETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERnSDQASMPDDTAAqkVCHLLGMNVTDFTRAILSPR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 407 SKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSAT-LNYIGLLDIAGFEIFENNSFEQLCINYTN 485
Cdd:cd14932 307 IKVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 486 EKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIESKGPPTGVLPLLDEEAVLPKSTDESFYSKLISTWDQN 565
Cdd:cd14932 387 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNN 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 566 SSKFKRSRLKN--GFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQPEGEKSSSAGVEANISNQEV 643
Cdd:cd14932 467 PKFQKPKKLKDdaDFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 644 KKSARTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYPNRIAF 723
Cdd:cd14932 547 AFKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVF 626
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 6321812 724 QEFFQRYRILYPeNSTTTTFssklkASTKQNCEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14932 627 QEFRQRYEILTP-NAIPKGF-----MDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
90-779 |
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: 608.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHnkhnrlSKSRLDenshekLPPHIFAIAEEAYENLLS 169
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYF------GKRMGA------LPPHIFALAEAAYTNMQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 170 EGKDQSILVTGESGAGKTENTKKILQYLASITSGSpsniapvsgsSIVESfemKILQSNPILESFGNAQTVRNNNSSRFG 249
Cdd:cd14883 70 DGKNQSVIISGESGAGKTETTKLILQYLCAVTNNH----------SWVEQ---QILEANTILEAFGNAKTVRNDNSSRFG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 250 KFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSG-LDDSELKNLrLKSRNVKDYKILSNSNQDIIPG 328
Cdd:cd14883 137 KFIEVCFDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGaKHSKELKEK-LKLGEPEDYHYLNQSGCIRIDN 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 329 INDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAEQASFKND----VSAICSNLGVDEKDFQTAILR 404
Cdd:cd14883 216 INDKKDFDHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALTVEdkeiLKIVAKLLGVDPDKLKKALTI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 405 PRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENNSFEQLCINYT 484
Cdd:cd14883 296 RQINVRGNVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 485 NEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIEskGPPTGVLPLLDEEAVLPKSTDESFYSKLISTWDQ 564
Cdd:cd14883 376 NEKLHKFFNHYVFKLEQEEYEKEGINWSHIVF-TDNQECLDLIE--KPPLGILKLLDEECRFPKGTDLTYLEKLHAAHEK 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 565 NSS--KFKRSRLKNGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQPEGEkssSAGVEANISNQE 642
Cdd:cd14883 453 HPYyeKPDRRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDL---LALTGLSISLGG 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 643 VKKSARTSTFKTT-SSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYPNRI 721
Cdd:cd14883 530 DTTSRGTSKGKPTvGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHL 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 6321812 722 AFQEFFQRYRILYPENSTTTtfssklKASTKQNCEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14883 610 TFKEFVDRYLCLDPRARSAD------HKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
89-779 |
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: 608.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKHNrlsksrldenshekLPPHIFAIAEEAYENLL 168
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKLL--------------DSPHVYAVADTAYREMM 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEGKDQSILVTGESGAGKTENTKKILQYLASITSGspsniapvsGSSIvesfEMKILQSNPILESFGNAQTVRNNNSSRF 248
Cdd:cd01383 67 RDEINQSIIISGESGAGKTETAKIAMQYLAALGGG---------SSGI----ENEILQTNPILEAFGNAKTLRNDNSSRF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 249 GKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSrnVKDYKILSNSNQDIIPG 328
Cdd:cd01383 134 GKLIDIHFDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS--ASEYKYLNQSNCLTIDG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 329 INDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEF-VSDRAEQASFKND--VSAICSNLGVDEKDFQTAILRP 405
Cdd:cd01383 212 VDDAKKFHELKEALDTVGISKEDQEHIFQMLAAVLWLGNISFqVIDNENHVEVVADeaVSTAASLLGCNANDLMLALSTR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 406 RSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHG-SATLNYIGLLDIAGFEIFENNSFEQLCINYT 484
Cdd:cd01383 292 KIQAGGDKIVKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGkRRTGRSISILDIYGFESFQKNSFEQLCINYA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 485 NEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIESKgpPTGVLPLLDEEAVLPKSTDESFYSKLISTWDQ 564
Cdd:cd01383 372 NERLQQHFNRHLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEKK--PLGLISLLDEESNFPKATDLTFANKLKQHLKS 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 565 NSSKFKRSRlkNGFILKHYAGDVEYTVEGWLSKNKDPLNdnllsllsssqNDIISKLFQPEGEKSSSAGVEANISNQEVK 644
Cdd:cd01383 449 NSCFKGERG--GAFTIRHYAGEVTYDTSGFLEKNRDLLH-----------SDLIQLLSSCSCQLPQLFASKMLDASRKAL 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 645 KSARTSTF----KTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYPNR 720
Cdd:cd01383 516 PLTKASGSdsqkQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTR 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 6321812 721 IAFQEFFQRYRILYPENSTTTTFSSKLKASTKQNCEFLltslqldTKVYKIGNTKLFFK 779
Cdd:cd01383 596 MTHQEFARRYGFLLPEDVSASQDPLSTSVAILQQFNIL-------PEMYQVGYTKLFFR 647
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
89-779 |
0e+00 |
|
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: 598.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksRLDEnshekLPPHIFAIAEEAYENLL 168
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGK-------RRNE-----VPPHIFAISDGAYVDML 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNIAPVSGSSIvesfEMKILQSNPILESFGNAQTVRNNNSSRF 248
Cdd:cd14909 69 TNHVNQSMLITGESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSL----EDQVVQTNPVLEAFGNAKTVRNDNSSRF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 249 GKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGlDDSELKNLRLKSRNVKDYKILSNSnQDIIPG 328
Cdd:cd14909 145 GKFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSG-SVPGVKEMCLLSDNIYDYYIVSQG-KVTVPN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 329 INDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVS-DRAEQASF--KNDVSAICSNLGVDEKDFQTAILRP 405
Cdd:cd14909 223 VDDGEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQrGREEQAEQdgEEEGGRVSKLFGCDTAELYKNLLKP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 406 RSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENNSFEQLCINYTN 485
Cdd:cd14909 303 RIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 486 EKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIESkgpPTGVLPLLDEEAVLPKSTDESFYSKLISTWDQN 565
Cdd:cd14909 383 EKLQQFFNHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEK---PMGILSILEEESMFPKATDQTFSEKLTNTHLGK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 566 SSKFKRSR-LKNG-----FILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFqpegekSSSAGVEANIS 639
Cdd:cd14909 460 SAPFQKPKpPKPGqqaahFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIF------ADHAGQSGGGE 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 640 NQEVKKSARTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYPN 719
Cdd:cd14909 534 QAKGGRGKKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPN 613
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 720 RIAFQEFFQRYRILYPEnsttttfSSKLKASTKQNCEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14909 614 RMMYPDFKMRYKILNPA-------GIQGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
90-779 |
0e+00 |
|
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: 598.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnRLSKSrldensheklPPHIFAIAEEAYENLLS 169
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGK--RRSEA----------PPHIYAIADNAYNDMLR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 170 EGKDQSILVTGESGAGKTENTKKILQYLASITS--GSPSNIAPVSGSSIVESFEMKILQSNPILESFGNAQTVRNNNSSR 247
Cdd:cd14927 70 NRENQSMLITGESGAGKTVNTKRVIQYFAIVAAlgDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 248 FGKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGlDDSELKNLRLKSRNVKDYKILSNSnQDIIP 327
Cdd:cd14927 150 FGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSG-KKPELQDMLLVSMNPYDYHFCSQG-VTTVD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 328 GINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVS-DRAEQASFKNDVSAICSN--LGVDEKDFQTAILR 404
Cdd:cd14927 228 NMDDGEELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQkQREEQAEADGTESADKAAylMGVSSADLLKGLLH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 405 PRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENNSFEQLCINYT 484
Cdd:cd14927 308 PRVKVGNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 485 NEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIESkgpPTGVLPLLDEEAVLPKSTDESFYSKLISTWDQ 564
Cdd:cd14927 388 NEKLQQFFNHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEK---PLGILSILEEECMFPKASDASFKAKLYDNHLG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 565 NSSKFKRSRL------KNGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFqpEGEKSSSAGVEANI 638
Cdd:cd14927 465 KSPNFQKPRPdkkrkyEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY--ENYVGSDSTEDPKS 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 639 SNQEVKKSArtSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYP 718
Cdd:cd14927 543 GVKEKRKKA--ASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFP 620
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321812 719 NRIAFQEFFQRYRILYPENSTTTTFSSKLKASTKqncefLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14927 621 NRILYADFKQRYRILNPSAIPDDKFVDSRKATEK-----LLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
89-779 |
0e+00 |
|
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: 594.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksrldenSHEKLPPHIFAIAEEAYENLL 168
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGK------------KRQEAPPHIFSISDNAYQFML 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEGKDQSILVTGESGAGKTENTKKILQYLASItsGSPSNIAPVSGSSIVESFEMKILQSNPILESFGNAQTVRNNNSSRF 248
Cdd:cd14913 69 TDRENQSILITGESGAGKTVNTKRVIQYFATI--AATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 249 GKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGlDDSELKNLRLKSRNVKDYKILSNSnQDIIPG 328
Cdd:cd14913 147 GKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSN-KKPELIELLLITTNPYDYPFISQG-EILVAS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 329 INDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVS-DRAEQAsfKNDVSAICSN----LGVDEKDFQTAIL 403
Cdd:cd14913 225 IDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQkQREEQA--EPDGTEVADKtaylMGLNSSDLLKALC 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 404 RPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENNSFEQLCINY 483
Cdd:cd14913 303 FPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINF 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 484 TNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIESkgpPTGVLPLLDEEAVLPKSTDESFYSKLISTWD 563
Cdd:cd14913 383 TNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK---PMGIFSILEEECMFPKATDTSFKNKLYDQHL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 564 QNSSKFKRSRLKNG-----FILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFqpegekSSSAGVEANI 638
Cdd:cd14913 460 GKSNNFQKPKVVKGraeahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY------ATFATADADS 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 639 SNQEVKKSaRTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYP 718
Cdd:cd14913 534 GKKKVAKK-KGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFP 612
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321812 719 NRIAFQEFFQRYRILYPENSTTTTFssklkASTKQNCEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14913 613 NRILYGDFKQRYRVLNASAIPEGQF-----IDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
90-779 |
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: 594.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksRLDEnshekLPPHIFAIAEEAYENLLS 169
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNK-------KIGE-----LPPHIFAIADNAYTNMKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 170 EGKDQSILVTGESGAGKTENTKKILQYLASItSGSPSNIapvsgssivesfEMKILQSNPILESFGNAQTVRNNNSSRFG 249
Cdd:cd01381 70 NKRDQCVVISGESGAGKTESTKLILQYLAAI-SGQHSWI------------EQQILEANPILEAFGNAKTIRNDNSSRFG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 250 KFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKsrNVKDYKILSNSNQDIIPGI 329
Cdd:cd01381 137 KYIDIHFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELG--DASDYYYLTQGNCLTCEGR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 330 NDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEF---VSDRAEQASFKN--DVSAICSNLGVDEKDFQTAILR 404
Cdd:cd01381 215 DDAAEFADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFeatVVDNLDASEVRDppNLERAAKLLEVPKQDLVDALTT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 405 PRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMIN----KNLDHgSATLNYIGLLDIAGFEIFENNSFEQLC 480
Cdd:cd01381 295 RTIFTRGETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINsaiyKPRGT-DSSRTSIGVLDIFGFENFEVNSFEQLC 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 481 INYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIESKgpPTGVLPLLDEEAVLPKSTDESFYSKLIS 560
Cdd:cd01381 374 INFANENLQQFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIALK--PMNIMSLIDEESKFPKGTDQTMLEKLHS 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 561 TWDQNSSKFK-RSRLKNGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQPE-GEKSSSAgveani 638
Cdd:cd01381 451 THGNNKNYLKpKSDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDiSMGSETR------ 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 639 snqevKKSartstfKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYP 718
Cdd:cd01381 525 -----KKS------PTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYP 593
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321812 719 NRIAFQEFFQRYRILYPenSTTTTFSSKLKASTKQNCEFLLtslqLDTKVYKIGNTKLFFK 779
Cdd:cd01381 594 IRHTFEEFVERYRVLVP--GIPPAHKTDCRAATRKICCAVL----GGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
89-779 |
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: 590.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNL-NLYSEDHINLYHNKhnrlsksRLDEnshekLPPHIFAIAEEAYENL 167
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLpHLYDAHMMEQYKGA-------PLGE-----LSPHVFAVADAAYRAM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 168 LSEGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNIAPVsgssivesfEMKILQSNPILESFGNAQTVRNNNSSR 247
Cdd:cd01384 69 INEGKSQSILVSGESGAGKTETTKMLMQYLAYMGGRAVTEGRSV---------EQQVLESNPLLEAFGNAKTVRNNNSSR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 248 FGKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKsrNVKDYKILSNSNQDIIP 327
Cdd:cd01384 140 FGKFVEIQFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLK--DPKQFHYLNQSKCFELD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 328 GINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFV-SDRAEQASFKNDVS----AICSNL-GVDEKDFQTA 401
Cdd:cd01384 218 GVDDAEEYRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSkGEEDDSSVPKDEKSefhlKAAAELlMCDEKALEDA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 402 ILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENNSFEQLCI 481
Cdd:cd01384 298 LCKRVIVTPDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 482 NYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIESKgpPTGVLPLLDEEAVLPKSTDESFYSKLIST 561
Cdd:cd01384 378 NLANEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEKK--PGGIIALLDEACMFPRSTHETFAQKLYQT 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 562 WDQNS--SKFKRSRlkNGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQPEGEKSSSAGveanis 639
Cdd:cd01384 455 LKDHKrfSKPKLSR--TDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGTSSS------ 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 640 nqevkksartSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYPN 719
Cdd:cd01384 527 ----------SKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPT 596
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 720 RIAFQEFFQRYRILYPEnsttttfSSKLKASTKQNCEFLLTSLQLDTkvYKIGNTKLFFK 779
Cdd:cd01384 597 RKPFEEFLDRFGLLAPE-------VLKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
90-779 |
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: 582.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhNRLsksrldensheKLPPHIFAIAEEAYENLLS 169
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGK-NRY-----------EVPPHVFALADSAYRNMKS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 170 EGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNIAPVSgssivesfEMkILQSNPILESFGNAQTVRNNNSSRFG 249
Cdd:cd01378 70 EKENQCVIISGESGAGKTEASKRIMQYIAAVSGGSESEVERVK--------DM-LLASNPLLEAFGNAKTLRNDNSSRFG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 250 KFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSRNvkDYKILSNSNQDIIPGI 329
Cdd:cd01378 141 KYMEIQFDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPE--QYYYYSKSGCFDVDGI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 330 NDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAEQA--SFKNDVSAICSNLGVDEKDFQTAILRPRS 407
Cdd:cd01378 219 DDAADFKEVLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAaiSDTSVLDFVAYLLGVDPDQLEKALTHRTI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 408 KAGKEWVSQSK---NSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNY-IGLLDIAGFEIFENNSFEQLCINY 483
Cdd:cd01378 299 ETGGGGRSVYEvplNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKvIGVLDIYGFEIFEKNSFEQFCINY 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 484 TNEKLQQFFNNhmFVL--EQSEYLKENIQWDYIDYgKDLQLTIDLIESKgpPTGVLPLLDEE-AVLPKSTDESFYSKLIS 560
Cdd:cd01378 379 VNEKLQQIFIE--LTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEEK--PPGIFAILDDAcLTAGDATDQTFLQKLNQ 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 561 TWDQNSSKFKRSRLK----NGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFqPEGeksssagvea 636
Cdd:cd01378 454 LFSNHPHFECPSGHFelrrGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLF-PEG---------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 637 niSNQEVKKSARTSTFKTtssrhREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREG 716
Cdd:cd01378 523 --VDLDSKKRPPTAGTKF-----KNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAG 595
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321812 717 YPNRIAFQEFFQRYRILYPENSTTTTFSSklkastKQNCEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd01378 596 FAYRQTYEKFLERYKLLSPKTWPAWDGTW------QGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
90-779 |
0e+00 |
|
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: 580.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksrldeNSHEkLPPHIFAIAEEAYENLLS 169
Cdd:cd15896 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGK-----------KRHE-MPPHIYAITDTAYRSMMQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 170 EGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNIAPVSGSSIVESFEMKILQSNPILESFGNAQTVRNNNSSRFG 249
Cdd:cd15896 70 DREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 250 KFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSRNvkDYKILSNSNQdIIPGI 329
Cdd:cd15896 150 KFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYN--NYRFLSNGNV-TIPGQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 330 NDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDR-AEQASFKNDVSA--ICSNLGVDEKDFQTAILRPR 406
Cdd:cd15896 227 QDKDLFTETMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERhTDQASMPDNTAAqkVCHLMGMNVTDFTRAILSPR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 407 SKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSAT-LNYIGLLDIAGFEIFENNSFEQLCINYTN 485
Cdd:cd15896 307 IKVGRDYVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 486 EKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIESKGPPTGVLPLLDEEAVLPKSTDESFYSKLISTWDQN 565
Cdd:cd15896 387 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTH 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 566 SSKFKRSRLKN--GFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQpegEKSSSAGVE--ANISNQ 641
Cdd:cd15896 467 PKFFKPKKLKDeaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWK---DVDRIVGLDkvSGMSEM 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 642 EVKKSARTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYPNRI 721
Cdd:cd15896 544 PGAFKTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRI 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 6321812 722 AFQEFFQRYRILYPeNSTTTTFssklkASTKQNCEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd15896 624 VFQEFRQRYEILTP-NAIPKGF-----MDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
89-779 |
0e+00 |
|
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: 578.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKHnrlsksrldensHEKLPPHIFAIAEEAYENLL 168
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKR------------RSEAPPHIFAVANNAFQDML 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNiapvsgsSIVESFEMKILQSNPILESFGNAQTVRNNNSSRF 248
Cdd:cd14929 69 HNRENQSILFTGESGAGKTVNTKHIIQYFATIAAMIESK-------KKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 249 GKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGldDSELKNLRLKSRNVKDYKILSNSnqdiIPG 328
Cdd:cd14929 142 GKFIRMHFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSG--KKELRDLLLVSANPSDFHFCSCG----AVA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 329 INDVENFKELLS---ALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSD-RAEQ--ASFKNDVSAICSNLGVDEKDFQTAI 402
Cdd:cd14929 216 VESLDDAEELLAteqAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKpREEQleADGTENADKAAFLMGINSSELVKGL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 403 LRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENNSFEQLCIN 482
Cdd:cd14929 296 IHPRIKVGNEYVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCIN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 483 YTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIESkgpPTGVLPLLDEEAVLPKSTDESFYSKLISTW 562
Cdd:cd14929 376 FTNEKLQQFFNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEK---PMGIFSILEEECMFPKATDLTFKTKLFDNH 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 563 DQNSSKFKR-----SRLKNGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFqpegEKSSSAGVEAN 637
Cdd:cd14929 453 FGKSVHFQKpkpdkKKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF----ENYISTDSAIQ 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 638 ISNQEVKKSArtsTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGY 717
Cdd:cd14929 529 FGEKKRKKGA---SFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGF 605
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321812 718 PNRIAFQEFFQRYRILYPENSTTTTFSSKLKAStkqncEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14929 606 PNRLLYADFKQRYCILNPRTFPKSKFVSSRKAA-----EELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
90-779 |
0e+00 |
|
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: 575.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksrldeNSHEkLPPHIFAIAEEAYENLLS 169
Cdd:cd14921 2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGK-----------KRHE-MPPHIYAIADTAYRSMLQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 170 EGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNiapvSGSSIVESFEMKILQSNPILESFGNAQTVRNNNSSRFG 249
Cdd:cd14921 70 DREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGK----KDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 250 KFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSRNvkDYKILSNSNQDIiPGI 329
Cdd:cd14921 146 KFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFN--NYTFLSNGFVPI-PAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 330 NDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDR-AEQASFKNDVSA--ICSNLGVDEKDFQTAILRPR 406
Cdd:cd14921 223 QDDEMFQETLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERnTDQASMPDNTAAqkVCHLMGINVTDFTRSILTPR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 407 SKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSAT-LNYIGLLDIAGFEIFENNSFEQLCINYTN 485
Cdd:cd14921 303 IKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 486 EKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIESKGPPTGVLPLLDEEAVLPKSTDESFYSKLISTwDQN 565
Cdd:cd14921 383 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTE-QGN 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 566 SSKFKRSRL---KNGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQpEGEKSSSAGVEANISNQE 642
Cdd:cd14921 462 HPKFQKPKQlkdKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWK-DVDRIVGLDQMAKMTESS 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 643 VKKSARTS--TFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYPNR 720
Cdd:cd14921 541 LPSASKTKkgMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNR 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 6321812 721 IAFQEFFQRYRILyPENSTTTTFssklkASTKQNCEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14921 621 IVFQEFRQRYEIL-AANAIPKGF-----MDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
90-779 |
0e+00 |
|
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: 567.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksrldeNSHEkLPPHIFAIAEEAYENLLS 169
Cdd:cd14919 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGK-----------KRHE-MPPHIYAITDTAYRSMMQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 170 EGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNiapvsgsSIVESFEMKILQSNPILESFGNAQTVRNNNSSRFG 249
Cdd:cd14919 70 DREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKSK-------KDQGELERQLLQANPILEAFGNAKTVKNDNSSRFG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 250 KFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSRNvkDYKILSNSNQdIIPGI 329
Cdd:cd14919 143 KFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYN--KYRFLSNGHV-TIPGQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 330 NDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDR-AEQASFKNDVSA--ICSNLGVDEKDFQTAILRPR 406
Cdd:cd14919 220 QDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERnTDQASMPDNTAAqkVSHLLGINVTDFTRGILTPR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 407 SKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSAT-LNYIGLLDIAGFEIFENNSFEQLCINYTN 485
Cdd:cd14919 300 IKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 486 EKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIESKGPPTGVLPLLDEEAVLPKSTDESFYSKLISTWDQN 565
Cdd:cd14919 380 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTH 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 566 SSKFKRSRLKN--GFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQpEGEKSSSAGVEANISNQEV 643
Cdd:cd14919 460 PKFQKPKQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWK-DVDRIIGLDQVAGMSETAL 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 644 KKS--ARTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYPNRI 721
Cdd:cd14919 539 PGAfkTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRV 618
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 6321812 722 AFQEFFQRYRILYPeNSTTTTFssklkASTKQNCEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14919 619 VFQEFRQRYEILTP-NSIPKGF-----MDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
90-779 |
0e+00 |
|
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: 564.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksrldeNSHEkLPPHIFAIAEEAYENLLS 169
Cdd:cd14930 2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGK-----------KRHE-VPPHVYAVTEGAYRSMLQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 170 EGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNIAPvsgsSIVESFEMKILQSNPILESFGNAQTVRNNNSSRFG 249
Cdd:cd14930 70 DREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEP----GVPGELERQLLQANPILEAFGNAKTVKNDNSSRFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 250 KFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSrnVKDYKILSNSNQDIiPGi 329
Cdd:cd14930 146 KFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP--CSHYRFLTNGPSSS-PG- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 330 NDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDR-AEQASFKNDVSA--ICSNLGVDEKDFQTAILRPR 406
Cdd:cd14930 222 QERELFQETLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERnTDQATMPDNTAAqkLCRLLGLGVTDFSRALLTPR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 407 SKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSAT-LNYIGLLDIAGFEIFENNSFEQLCINYTN 485
Cdd:cd14930 302 IKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 486 EKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIESKGPPTGVLPLLDEEAVLPKSTDESFYSKlISTWDQN 565
Cdd:cd14930 382 EKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEK-VAQEQGG 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 566 SSKFKRSR-LKN--GFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQpegEKSSSAGVE--ANISN 640
Cdd:cd14930 461 HPKFQRPRhLRDqaDFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWK---DVEGIVGLEqvSSLGD 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 641 QEVKKSARTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYPNR 720
Cdd:cd14930 538 GPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNR 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 6321812 721 IAFQEFFQRYRILYPeNSTTTTFssklkASTKQNCEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14930 618 ILFQEFRQRYEILTP-NAIPKGF-----MDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
89-779 |
2.44e-178 |
|
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: 556.25 E-value: 2.44e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksrldenSHEKLPPHIFAIAEEAYENLL 168
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGK------------KRSEAPPHIFSISDNAYQYML 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEGKDQSILVTGESGAGKTENTKKILQY---LASITSGSPSNIAPVSGSsivesFEMKILQSNPILESFGNAQTVRNNNS 245
Cdd:cd14917 69 TDRENQSILITGESGAGKTVNTKRVIQYfavIAAIGDRSKKDQTPGKGT-----LEDQIIQANPALEAFGNAKTVRNDNS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 246 SRFGKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGlDDSELKNLRLKSRNVKDYKILSNSnQDI 325
Cdd:cd14917 144 SRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSN-KKPELLDMLLITNNPYDYAFISQG-ETT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 326 IPGINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEF-VSDRAEQA----SFKNDVSAICsnLGVDEKDFQT 400
Cdd:cd14917 222 VASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFkQKQREEQAepdgTEEADKSAYL--MGLNSADLLK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 401 AILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENNSFEQLC 480
Cdd:cd14917 300 GLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLC 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 481 INYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIESkgpPTGVLPLLDEEAVLPKSTDESFYSKLIS 560
Cdd:cd14917 380 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEK---PMGIMSILEEECMFPKATDMTFKAKLFD 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 561 TWDQNSSKFKRSRLKNG-----FILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFqpegekSSSAGVE 635
Cdd:cd14917 457 NHLGKSNNFQKPRNIKGkpeahFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLF------ANYAGAD 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 636 ANISNQEvKKSARTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLARE 715
Cdd:cd14917 531 APIEKGK-GKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRK 609
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321812 716 GYPNRIAFQEFFQRYRILYPENSTTTTFSSKLKASTKqncefLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14917 610 GFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEK-----LLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
90-779 |
3.93e-177 |
|
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: 552.71 E-value: 3.93e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksrldenSHEKLPPHIFAIAEEAYENLLS 169
Cdd:cd14934 2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGK------------KRTEMPPHLFSISDNAYHDMLM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 170 EGKDQSILVTGESGAGKTENTKKILQYLASItsGSPSNIAPVSGSSIvesfEMKILQSNPILESFGNAQTVRNNNSSRFG 249
Cdd:cd14934 70 DRENQSMLITGESGAGKTENTKKVIQYFANI--GGTGKQSSDGKGSL----EDQIIQANPVLEAFGNAKTTRNNNSSRFG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 250 KFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSrNVKDYKILSNSnQDIIPGI 329
Cdd:cd14934 144 KFIRIHFGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVP-NPKEYHWVSQG-VTVVDNM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 330 NDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSD-RAEQASFKNDVSA--ICSNLGVDEKDFQTAILRPR 406
Cdd:cd14934 222 DDGEELQITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKpREEQAEVDTTEVAdkVAHLMGLNSGELQKGITRPR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 407 SKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENNSFEQLCINYTNE 486
Cdd:cd14934 302 VKVGNEFVQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 487 KLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIESkgpPTGVLPLLDEEAVLPKSTDESFYSKLISTWDQNS 566
Cdd:cd14934 382 KLQQFFNHHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEK---PMGIFSILEEQCVFPKATDATFKAALYDNHLGKS 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 567 SKFKRSRLKNG------FILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQPEGEKSSSagveanisn 640
Cdd:cd14934 459 SNFLKPKGGKGkgpeahFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAGS--------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 641 qevKKSARTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYPNR 720
Cdd:cd14934 530 ---KKQKRGSSFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNR 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 6321812 721 IAFQEFFQRYRILYPeNSTTTTFSSKLKAStkqncEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14934 607 LQYPEFKQRYQVLNP-NVIPQGFVDNKKAS-----ELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
89-779 |
7.72e-172 |
|
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: 538.88 E-value: 7.72e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksrldenSHEKLPPHIFAIAEEAYENLL 168
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGK------------KRSEAPPHIFSISDNAYQYML 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNIAPVSGSSiVESFEMKILQSNPILESFGNAQTVRNNNSSRF 248
Cdd:cd14916 69 TDRENQSILITGESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNAN-KGTLEDQIIQANPALEAFGNAKTVRNDNSSRF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 249 GKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGlDDSELKNLRLKSRNVKDYKILSNSnQDIIPG 328
Cdd:cd14916 148 GKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSN-KKPELLDMLLVTNNPYDYAFVSQG-EVSVAS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 329 INDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVS-DRAEQAS--FKNDVSAICSNLGVDEKDFQTAILRP 405
Cdd:cd14916 226 IDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQkQREEQAEpdGTEDADKSAYLMGLNSADLLKGLCHP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 406 RSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENNSFEQLCINYTN 485
Cdd:cd14916 306 RVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 486 EKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIESkgpPTGVLPLLDEEAVLPKSTDESFYSKLISTWDQN 565
Cdd:cd14916 386 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEK---PMGIMSILEEECMFPKASDMTFKAKLYDNHLGK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 566 SSKFKRSRLKNG-----FILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFqpegekSSSAGVEANISN 640
Cdd:cd14916 463 SNNFQKPRNVKGkqeahFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLF------STYASADTGDSG 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 641 QEVKKSARTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYPNR 720
Cdd:cd14916 537 KGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNR 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 6321812 721 IAFQEFFQRYRILYPENSTTTTFSSKLKASTKqncefLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14916 617 ILYGDFRQRYRILNPAAIPEGQFIDSRKGAEK-----LLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
89-779 |
1.62e-169 |
|
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: 532.77 E-value: 1.62e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksrldenSHEKLPPHIFAIAEEAYENLL 168
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGK------------KRQEAPPHIFSISDNAYQFML 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNIAPVSGSSIVESFEMKILQSNPILESFGNAQTVRNNNSSRF 248
Cdd:cd14910 69 TDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 249 GKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGlDDSELKNLRLKSRNVKDYKILSNSnQDIIPG 328
Cdd:cd14910 149 GKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSN-KKPDLIEMLLITTNPYDYAFVSQG-EITVPS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 329 INDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAEQASFKN-----DVSAICSNLgvDEKDFQTAIL 403
Cdd:cd14910 227 IDDQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDgtevaDKAAYLQNL--NSADLLKALC 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 404 RPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENNSFEQLCINY 483
Cdd:cd14910 305 YPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 484 TNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIESkgpPTGVLPLLDEEAVLPKSTDESFYSKLISTWD 563
Cdd:cd14910 385 TNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK---PMGIFSILEEECMFPKATDTSFKNKLYEQHL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 564 QNSSKFKRSRLKNG-----FILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFqpegekSSSAGVEANI 638
Cdd:cd14910 462 GKSNNFQKPKPAKGkveahFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLF------SGAAAAEAEE 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 639 SNQEVKKSARTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYP 718
Cdd:cd14910 536 GGGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFP 615
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321812 719 NRIAFQEFFQRYRILYPENSTTTTFSSKLKASTKqncefLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14910 616 SRILYADFKQRYKVLNASAIPEGQFIDSKKASEK-----LLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
89-779 |
1.13e-167 |
|
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: 526.82 E-value: 1.13e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNL-NLYSEDHINLYHNKhnrlsksrldenSHEKLPPHIFAIAEEAYENL 167
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIpKLYSSETIKSYQGK------------SLGTLPPHVFAIADKAYRDM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 168 LSEGKDQSILVTGESGAGKTENTKKILQYLASitsgspsniapvSGSSIVESFEMKILQSNPILESFGNAQTVRNNNSSR 247
Cdd:cd01382 69 KVLKQSQSIIVSGESGAGKTESTKYILRYLTE------------SWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 248 FGKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDsELKNLRLKsrnvkdykilsnsnqdiIP 327
Cdd:cd01382 137 FGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPE-DLREKLLK-----------------DP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 328 GINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEF---VSDRAEQASFKNDVS---AICSNL-GVDEKDFQT 400
Cdd:cd01382 199 LLDDVGDFIRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFeenGSDSGGGCNVKPKSEqslEYAAELlGLDQDELRV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 401 A----ILRPRSKAGKEWVSQ-SKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATlNYIGLLDIAGFEIFENNS 475
Cdd:cd01382 279 SlttrVMQTTRGGAKGTVIKvPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFETSS-YFIGVLDIAGFEYFEVNS 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 476 FEQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIESKgpPTGVLPLLDEEAVLPKSTDESFY 555
Cdd:cd01382 358 FEQFCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAK--LVGILDLLDEESKLPKPSDQHFT 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 556 SKLISTWDQN-------SSKFKRSR-LKN--GFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQPE 625
Cdd:cd01382 435 SAVHQKHKNHfrlsiprKSKLKIHRnLRDdeGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESS 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 626 GEKSSSagveanisnqeVKKSARTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNG 705
Cdd:cd01382 515 TNNNKD-----------SKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSG 583
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321812 706 VLEGIRLAREGYPNRIAFQEFFQRYRILYPENsttttfSSKLKASTkqNCEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd01382 584 MVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPK------LARLDPRL--FCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
89-779 |
1.32e-167 |
|
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: 527.38 E-value: 1.32e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksrldenSHEKLPPHIFAIAEEAYENLL 168
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGK------------KRQEAPPHIFSISDNAYQFML 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNIAPVSGSSIVESFEMKILQSNPILESFGNAQTVRNNNSSRF 248
Cdd:cd14915 69 TDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 249 GKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGlDDSELKNLRLKSRNVKDYKILSNSnQDIIPG 328
Cdd:cd14915 149 GKFIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSN-KKPELIEMLLITTNPYDFAFVSQG-EITVPS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 329 INDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVS-DRAEQASFKN----DVSAICSNLgvDEKDFQTAIL 403
Cdd:cd14915 227 IDDQEELMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQkQREEQAEPDGtevaDKAAYLTSL--NSADLLKALC 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 404 RPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENNSFEQLCINY 483
Cdd:cd14915 305 YPRVKVGNEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 484 TNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIESkgpPTGVLPLLDEEAVLPKSTDESFYSKLISTWD 563
Cdd:cd14915 385 TNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK---PMGIFSILEEECMFPKATDTSFKNKLYEQHL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 564 QNSSKFKRSRLKNG-----FILKHYAGDVEYTVEGWLSKNKDPLNDNllsllsssqndiISKLFQPEGEKS----SSAGV 634
Cdd:cd14915 462 GKSNNFQKPKPAKGkaeahFSLVHYAGTVDYNIAGWLDKNKDPLNET------------VVGLYQKSGMKTlaflFSGGQ 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 635 EANISNQEVKKSART--STFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRL 712
Cdd:cd14915 530 TAEAEGGGGKKGGKKkgSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRI 609
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321812 713 AREGYPNRIAFQEFFQRYRILYPENSTTTTFSSKLKASTKqncefLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14915 610 CRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEK-----LLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
89-779 |
2.65e-167 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in 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: 526.61 E-value: 2.65e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksrldenSHEKLPPHIFAIAEEAYENLL 168
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGK------------KRQEAPPHIFSISDNAYQFML 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNIAPVSGSSIVESFEMKILQSNPILESFGNAQTVRNNNSSRF 248
Cdd:cd14912 69 TDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 249 GKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGlDDSELKNLRLKSRNVKDYKILSNSNQDiIPG 328
Cdd:cd14912 149 GKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSN-KKPELIEMLLITTNPYDYPFVSQGEIS-VAS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 329 INDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAEQASFKN-----DVSAICSNLgvDEKDFQTAIL 403
Cdd:cd14912 227 IDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDgtevaDKAAYLQSL--NSADLLKALC 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 404 RPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENNSFEQLCINY 483
Cdd:cd14912 305 YPRVKVGNEYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 484 TNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIESkgpPTGVLPLLDEEAVLPKSTDESFYSKLISTWD 563
Cdd:cd14912 385 TNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK---PMGIFSILEEECMFPKATDTSFKNKLYEQHL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 564 QNSSKFKRSRLKNG-----FILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFqpegekSSSAGVEANI 638
Cdd:cd14912 462 GKSANFQKPKVVKGkaeahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLF------SGAQTAEGAS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 639 SNQEVKKSART--STFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREG 716
Cdd:cd14912 536 AGGGAKKGGKKkgSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKG 615
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321812 717 YPNRIAFQEFFQRYRILYPENSTTTTFSSKLKASTKqncefLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14912 616 FPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEK-----LLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
89-779 |
3.15e-167 |
|
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: 526.56 E-value: 3.15e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksrldenSHEKLPPHIFAIAEEAYENLL 168
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGK------------KRQEAPPHIFSISDNAYQFML 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNiAPVSGSSIVESFEMKILQSNPILESFGNAQTVRNNNSSRF 248
Cdd:cd14923 69 TDRDNQSILITGESGAGKTVNTKRVIQYFATIAVTGDKK-KEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 249 GKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGlDDSELKNLRLKSRNVKDYKILSNSnQDIIPG 328
Cdd:cd14923 148 GKFIRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSN-KKPELIDLLLISTNPFDFPFVSQG-EVTVAS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 329 INDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVS-DRAEQAsfKNDVSAICSN----LGVDEKDFQTAIL 403
Cdd:cd14923 226 IDDSEELLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQkQREEQA--EPDGTEVADKagylMGLNSAEMLKGLC 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 404 RPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENNSFEQLCINY 483
Cdd:cd14923 304 CPRVKVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 484 TNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIESkgpPTGVLPLLDEEAVLPKSTDESFYSKLISTWD 563
Cdd:cd14923 384 TNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK---PMGIFSILEEECMFPKATDTSFKNKLYDQHL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 564 QNSSKFKRSRLKNG-----FILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFqpegekSSSAGVEANI 638
Cdd:cd14923 461 GKSNNFQKPKPAKGkaeahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLF------SNYAGAEAGD 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 639 SNQEVKKSART-STFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGY 717
Cdd:cd14923 535 SGGSKKGGKKKgSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGF 614
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321812 718 PNRIAFQEFFQRYRILYPENSTTTTFSSKLKASTKqncefLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14923 615 PSRILYADFKQRYRILNASAIPEGQFIDSKNASEK-----LLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
89-779 |
1.13e-166 |
|
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: 525.07 E-value: 1.13e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksrldenSHEKLPPHIFAIAEEAYENLL 168
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGK------------KRQEAPPHIFSISDNAYQFML 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNiaPVSGSSIVESFEMKILQSNPILESFGNAQTVRNNNSSRF 248
Cdd:cd14918 69 TDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKK--KEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 249 GKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGlDDSELKNLRLKSRNVKDYKILSNSnQDIIPG 328
Cdd:cd14918 147 GKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSN-KKPDLIEMLLITTNPYDYAFVSQG-EITVPS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 329 INDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAEQASFKN-----DVSAICSNLgvDEKDFQTAIL 403
Cdd:cd14918 225 IDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDgtevaDKAAYLQSL--NSADLLKALC 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 404 RPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENNSFEQLCINY 483
Cdd:cd14918 303 YPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINF 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 484 TNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIESkgpPTGVLPLLDEEAVLPKSTDESFYSKLISTWD 563
Cdd:cd14918 383 TNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK---PLGIFSILEEECMFPKATDTSFKNKLYDQHL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 564 QNSSKFKRSRLKNG-----FILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFqpegekSSSAGVEANI 638
Cdd:cd14918 460 GKSANFQKPKVVKGkaeahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLF------STYASAEADS 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 639 SNQEVKKSaRTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYP 718
Cdd:cd14918 534 GAKKGAKK-KGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFP 612
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321812 719 NRIAFQEFFQRYRILYPENSTTTTFSSKLKASTKqncefLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14918 613 SRILYGDFKQRYKVLNASAIPEGQFIDSKKASEK-----LLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
95-779 |
1.82e-166 |
|
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: 523.94 E-value: 1.82e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 95 LEKRYDCDLIYTYSGLFLVAINPYHNLNLysedhinLYhnKHNRLSKSRLDENSHEKLPPHIFAIAEEAYENLLSEGK-- 172
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPL-------LY--DVPGFDSQRKEEATASSPPPHVFSIAERAYRAMKGVGKgq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 173 --DQSILVTGESGAGKTENTKKILQYLASITSGSPSNIAPVSGSSIVESFEMKILQSNPILESFGNAQTVRNNNSSRFGK 250
Cdd:cd14892 78 gtPQSIVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 251 FIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDdsELKNLRLKSRNVKDYKILSNSNQDIIPGIN 330
Cdd:cd14892 158 YIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD--ANENAALELTPAESFLFLNQGNCVEVDGVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 331 DVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVS-----DRAEQASFKNDVSAICSNLGVDEKDFQTAILRP 405
Cdd:cd14892 236 DATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaddeDVFAQSADGVNVAKAAGLLGVDAAELMFKLVTQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 406 RSKAGKEWVSQSKNS-QQAKFILNALSRNLYERLFGYIVDMINK------NLDHGSATLN----YIGLLDIAGFEIFENN 474
Cdd:cd14892 316 TTSTARGSVLEIKLTaREAKNALDALCKYLYGELFDWLISRINAchkqqtSGVTGGAASPtfspFIGILDIFGFEIMPTN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 475 SFEQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIEskGPPTGVLPLLDEEAVLP-KSTDES 553
Cdd:cd14892 396 SFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQ--KKPLGLLPLLEEQMLLKrKTTDKQ 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 554 FYSKLISTWDQNSSKFKRSRLKNG-FILKHYAGDVEYTVEGWLSKNKDPLndnllsllsssQNDIISKLfqpegeksssa 632
Cdd:cd14892 473 LLTIYHQTHLDKHPHYAKPRFECDeFVLRHYAGDVTYDVHGFLAKNNDNL-----------HDDLRDLL----------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 633 gveanisnqevkksartstfkTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRL 712
Cdd:cd14892 531 ---------------------RSSSKFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRI 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321812 713 AREGYPNRIAFQEFFQRYRILyPENS--TTTTFSSKLKASTKQNCEFLLTSlQLDTKVYKIGNTKLFFK 779
Cdd:cd14892 590 RREGFPIRRQFEEFYEKFWPL-ARNKagVAASPDACDATTARKKCEEIVAR-ALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
89-779 |
5.12e-165 |
|
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: 519.33 E-value: 5.12e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKHNRlsksrldensheKLPPHIFAIAEEAYENLL 168
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPK------------EMPPHTYNIADDAYRAMI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEGKDQSILVTGESGAGKTENTKKILQYLASItSGSPSNIapvsgssivesfEMKILQSNPILESFGNAQTVRNNNSSRF 248
Cdd:cd14872 69 VDAMNQSILISGESGAGKTEATKQCLSFFAEV-AGSTNGV------------EQRVLLANPILEAFGNAKTLRNNNSSRF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 249 GKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSrnvkDYKILSNSNQDIIPG 328
Cdd:cd14872 136 GKWVEIHFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSA----AYGYLSLSGCIEVEG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 329 INDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFV-----SDRAEQASFKNDVSAICSN-LGVDEKDFQTAI 402
Cdd:cd14872 212 VDDVADFEEVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFAsgggkSLVSGSTVANRDVLKEVATlLGVDAATLEEAL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 403 L-RPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLN-YIGLLDIAGFEIFENNSFEQLC 480
Cdd:cd14872 292 TsRLMEIKGCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTtFIGVLDIFGFEIFEKNSFEQLC 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 481 INYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIESKGPptGVLPLLDEEAVLPKSTDESFYSKL-- 558
Cdd:cd14872 372 INFTNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKKQP--GLMLALDDQVKIPKGSDATFMIAAnq 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 559 ----ISTWDQNSSkfKRSRLKngFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQPegeksssagv 634
Cdd:cd14872 449 thaaKSTFVYAEV--RTSRTE--FIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPP---------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 635 eanisnqevkKSARTSTFKTT-SSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLA 713
Cdd:cd14872 515 ----------SEGDQKTSKVTlGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIR 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321812 714 REGYPNRIAFQEFFQRYRILypenstTTTFSSKLKASTKQNCEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14872 585 KTGYPFRYSHERFLKRYRFL------VKTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
89-777 |
1.59e-163 |
|
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: 515.88 E-value: 1.59e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKHNRlsksrlDENSHEKLPPHIFAIAEEAYENLL 168
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYYEHGER------RAAGERKLPPHVYAVADKAFRAML 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 S----EGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNIAPVSGSSIVEsfemKILQSNPILESFGNAQTVRNNN 244
Cdd:cd14901 75 FasrgQKCDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENVRD----RVLESNPILEAFGNARTNRNNN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 245 SSRFGKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKsrNVKDYKILsNSNQ- 323
Cdd:cd14901 151 SSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLT--HVEEYKYL-NSSQc 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 324 -DIIPGINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAEQASFKN----DVSAICSNLGVDEKDF 398
Cdd:cd14901 228 yDRRDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMsslaNVRAACDLLGLDMDVL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 399 QTAILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNY--IGLLDIAGFEIFENNSF 476
Cdd:cd14901 308 EKTLCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrfIGIVDIFGFEIFATNSL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 477 EQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDlQLTIDLIESKgpPTGVLPLLDEEAVLPKSTDESFYS 556
Cdd:cd14901 388 EQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEAR--PTGLFSLLDEQCLLPRGNDEKLAN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 557 KLISTWDQNSSkFKRSRLKNG---FILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISklfqpegeksssag 633
Cdd:cd14901 465 KYYDLLAKHAS-FSVSKLQQGkrqFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS-------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 634 veanisnqevkksartstfKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLA 713
Cdd:cd14901 530 -------------------STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKIS 590
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321812 714 REGYPNRIAFQEFFQRYRILYPENSTTTTFSSKLKASTKQNCEFLLTSLQlDTKVYKIGNTKLF 777
Cdd:cd14901 591 RSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIE-HLPPFQVGKTKVF 653
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
90-779 |
2.78e-162 |
|
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: 512.78 E-value: 2.78e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNL-NLYSEDHINLYHNKhnrlsksRLDEnshekLPPHIFAIAEEAYENLL 168
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIpDLYSEERMLLYHGT-------TAGE-----LPPHVFAIADHAYTQLI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEG----KDQSILVTGESGAGKTENTKKILQYLASITSGSPSNIAPVS------GSSIVESFEMKILQSNPILESFGNAQ 238
Cdd:cd14890 70 QSGvldpSNQSIIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGeaaseaIEQTLGSLEDRVLSSNPLLESFGNAK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 239 TVRNNNSSRFGKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSRNVKDYkIL 318
Cdd:cd14890 150 TLRNDNSSRFGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFY-LR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 319 SNSNQdiIPGINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEF----VSDRAEQASFKNDVSAICSNLGVD 394
Cdd:cd14890 229 GECSS--IPSCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFesenDTTVLEDATTLQSLKLAAELLGVN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 395 EKDFQTAILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENN 474
Cdd:cd14890 307 EDALEKALLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 475 SFEQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIESK--GPPtGVLPLLDEEAVLPKS-TD 551
Cdd:cd14890 387 TFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEGKvnGKP-GIFITLDDCWRFKGEeAN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 552 ESFYSKLISTWDQNSSKFKRSRLKNG--------------FILKHYAGDVEYTVEGWLSKNKDPLNDNLLsllsssqnDI 617
Cdd:cd14890 465 KKFVSQLHASFGRKSGSGGTRRGSSQhphfvhpkfdadkqFGIKHYAGDVIYDASGFNEKNNETLNAEMK--------EL 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 618 IsklfqpegeksssagveanisnqevKKSARTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLI 697
Cdd:cd14890 537 I-------------------------KQSRRSIREVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDC 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 698 LDQLRCNGVLEGIRLAREGYPNRIAFQEFFQRYRILYPENSTTT----TFSSKLKASTKQnceflltslqldtkvYKIGN 773
Cdd:cd14890 592 LRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTAENIEqlvaVLSKMLGLGKAD---------------WQIGS 656
|
....*.
gi 6321812 774 TKLFFK 779
Cdd:cd14890 657 SKIFLK 662
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
89-779 |
2.72e-161 |
|
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: 509.70 E-value: 2.72e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNL-NLYSEDhinlyhnKHNRLSKSRLDEnshekLPPHIFAIAEEAYENL 167
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLpELYTEE-------QHSKYLNKPKEE-----LPPHVYATSVAAYNHM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 168 LSEGKDQSILVTGESGAGKTENTKKILQYLASITSGspsniapVSGSSIvesfeMKILQSNPILESFGNAQTVRNNNSSR 247
Cdd:cd14903 69 KRSGRNQSILVSGESGAGKTETTKILMNHLATIAGG-------LNDSTI-----KKIIEVNPLLESFGNAKTVRNDNSSR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 248 FGKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKsrnvKDYKILSNSNQDIIP 327
Cdd:cd14903 137 FGKFTQLQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSA----NECAYTGANKTIKIE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 328 GINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAE---QASFKNDVSAICSN--LGVDEKDFQTAI 402
Cdd:cd14903 213 GMSDRKHFARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDdekSAIAPGDQGAVYATklLGLSPEALEKAL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 403 LRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENNSFEQLCIN 482
Cdd:cd14903 293 CSRTMRAAGDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCIN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 483 YTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGkDLQLTIDLIESKgppTGVLPLLDEEAVLPKSTDESFYSKLISTW 562
Cdd:cd14903 373 YANEKLQQKFTQDVFKTVQIEYEEEGIRWAHIDFA-DNQDVLAVIEDR---LGIISLLNDEVMRPKGNEESFVSKLSSIH 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 563 --DQNSSKFKRSRlKNGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQPEGEKSSSAGVEANISN 640
Cdd:cd14903 449 kdEQDVIEFPRTS-RTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGA 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 641 QevKKSARTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYPNR 720
Cdd:cd14903 528 R--RRRGGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNR 605
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 721 IAFQEFFQRYRILYPENSTTTTFssklkasTKQNCEFLLTSLQLDT-KVYKIGNTKLFFK 779
Cdd:cd14903 606 LLHEEFLDKFWLFLPEGRNTDVP-------VAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
89-736 |
3.03e-160 |
|
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: 507.31 E-value: 3.03e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNL-NLYSEDHINlyhnKHNRLSKSRldensheklPPHIFAIAEEAYENL 167
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIpGLYSDEMLL----KFIQPSISK---------SPHVFSTASSAYQGM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 168 LSEGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNIAPVsgssivesfEMKILQSNPILESFGNAQTVRNNNSSR 247
Cdd:cd14888 68 CNNKKSQTILISGESGAGKTESTKYVMKFLACAGSEDIKKRSLV---------EAQVLESNPLLEAFGNARTLRNDNSSR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 248 FGKFIKIEFNE---------HGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSRNVKD---- 314
Cdd:cd14888 139 FGKFIELQFSKlkskrmsgdRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLakga 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 315 -----------------YKILSNSNQDIIPGINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAE- 376
Cdd:cd14888 219 dakpisidmssfephlkFRYLTKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACs 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 377 -----QASFKNDVSAICSNLGVDEKDFQTAILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLD 451
Cdd:cd14888 299 egavvSASCTDDLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 452 HGSATLN-YIGLLDIAGFEIFENNSFEQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIESK 530
Cdd:cd14888 379 YSKDNSLlFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDF-PDNQDCVDLLQEK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 531 gpPTGVLPLLDEEAVLPKSTDESFYSKLISTWDQNsSKFKRSRLK-NGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSL 609
Cdd:cd14888 458 --PLGIFCMLDEECFVPGGKDQGLCNKLCQKHKGH-KRFDVVKTDpNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEV 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 610 LSSSQNDIISKLFqpegEKSSSAGVEaniSNQEVKKsartstFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKV 689
Cdd:cd14888 535 IKNSKNPFISNLF----SAYLRRGTD---GNTKKKK------FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVP 601
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 6321812 690 KTFNRRLILDQLRCNGVLEGIRLAREGYPNRIAFQEFFQRYRILYPE 736
Cdd:cd14888 602 DLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLNG 648
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
90-779 |
1.13e-157 |
|
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: 499.71 E-value: 1.13e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLN-LYSEDHINLYHNKHnrlsksrLDEnshekLPPHIFAIAEEAYENLL 168
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRH-------LGE-----LPPHIFAIANECYRCLW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEGKDQSILVTGESGAGKTENTKKILQYLASITSgspsNIAPVSGSSIVESFEMKILQSNPILESFGNAQTVRNNNSSRF 248
Cdd:cd14873 70 KRHDNQCILISGESGAGKTESTKLILKFLSVISQ----QSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 249 GKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSrnVKDYKILSNSNQDIIPG 328
Cdd:cd14873 146 GKFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLST--PENYHYLNQSGCVEDKT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 329 INDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAEQASFKNDVSAICSNLGVDEKDFqTAILRPRSK 408
Cdd:cd14873 224 ISDQESFREVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFITAGGAQVSFKTALGRSAELLGLDPTQL-TDALTQRSM 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 409 AGK-EWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLdHGSATLNYIGLLDIAGFEIFENNSFEQLCINYTNEK 487
Cdd:cd14873 303 FLRgEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRI-KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 488 LQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIESKgppTGVLPLLDEEAVLPKSTDESFYSKLISTWDQNSS 567
Cdd:cd14873 382 LQEYFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKK---LGLLALINEESHFPQATDSTLLEKLHSQHANNHF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 568 KFKRSRLKNGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFqpegEKSSSAGveanisNQEVKKSA 647
Cdd:cd14873 458 YVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF----EHVSSRN------NQDTLKCG 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 648 RTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYPNRIAFQEFF 727
Cdd:cd14873 528 SKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFY 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 6321812 728 QRYRILYPENSTTTTFSSKlkastkqnCEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14873 608 KRYKVLMRNLALPEDVRGK--------CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
90-779 |
1.68e-157 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 498.45 E-value: 1.68e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksrldeNSHEKLPPHIFAIAEEAYENLLS 169
Cdd:cd14897 2 TIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNL-----------SVRSQRPPHLFWIADQAYRRLLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 170 EGKDQSILVTGESGAGKTENTKKILQYLASITSgspsniapvsgsSIVESFEMKILQSNPILESFGNAQTVRNNNSSRFG 249
Cdd:cd14897 71 TGRNQCILVSGESGAGKTESTKYMIKHLMKLSP------------SDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 250 KFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSRNvkDYKILSNSNQDIiPGI 329
Cdd:cd14897 139 KFIELHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPD--CHRILRDDNRNR-PVF 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 330 NDVEN-------FKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSD-RAEQASFKND--VSAICSNLGVDEKDFQ 399
Cdd:cd14897 216 NDSEEleyyrqmFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDeDTDGVTVADEypLHAVAKLLGIDEVELT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 400 TAILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNL-----DHGSATLNYIGLLDIAGFEIFENN 474
Cdd:cd14897 296 EALISNVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkdFQIMTRGPSIGILDMSGFENFKIN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 475 SFEQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIESKgpPTGVLPLLDEEAVLPKSTDESF 554
Cdd:cd14897 376 SFDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFFKK--PLGILPLLDEESTFPQSTDSSL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 555 YSKLISTWDQNSSKFKRSRLKNGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFqpegeksssagv 634
Cdd:cd14897 453 VQKLNKYCGESPRYVASPGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF------------ 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 635 eanisnqevkksarTSTFKTTSSrhreqqiTLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAR 714
Cdd:cd14897 521 --------------TSYFKRSLS-------DLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRR 579
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321812 715 EGYPNRIAFQEFFQRYRILYPensttttFSSKLKASTKQNCEFLLTSLQLdtKVYKIGNTKLFFK 779
Cdd:cd14897 580 DGYPIRIKYEDFVKRYKEICD-------FSNKVRSDDLGKCQKILKTAGI--KGYQFGKTKVFLK 635
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
89-779 |
4.39e-155 |
|
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: 491.79 E-value: 4.39e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlskSRLDenshekLPPHIFAIAEEAYENLL 168
Cdd:cd01379 1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGA------KRSD------NPPHIFAVADAAYQAMI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEGKDQSILVTGESGAGKTENTKKILQYLASItsgspsniapvsGSSIVESFEMKILQSNPILESFGNAQTVRNNNSSRF 248
Cdd:cd01379 69 HQKKNQCIVISGESGAGKTESANLLVQQLTVL------------GKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 249 GKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGL-DDSELKNLRLK-SRNVKDYKILSNSNQDII 326
Cdd:cd01379 137 GKYLEMKFTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLaEDKKLAKYKLPeNKPPRYLQNDGLTVQDIV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 327 PGINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDraeQASFKNDVSAICSN----------LGVDEK 396
Cdd:cd01379 217 NNSGNREKFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEV---ESNHQTDKSSRISNpealnnvaklLGIEAD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 397 DFQTAILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSAT----LNyIGLLDIAGFEIFE 472
Cdd:cd01379 294 ELQEALTSHSVVTRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSAsdepLS-IGILDIFGFENFQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 473 NNSFEQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIESKgpPTGVLPLLDEEAVLPKSTDE 552
Cdd:cd01379 373 KNSFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEY-EDNRPLLDMFLQK--PMGLLALLDEESRFPKATDQ 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 553 SfyskLISTWDQN-SSKFKRSRLKNG--FILKHYAGDVEYTVEGWLSKNKDPLndnllsllsssQNDIISKLfqpegeks 629
Cdd:cd01379 450 T----LVEKFHNNiKSKYYWRPKSNAlsFGIHHYAGKVLYDASGFLEKNRDTL-----------PPDVVQLL-------- 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 630 ssagveanisnqevKKSARTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEG 709
Cdd:cd01379 507 --------------RSSENPLVRQTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLET 572
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321812 710 IRLAREGYPNRIAFQEFFQRYRIL-YPENSTTTtfssklkaSTKQNCEFLLTSLQLDTkvYKIGNTKLFFK 779
Cdd:cd01379 573 TRIRRQGFSHRILFADFLKRYYFLaFKWNEEVV--------ANRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
90-779 |
1.92e-150 |
|
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: 481.11 E-value: 1.92e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnRLSKsrldenshekLPPHIFAIAEEAYENLLS 169
Cdd:cd01385 2 TLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNR--RLGK----------LPPHIFAIADVAYHAMLR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 170 EGKDQSILVTGESGAGKTENTKKILQYLASI-TSGSPSNIapvsgssivesfEMKILQSNPILESFGNAQTVRNNNSSRF 248
Cdd:cd01385 70 KKKNQCIVISGESGSGKTESTNFLLHHLTALsQKGYGSGV------------EQTILGAGPVLEAFGNAKTAHNNNSSRF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 249 GKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSRnvKDYKILSNSNQDIIPG 328
Cdd:cd01385 138 GKFIQVNYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQP--EDYHYLNQSDCYTLEG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 329 INDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVS---DRAEQASFKN-DVSAICSNL-GVDEKDFQTAIL 403
Cdd:cd01385 216 EDEKYEFERLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKkayHRDESVTVGNpEVLDIISELlRVKEETLLEALT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 404 RPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNL----DHGSATLNYIGLLDIAGFEIFENNSFEQL 479
Cdd:cd01385 296 TKKTVTVGETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 480 CINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIESKgpPTGVLPLLDEEAVLPKSTDESFYSKLI 559
Cdd:cd01385 376 CINYANEHLQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISKK--PTGLLCLLDEESNFPGATNQTLLAKFK 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 560 STWDQNSSKFKRSRLKNGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKL------------------ 621
Cdd:cd01385 453 QQHKDNKYYEKPQVMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELigidpvavfrwavlraff 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 622 -----FQPEGEKSSSAGVEAN-ISNQEVKKSA---RTSTFKTTSSRHREQQIT-LLNQLASTHPHFVRCIIPNNVKKVKT 691
Cdd:cd01385 533 ramaaFREAGRRRAQRTAGHSlTLHDRTTKSLlhlHKKKKPPSVSAQFQTSLSkLMETLGQAEPFFIRCIKSNAEKKPLR 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 692 FNRRLILDQLRCNGVLEGIRLAREGYPNRIAFQEFFQRYRILYPENsttttfssklKASTKQNCEFLLTSLQLDTKVYKI 771
Cdd:cd01385 613 FDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKG----------LISSKEDIKDFLEKLNLDRDNYQI 682
|
....*...
gi 6321812 772 GNTKLFFK 779
Cdd:cd01385 683 GKTKVFLK 690
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
90-779 |
2.62e-149 |
|
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: 476.94 E-value: 2.62e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksRLDEnshekLPPHIFAIAEEAYENLLS 169
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGR-------ALGE-----LPPHLFAIANLAFAKMLD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 170 EGKDQSILVTGESGAGKTENTKKILQYLASItsgSPSNIAPVSgssivesfeMKILQSNPILESFGNAQTVRNNNSSRFG 249
Cdd:cd01387 70 AKQNQCVVISGESGSGKTEATKLIMQYLAAV---NQRRNNLVT---------EQILEATPLLEAFGNAKTVRNDNSSRFG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 250 KFIKIEFnEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKsrNVKDYKILSNSNQDIIPGI 329
Cdd:cd01387 138 KYLEVFF-EGGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQ--EAEKYFYLNQGGNCEIAGK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 330 NDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEF----VSDRAEQASFKND--VSAICSNLGVDEKDFQTAIL 403
Cdd:cd01387 215 SDADDFRRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFhkrqLRHGQEGVSVGSDaeIQWVAHLLQISPEGLQKALT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 404 RPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENNSFEQLCINY 483
Cdd:cd01387 295 FKVTETRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 484 TNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIESKgpPTGVLPLLDEEAVLPKSTDESFYSKLISTWD 563
Cdd:cd01387 375 ANENLQYYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLISKK--PVGILHILDDECNFPQATDHSFLEKCHYHHA 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 564 QNSSkFKRSRLK-NGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQPegeksssagVEANISNQE 642
Cdd:cd01387 452 LNEL-YSKPRMPlPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSS---------HRAQTDKAP 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 643 VKKS-ARTSTFK----TTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGY 717
Cdd:cd01387 522 PRLGkGRFVTMKprtpTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGY 601
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321812 718 PNRIAFQEFFQRYRILYPensttttfSSKLKASTKQNCEFLLTSLQ--LDTKVYKIGNTKLFFK 779
Cdd:cd01387 602 PVRLPFQVFIDRYRCLVA--------LKLPRPAPGDMCVSLLSRLCtvTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
89-733 |
1.80e-145 |
|
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: 466.82 E-value: 1.80e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNL-NLYSEDHINLYHNKHNRLSKSrldeNSHEKLPPHIFAIAEEAYENL 167
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIdNLFSEEVMQMYKEQIIQNGEY----FDIKKEPPHIYAIAALAFKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 168 LSEGKDQSILVTGESGAGKTENTKKILQYLASITS---------GSPSNIAPVSGSSIveSFEMKILQSNPILESFGNAQ 238
Cdd:cd14907 77 FENNKKQAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevlTLTSSIRATSKSTK--SIEQKILSCNPILEAFGNAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 239 TVRNNNSSRFGKFIKIEFNEH-GMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSRNVKD-YK 316
Cdd:cd14907 155 TVRNDNSSRFGKYVSILVDKKkRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSGDrYD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 317 ILSNSNQDIIPGINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEF-----VSDRAEQASFKNDVSAICSNL 391
Cdd:cd14907 235 YLKKSNCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFddstlDDNSPCCVKNKETLQIIAKLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 392 GVDEKDFQTAILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNY--------IGLL 463
Cdd:cd14907 315 GIDEEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMPKDEKDQQlfqnkylsIGLL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 464 DIAGFEIFENNSFEQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQwDYIDY--GKDLQLTIDLIESkgPPTGVLPLLD 541
Cdd:cd14907 395 DIFGFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLE-DYLNQlsYTDNQDVIDLLDK--PPIGIFNLLD 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 542 EEAVLPKSTDESFYSKLISTWDQNSS-KFKRSRLKNGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISK 620
Cdd:cd14907 472 DSCKLATGTDEKLLNKIKKQHKNNSKlIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISS 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 621 LFQpeGEKSSSAGVEANISNQEVKKsartstfKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQ 700
Cdd:cd14907 552 IFS--GEDGSQQQNQSKQKKSQKKD-------KFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQ 622
|
650 660 670
....*....|....*....|....*....|...
gi 6321812 701 LRCNGVLEGIRLAREGYPNRIAFQEFFQRYRIL 733
Cdd:cd14907 623 IRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLL 655
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
90-733 |
1.11e-144 |
|
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: 463.24 E-value: 1.11e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNL-NLYSEDHINLYHNKHNRLSKSRLDENShEKLPPHIFAIAEEAYE--- 165
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLpGLYSSDTMAKYLLSFEARSSSTRNKGS-DPMPPHIYQVAGEAYKamm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 166 -NLLSEGKDQSILVTGESGAGKTENTKKILQYLASItsGSPSNIAPVSGSSIVESFEMKILQSNPILESFGNAQTVRNNN 244
Cdd:cd14900 81 lGLNGVMSDQSILVSGESGSGKTESTKFLMEYLAQA--GDNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 245 SSRFGKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNlrlksrnvkdykilsnsnqd 324
Cdd:cd14900 159 SSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKR-------------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 325 iipgindvENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAEQ--ASFKNDVSAIC--------SNLGVD 394
Cdd:cd14900 219 --------DMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrlGQLKSDLAPSSiwsrdaaaTLLSVD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 395 EKDFQTAILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDH-----GSATLNYIGLLDIAGFE 469
Cdd:cd14900 291 ATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMddsskSHGGLHFIGILDIFGFE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 470 IFENNSFEQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIESKgpPTGVLPLLDEEAVLPKS 549
Cdd:cd14900 371 VFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLISQR--PTGILSLIDEECVMPKG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 550 TDESFYSKLISTWdQNSSKFKRSRLKNG---FILKHYAGDVEYTVEGWLSKNKDPLNDNllsllsssqndiISKLFQPEG 626
Cdd:cd14900 448 SDTTLASKLYRAC-GSHPRFSASRIQRArglFTIVHYAGHVEYSTDGFLEKNKDVLHQE------------AVDLFVYGL 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 627 EksssagveanisnqevkksartstFKttssrhrEQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGV 706
Cdd:cd14900 515 Q------------------------FK-------EQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGV 563
|
650 660
....*....|....*....|....*..
gi 6321812 707 LEGIRLAREGYPNRIAFQEFFQRYRIL 733
Cdd:cd14900 564 MEAVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
91-779 |
1.82e-144 |
|
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: 462.98 E-value: 1.82e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 91 VLYNLEKRYDCDLI--YTYSGLFLVAINPYHNLnlySEDHINLYHNKhnrlsksrldenSHEKLPPHIFAIAEEAYENL- 167
Cdd:cd14891 3 ILHNLEERSKLDNQrpYTFMANVLIAVNPLRRL---PEPDKSDYINT------------PLDPCPPHPYAIAEMAYQQMc 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 168 LSEGKD--QSILVTGESGAGKTENTKKILQYL------ASITSGSPSNIAPVSGSSIVESFEMKILQSNPILESFGNAQT 239
Cdd:cd14891 68 LGSGRMqnQSIVISGESGAGKTETSKIILRFLttravgGKKASGQDIEQSSKKRKLSVTSLDERLMDTNPILESFGNAKT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 240 VRNNNSSRFGKFIKIEF-NEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSrnVKDYKIL 318
Cdd:cd14891 148 LRNHNSSRFGKFMKLQFtKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLS--PEDFIYL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 319 SNSNQDIIPGINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAEQA-------SFKNDVSAICSNL 391
Cdd:cd14891 226 NQSGCVSDDNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGeaeiaseSDKEALATAAELL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 392 GVDEKDFQTAILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIF 471
Cdd:cd14891 306 GVDEEALEKVITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 472 E-NNSFEQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIESKgpPTGVLPLLDEEAVLPKST 550
Cdd:cd14891 386 EtKNDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITW-PDNRECLDLIASK--PNGILPLLDNEARNPNPS 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 551 DESFYSKLISTWDQNSSkFKRSRLKN---GFILKHYAGDVEYTVEGWLSKNkdplndnllsllsssqNDIISKLFqpege 627
Cdd:cd14891 463 DAKLNETLHKTHKRHPC-FPRPHPKDmreMFIVKHYAGTVSYTIGSFIDKN----------------NDIIPEDF----- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 628 ksssagveanisnqevkksartSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVL 707
Cdd:cd14891 521 ----------------------EDLLASSAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGIL 578
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321812 708 EGIRLAREGYPNRIAFQEFFQRYRILYPEnSTTTTFSSKLKASTkqncEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14891 579 QTCEVLKVGLPTRVTYAELVDVYKPVLPP-SVTRLFAENDRTLT----QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
89-768 |
7.21e-143 |
|
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: 461.28 E-value: 7.21e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNL-NLYSEDHINLY-HNKHNRLSKSRLDEnshekLPPHIFAIAEEAYEN 166
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLpDLYSESQLNAYkASMTSTSPVSQLSE-----LPPHVFAIGGKAFGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 167 LL-SEGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNIAPVSGSSIVESfemKILQSNPILESFGNAQTVRNNNS 245
Cdd:cd14902 76 LLkPERRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAVEIGK---RILQTNPILESFGNAQTIRNDNS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 246 SRFGKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKsrNVKDYKILSNS---- 321
Cdd:cd14902 153 SRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQ--KGGKYELLNSYgpsf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 322 NQDIIPGINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFvsDRAEQASFKNDVSAICSN--------LGV 393
Cdd:cd14902 231 ARKRAVADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNF--TAENGQEDATAVTAASRFhlakcaelMGV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 394 DEKDFQTAILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSAT---------LNYIGLLD 464
Cdd:cd14902 309 DVDKLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAvsisdedeeLATIGILD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 465 IAGFEIFENNSFEQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQlTIDLIESKgpPTGVLPLLDEEA 544
Cdd:cd14902 389 IFGFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAA-CLALFDDK--SNGLFSLLDQEC 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 545 VLPKSTDESFysklistwdqnSSKFKRSRLKNG-FILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQ 623
Cdd:cd14902 466 LMPKGSNQAL-----------STKFYRYHGGLGqFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 624 peGEKSSSAGVEANisnqeVKKSARTSTFKT--TSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQL 701
Cdd:cd14902 535 --DENRDSPGADNG-----AAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQM 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321812 702 RCNGVLEGIRLAREGYPNRIAFQEFFQRYRILYPENSTTTTFSSKLK-ASTKQNCEFLLTSLQLDTKV 768
Cdd:cd14902 608 RSVGVLEAVRIARHGYSVRLAHASFIELFSGFKCFLSTRDRAAKMNNhDLAQALVTVLMDRVLLEDGV 675
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
46-821 |
1.14e-137 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 450.25 E-value: 1.14e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 46 IVHPLDSTEVSNLVQ----------VRISDVF----PVNPSTFDKVeNMseLTHLNEPSVLYNLEKRYDCDLIYTYSGLF 111
Cdd:PTZ00014 56 LVLPGSTGEKLTLKQidpptnstfeVKPEHAFnansQIDPMTYGDI-GL--LPHTNIPCVLDFLKHRYLKNQIYTTADPL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 112 LVAINPYHNLNLYSEDHINLYHnkhnrlsksrlDENSHEKLPPHIFAIAEEAYENLLSEGKDQSILVTGESGAGKTENTK 191
Cdd:PTZ00014 133 LVAINPFKDLGNTTNDWIRRYR-----------DAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 192 KILQYLASITSGSPSniapvsgssivESFEMKILQSNPILESFGNAQTVRNNNSSRFGKFIKIEFNEHGMINGAHIEWYL 271
Cdd:PTZ00014 202 QIMRYFASSKSGNMD-----------LKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 272 LEKSRIVHQNSKERNYHIFYQLLSGLDDsELKNlRLKSRNVKDYKILSNSNQDiIPGINDVENFKELLSALNIIGFSKDQ 351
Cdd:PTZ00014 271 LEKSRVVTQEDDERSYHIFYQLLKGAND-EMKE-KYKLKSLEEYKYINPKCLD-VPGIDDVKDFEEVMESFDSMGLSESQ 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 352 IRWIFQVVAIILLIGNIEFVSdraEQASFKNDVSAI-----------CSNLGVDEKDFQTAILRPRSKAGKEWVSQSKNS 420
Cdd:PTZ00014 348 IEDIFSILSGVLLLGNVEIEG---KEEGGLTDAAAIsdeslevfneaCELLFLDYESLKKELTVKVTYAGNQKIEGPWSK 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 421 QQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENNSFEQLCINYTNEKLQQFFNNHMFVLE 500
Cdd:PTZ00014 425 DESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERE 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 501 QSEYLKENIQWDYIDYgKDLQLTIDLIESKGppTGVLPLLDEEAVLPKSTDESFYSKLISTWdQNSSKFKRSRL-KNG-F 578
Cdd:PTZ00014 505 SKLYKDEGISTEELEY-TSNESVIDLLCGKG--KSVLSILEDQCLAPGGTDEKFVSSCNTNL-KNNPKYKPAKVdSNKnF 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 579 ILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQpegeksssaGVEAnisnqEVKKSARTSTFkttSSR 658
Cdd:PTZ00014 581 VIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFE---------GVEV-----EKGKLAKGQLI---GSQ 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 659 HREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYPNRIAFQEFFQRYRILypenS 738
Cdd:PTZ00014 644 FLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYL----D 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 739 TTTTFSSKLKASTKqnCEFLLTSLQLDTKVYKIGNTKLFFK---AGVLADLEKQKDVKLNNIMIKLTATIRGYTVRKEIT 815
Cdd:PTZ00014 720 LAVSNDSSLDPKEK--AEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKVR 797
|
....*.
gi 6321812 816 YHLQKL 821
Cdd:PTZ00014 798 KNIKSL 803
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
91-779 |
1.01e-135 |
|
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: 439.34 E-value: 1.01e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 91 VLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYhnkhnrlsksRLDENSheKLPPHIFAIAEEAYENLLSE 170
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKY----------KCEKKS--SLPPHIFAVADRAYQSMLGR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 171 G----KDQSILVTGESGAGKTENTKKILQYLASITSGSpsniapvsgssivESFEMKILQSNPILESFGNAQTVRNNNSS 246
Cdd:cd14889 71 LargpKNQCIVISGESGAGKTESTKLLLRQIMELCRGN-------------SQLEQQILQVNPLLEAFGNAQTVMNDNSS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 247 RFGKFIKIEFnEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLksRNVKDYKILSN--SNQD 324
Cdd:cd14889 138 RFGKYIQLRF-RNGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGL--LDPGKYRYLNNgaGCKR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 325 IIPGINdvENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAEQASFKND----VSAICSNLGVDEKDFQT 400
Cdd:cd14889 215 EVQYWK--KKYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEALKVENDsngwLKAAAGQFGVSEEDLLK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 401 AILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNL---DHGSATLNYIGLLDIAGFEIFENNSFE 477
Cdd:cd14889 293 TLTCTVTFTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLapkDDSSVELREIGILDIFGFENFAVNRFE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 478 QLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIESKgpPTGVLPLLDEEAVLPKSTDESFYSK 557
Cdd:cd14889 373 QACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFLNK--PIGILSLLDEQSHFPQATDESFVDK 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 558 LISTWDQNSSKFKRSRLKNGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQpeGEKSSSAGVEAN 637
Cdd:cd14889 450 LNIHFKGNSYYGKSRSKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFT--ATRSRTGTLMPR 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 638 ISNQEVKKSARTSTFK-TTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREG 716
Cdd:cd14889 528 AKLPQAGSDNFNSTRKqSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREG 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321812 717 YPNRIAFQEFFQRYRILYPENSTTTtfssklkasTKQNCEFLLTSLQLdtKVYKIGNTKLFFK 779
Cdd:cd14889 608 FSWRPSFAEFAERYKILLCEPALPG---------TKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
89-779 |
1.93e-132 |
|
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: 431.68 E-value: 1.93e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNlysedhiNLYHnkhnrLSKSRLDENSHEKLPPHIFAIAEEAYENLL 168
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYD-----LHKYREEMPGWTALPPHVFSIAEGAYRSLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 -------SEGKDQSILVTGESGAGKTENTKKILQYLASItsgSPSNIAPVSGSSIVESFEMKILQSNPILESFGNAQTVR 241
Cdd:cd14895 69 rrlhepgASKKNQTILVSGESGAGKTETTKFIMNYLAES---SKHTTATSSSKRRRAISGSELLSANPILESFGNARTLR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 242 NNNSSRFGKFIKIEFNEHGM-----INGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSRNVKDYK 316
Cdd:cd14895 146 NDNSSRFGKFVRMFFEGHELdtslrMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQEFQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 317 ILSNSN----QDiipGINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAEQASFKNDV-SAIC--- 388
Cdd:cd14895 226 YISGGQcyqrND---GVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAaSAPCrla 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 389 -----------------SNLGVDEKDFQTAILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINK--- 448
Cdd:cd14895 303 saspssltvqqhldivsKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSasp 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 449 --------NLDHGSATLNYIGLLDIAGFEIFENNSFEQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDL 520
Cdd:cd14895 383 qrqfalnpNKAANKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDY-EDN 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 521 QLTIDLIESKgpPTGVLPLLDEEAVLPKSTDESFYSKLISTWdQNSSKFKRSRLKN---GFILKHYAGDVEYTVEGWLSK 597
Cdd:cd14895 462 SVCLEMLEQR--PSGIFSLLDEECVVPKGSDAGFARKLYQRL-QEHSNFSASRTDQadvAFQIHHYAGAVRYQAEGFCEK 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 598 NKDPLNDNLLSLLSSSQNDIISKLFQPegeksSSAGVEANISNQEVKKSARTSTFKTT--SSRHREQQITLLNQLASTHP 675
Cdd:cd14895 539 NKDQPNAELFSVLGKTSDAHLRELFEF-----FKASESAELSLGQPKLRRRSSVLSSVgiGSQFKQQLASLLDVVQQTQT 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 676 HFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYPNRIAFQEFFQRYRILypensTTTTFSSKLKASTkqnc 755
Cdd:cd14895 614 HYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLL-----VAAKNASDATASA---- 684
|
730 740
....*....|....*....|....
gi 6321812 756 efLLTSLQLDTKvyKIGNTKLFFK 779
Cdd:cd14895 685 --LIETLKVDHA--ELGKTRVFLR 704
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
89-779 |
2.74e-131 |
|
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: 426.67 E-value: 2.74e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNL-NLYSeDHINLYHNKHNRlsksrldenshEKLPPHIFAIAEEAYENL 167
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIdNLYG-DHLHEQYLKKPR-----------DKLQPHVYATSTAAYKHM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 168 LSEGKDQSILVTGESGAGKTENTKKILQYLASITSG-SPSNIApvsgssivesfemKILQSNPILESFGNAQTVRNNNSS 246
Cdd:cd14904 69 LTNEMNQSILVSGESGAGKTETTKIVMNHLASVAGGrKDKTIA-------------KVIDVNPLLESFGNAKTTRNDNSS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 247 RFGKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSRnvKDYKILSNS-NQDI 325
Cdd:cd14904 136 RFGKFTQLQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPN--CQYQYLGDSlAQMQ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 326 IPGINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFvSDRAEQASFKNDVSAIC---SNLGVDEKDFQTAI 402
Cdd:cd14904 214 IPGLDDAKLFASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSqvaKMLGLPTTRIEEAL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 403 LRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLD-HGSATLNYIGLLDIAGFEIFENNSFEQLCI 481
Cdd:cd14904 293 CNRSVVTRNESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAIStDDDRIKGQIGVLDIFGFEDFAHNGFEQFCI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 482 NYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIESKgppTGVLPLLDEEAVLPKSTDESFYSK---- 557
Cdd:cd14904 373 NYANEKLQQKFTTDVFKTVEEEYIREGLQWDHIEY-QDNQGIVEVIDGK---MGIIALMNDHLRQPRGTEEALVNKirtn 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 558 LISTWDQNSSKFKRSRlKNGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQpegeksssaGVEAN 637
Cdd:cd14904 449 HQTKKDNESIDFPKVK-RTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFG---------SSEAP 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 638 ISNQEVKKSARTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGY 717
Cdd:cd14904 519 SETKEGKSGKGTKAPKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGY 598
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321812 718 PNRIAFQEFFQRYRILYPensttttfSSKLKASTKQNCEFLLTSLQLDTKV-YKIGNTKLFFK 779
Cdd:cd14904 599 PSRLTPKELATRYAIMFP--------PSMHSKDVRRTCSVFMTAIGRKSPLeYQIGKSLIYFK 653
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
89-779 |
6.78e-131 |
|
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: 425.56 E-value: 6.78e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHnkhnrlsksrlDENSHEKLPPHIFAIAEEAYENLL 168
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYR-----------DAPDLTKLPPHVFYTARRALENLH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNiapvsgssiveSFEMKILQSNPILESFGNAQTVRNNNSSRF 248
Cdd:cd14876 70 GVNKSQTIIVSGESGAGKTEATKQIMRYFASAKSGNMDL-----------RIQTAIMAANPVLEAFGNAKTIRNNNSSRF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 249 GKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDsELKNlRLKSRNVKDYKILSNSNQDiIPG 328
Cdd:cd14876 139 GRFMQLDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADS-EMKS-KYHLLGLKEYKFLNPKCLD-VPG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 329 INDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAE----QASFKNDVSAI----CSNLGVDEKDFQT 400
Cdd:cd14876 216 IDDVADFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQgvddAAAISNESLEVfkeaCSLLFLDPEALKR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 401 AILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENNSFEQLC 480
Cdd:cd14876 296 ELTVKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 481 INYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLtIDLIESKGppTGVLPLLDEEAVLPKSTDESFYSKLIS 560
Cdd:cd14876 376 INITNEMLQKNFIDIVFERESKLYKDEGIPTAELEYTSNAEV-IDVLCGKG--KSVLSILEDQCLAPGGSDEKFVSACVS 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 561 TWdQNSSKFKRSRLKN--GFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFqpEGEKsssagVEANi 638
Cdd:cd14876 453 KL-KSNGKFKPAKVDSniNFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALF--EGVV-----VEKG- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 639 snqevkKSARTSTFKTTSSRHREQQITLLNqlaSTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYP 718
Cdd:cd14876 524 ------KIAKGSLIGSQFLKQLESLMGLIN---STEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYS 594
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321812 719 NRIAFQEFFQRYRILYPenstttTFSSKLKASTKQNCEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14876 595 YRRPFEEFLYQFKFLDL------GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
89-737 |
5.20e-128 |
|
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: 418.54 E-value: 5.20e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhNRLSKSRLDenSHEKLPPHIFAIAEEAYENLL 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRQE-GLLRSQGIE--SPQALGPHVFAIADRSYRQMM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEG-KDQSILVTGESGAGKTENTKKILQYLAsiTSGSPSNIAPVSGSSIVESFEM-KILQSNPILESFGNAQTVRNNNSS 246
Cdd:cd14908 78 SEIrASQSILISGESGAGKTESTKIVMLYLT--TLGNGEEGAPNEGEELGKLSIMdRVLQSNPILEAFGNARTLRNDNSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 247 RFGKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSRNVKDYKILSN---SNQ 323
Cdd:cd14908 156 RFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGGLQLPNEfhyTGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 324 DIIPGINDVENFKEL---LSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVS----DRAEQASFKND--VSAICSNLGVD 394
Cdd:cd14908 236 GGAPDLREFTDEDGLvytLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESkeedGAAEIAEEGNEkcLARVAKLLGVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 395 EKDFQTAILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINK--NLDHGSATLNYIGLLDIAGFEIFE 472
Cdd:cd14908 316 VDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSsiNWENDKDIRSSVGVLDIFGFECFA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 473 NNSFEQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIEskGPPTGVLPLLDEEAVLP-KSTD 551
Cdd:cd14908 396 HNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEF-PDNQDCLDTIQ--AKKKGILTMLDDECRLGiRGSD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 552 ESFYSKLISTW----DQNSSKFKR------SRLKNGFILKHYAGDVEYTVE-GWLSKNKDPLNDNLLSllsssqndiisk 620
Cdd:cd14908 473 ANYASRLYETYlpekNQTHSENTRfeatsiQKTKLIFAVRHFAGQVQYTVEtTFCEKNKDEIPLTADS------------ 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 621 LFQpegeksssagveanisnqevkksartstfktTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQ 700
Cdd:cd14908 541 LFE-------------------------------SGQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQ 589
|
650 660 670
....*....|....*....|....*....|....*..
gi 6321812 701 LRCNGVLEGIRLAREGYPNRIAFQEFFQRYRILYPEN 737
Cdd:cd14908 590 LRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPLI 626
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
89-779 |
7.78e-124 |
|
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: 405.32 E-value: 7.78e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksRLDENsheklPPHIFAIAEEAYENLL 168
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPR-------KALNT-----TPHIFAIAASAYRLSQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEGKDQSILVTGESGAGKTENTKKILQYLASITSGSPS-NIAPVsgssivesfeMKILqsnPILESFGNAQTVRNNNSSR 247
Cdd:cd14896 69 STGQDQCILLSGHSGSGKTEAAKKIVQFLSSLYQDQTEdRLRQP----------EDVL---PILESFGHAKTILNANASR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 248 FGKFIKIEFnEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSrnVKDYKILSNSNQDIIP 327
Cdd:cd14896 136 FGQVLRLHL-QHGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQG--PETYYYLNQGGACRLQ 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 328 GINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSdrAEQASFknDVSAICSN---------LGVDEKDF 398
Cdd:cd14896 213 GKEDAQDFEGLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSS--SERESQ--EVAAVSSWaeihtaarlLQVPPERL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 399 QTAILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLD--HGSATLNYIGLLDIAGFEIFENNSF 476
Cdd:cd14896 289 EGAVTHRVTETPYGRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAppGEAESDATIGVVDAYGFEALRVNGL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 477 EQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIdYGKDLQLTIDLIESKgpPTGVLPLLDEEAVLPKSTDESFYS 556
Cdd:cd14896 369 EQLCINLASERLQLFSSQTLLAQEEEECQRELLPWVPI-PQPPRESCLDLLVDQ--PHSLLSILDDQTWLSQATDHTFLQ 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 557 KLISTWDQNSSKFKRSRLKNGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQpegEKSSSAGVEA 636
Cdd:cd14896 446 KCHYHHGDHPSYAKPQLPLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQ---EAEPQYGLGQ 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 637 NISnqevkksartstfkTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREG 716
Cdd:cd14896 523 GKP--------------TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEG 588
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321812 717 YPNRIAFQEFFQRYRILYPENSTTttfssklkASTKQNCEFLLTS-LQLDTKVYKIGNTKLFFK 779
Cdd:cd14896 589 FPVRVPFQAFLARFGALGSERQEA--------LSDRERCGAILSQvLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
90-777 |
2.94e-115 |
|
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: 381.51 E-value: 2.94e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNL-NLYSEDHINLYHNKHNRlsksrldenshEKLPPHIFAIAEEAYENLL 168
Cdd:cd14880 2 TVLRCLQARYTADTFYTNAGCTLVALNPFKPVpQLYSPELMREYHAAPQP-----------QKLKPHIFTVGEQTYRNVK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 S--EGKDQSILVTGESGAGKTENTKKILQYLASItSGSPSNIapvSGSSIVESFEMKILQSNPILESFGNAQTVRNNNSS 246
Cdd:cd14880 71 SliEPVNQSIVVSGESGAGKTWTSRCLMKFYAVV-AASPTSW---ESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 247 RFGKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSRnvKDYKILSNSNQDIi 326
Cdd:cd14880 147 RFGKFIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEG--AAFSWLPNPERNL- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 327 pginDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVS--DRAEQASFKND----VSAICSNLGVDEKDFQT 400
Cdd:cd14880 224 ----EEDCFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADseDEAQPCQPMDDtkesVRTSALLLKLPEDHLLE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 401 AiLRPRS-KAGKEWVSQSKNSQQAKFIL--NALSRNLYERLFGYIVDMINKNL--DHGSATlNYIGLLDIAGFEIFENNS 475
Cdd:cd14880 300 T-LQIRTiRAGKQQQVFKKPCSRAECDTrrDCLAKLIYARLFDWLVSVINSSIcaDTDSWT-TFIGLLDVYGFESFPENS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 476 FEQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIEskGPPTGVLPLLDEEAVLPKSTDESFY 555
Cdd:cd14880 378 LEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 556 SKLISTWDQNSSKFKRSRL--KNGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQPEGEKSSsag 633
Cdd:cd14880 455 QTRIESALAGNPCLGHNKLsrEPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKT--- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 634 veanisnQEVKKSARTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLA 713
Cdd:cd14880 532 -------QEEPSGQSRAPVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHIS 604
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321812 714 REGYPNRIAFQEFFQRYRILYPensttttfsskLKASTKQNCEFLLTSLQLDTKVYkIGNTKLF 777
Cdd:cd14880 605 AAGFPIRVSHQNFVERYKLLRR-----------LRPHTSSGPHSPYPAKGLSEPVH-CGRTKVF 656
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
90-775 |
3.80e-113 |
|
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: 377.40 E-value: 3.80e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNL-NLYSEDHINLYHnkhnrlsksrlDENSHEKLPPHIFAIAEEAYENLL 168
Cdd:cd14906 2 IILNNLGKRYKSDSIYTYIGNVLISINPYKDIsSIYSNLILNEYK-----------DINQNKSPIPHIYAVALRAYQSMV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEGKDQSILVTGESGAGKTENTKKILQYLASiTSGSPSNiAPVSGSSIVESFEMKILQSNPILESFGNAQTVRNNNSSRF 248
Cdd:cd14906 71 SEKKNQSIIISGESGSGKTEASKTILQYLIN-TSSSNQQ-QNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 249 GKFIKIEF-NEHGMINGAHIEWYLLEKSRIVHQ-NSKERNYHIFYQLLSGLDDSELKNLRLKSrNVKDYKILsNSNQDII 326
Cdd:cd14906 149 GKFLKIEFrSSDGKIDGASIETYLLEKSRISHRpDNINLSYHIFYYLVYGASKDERSKWGLNN-DPSKYRYL-DARDDVI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 327 PGIND---------------VENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDR------AEQASFKNDVS 385
Cdd:cd14906 227 SSFKSqssnknsnhnnktesIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfskyaYQKDKVTASLE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 386 AICSNLGVDEKDFQTAILRPRSKAGKEW--------VSQSKNSQqakfilNALSRNLYERLFGYIVDMIN---------K 448
Cdd:cd14906 307 SVSKLLGYIESVFKQALLNRNLKAGGRGsvycrpmeVAQSEQTR------DALSKSLYVRLFKYIVEKINrkfnqntqsN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 449 NLDHGSATLN--YIGLLDIAGFEIFENNSFEQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDL 526
Cdd:cd14906 381 DLAGGSNKKNnlFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIEL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 527 IESKGppTGVLPLLDEEAVLPKSTDESFYSKLISTWDQNSSKFKRSRLKNGFILKHYAGDVEYTVEGWLSKNKDPLNDNL 606
Cdd:cd14906 460 IEKKS--DGILSLLDDECIMPKGSEQSLLEKYNKQYHNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDV 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 607 LSLLSSSQNDIISKLFQPEgeksssagvEANISNQEVKKSARTstfkTTSSRHREQQITLLNQLASTHPHFVRCIIPNNV 686
Cdd:cd14906 538 EDLLLASSNFLKKSLFQQQ---------ITSTTNTTKKQTQSN----TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQT 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 687 KKVKTFNRRLILDQLRCNGVLEGIRLAREGYPNRIAFQEFFQRYRILypenstTTTFSSKLKASTKQNCEFLLTSLQLDT 766
Cdd:cd14906 605 MDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCI------VDMYNRKNNNNPKLASQLILQNIQSKL 678
|
....*....
gi 6321812 767 KVYKIGNTK 775
Cdd:cd14906 679 KTMGISNNK 687
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
90-779 |
6.10e-109 |
|
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: 363.36 E-value: 6.10e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYD-CDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNkhnrLSKSRLdenshekLPPHIFAIAEEAYENLL 168
Cdd:cd14875 2 TLLHCIKERFEkLHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLA----LPDPRL-------LPPHIWQVAHKAFNAIF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEGKD-QSILVTGESGAGKTENTKKILQYLASITSGSPSNiapVSGSSIVESFEMKILQSNPILESFGNAQTVRNNNSSR 247
Cdd:cd14875 71 VQGLGnQSVVISGESGSGKTENAKMLIAYLGQLSYMHSSN---TSQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 248 FGKFIKIEFNE-HGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNL-RLKSrnVKDYKILSNSNQDI 325
Cdd:cd14875 148 FGKYIKLYFDPtSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKT--AQDYKCLNGGNTFV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 326 IPG-----INDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAEQASFKND--VSAICSNLGVDEKDF 398
Cdd:cd14875 226 RRGvdgktLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADEtpFLTACRLLQLDPAKL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 399 QTAILrprSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLN--YIGLLDIAGFEIFENNSF 476
Cdd:cd14875 306 RECFL---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCSGckYIGLLDIFGFENFTRNSF 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 477 EQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIESKgpPTGVLPLLDEEAVLPKSTDESFYS 556
Cdd:cd14875 383 EQLCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEF-PDNSECVNMFDQK--RTGIFSMLDEECNFKGGTTERFTT 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 557 KLISTWDQNSSKF--KRSRLKNGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQPEgeksssagv 634
Cdd:cd14875 460 NLWDQWANKSPYFvlPKSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTE--------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 635 eanisnqevKKSARTStfKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAR 714
Cdd:cd14875 531 ---------KGLARRK--QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKR 599
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321812 715 EGYPNRIAFQEFFqRYRILYPENSTTTTFssKLKASTKQNCEFLLTSLQL---DTKVYKIGNTKLFFK 779
Cdd:cd14875 600 QGYPVRRPIEQFC-RYFYLIMPRSTASLF--KQEKYSEAAKDFLAYYQRLygwAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
95-779 |
1.56e-108 |
|
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: 361.90 E-value: 1.56e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 95 LEKRYDCDLIYTYSGLFLVAINPYHNL-NLYSEDHINLYHNKHNRLSKSrldenshEKLPPHIFAIAEEAYENLLSEGKD 173
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIrNLYGTEVIGRYRQADTSRGFP-------SDLPPHSYAVAQSALNGLISDGIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 174 QSILVTGESGAGKTENTKKILQYLAsitsgspsnIAPVSGSSIVESFemkILQSNPILESFGNAQTVRNNNSSRFGKFIK 253
Cdd:cd14886 80 QSCIVSGESGAGKTETAKQLMNFFA---------YGHSTSSTDVQSL---ILGSNPLLESFGNAKTLRNNNSSRFGKFIK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 254 IEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSrnVKDYKILSNSNQDIIPGINDVE 333
Cdd:cd14886 148 LLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKS--LESYNFLNASKCYDAPGIDDQK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 334 NFKELLSALNIIgFSKDQIRWIFQVVAIILLIGNIEF------VSDRAEQASFKNDVSAICSNLGVDEKDFQTAILRPRS 407
Cdd:cd14886 226 EFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFseegdmGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 408 KAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENNSFEQLCINYTNEK 487
Cdd:cd14886 305 VINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANER 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 488 LQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQltIDLIESKgPPTGVLPLLDEEAVLPKSTDESFYSKLISTWDQNSS 567
Cdd:cd14886 385 LQQYFINQVFKSEIQEYEIEGIDHSMITFTDNSN--VLAVFDK-PNLSIFSFLEEQCLIQTGSSEKFTSSCKSKIKNNSF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 568 -KFKRSRLKngFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQpegeksssagvEANISNQEVKKS 646
Cdd:cd14886 462 iPGKGSQCN--FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFS-----------DIPNEDGNMKGK 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 647 ARTSTFkttssrhREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYPNRIAFQEF 726
Cdd:cd14886 529 FLGSTF-------QLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEF 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 6321812 727 FQRYRILYPENSTTTTFSSKLKASTKQncefLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14886 602 FHRNKILISHNSSSQNAGEDLVEAVKS----ILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
90-779 |
1.37e-104 |
|
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: 350.65 E-value: 1.37e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKHNRLSKSrldenshekLPPHIFAIAEEAYENLLS 169
Cdd:cd14878 2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLSSSGQLCSS---------LPPHLFSCAERAFHQLFQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 170 EGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSniapvsgssiveSFEMKILQSNPILESFGNAQTVRNNNSSRFG 249
Cdd:cd14878 73 ERRPQCFILSGERGSGKTEASKQIMKHLTCRASSSRT------------TFDSRFKHVNCILEAFGHAKTTLNDLSSCFI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 250 KFIKIEFNEH-GMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKsrNVKDYKILSNSNQDIIPG 328
Cdd:cd14878 141 KYFELQFCERkKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLN--NLCAHRYLNQTMREDVST 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 329 IN---DVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAEQASFKND---VSAICSNLGVDEKDFQTAI 402
Cdd:cd14878 219 AErslNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDlqlLEQVAGMLQVSTDELASAL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 403 LRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNY----IGLLDIAGFEIFENNSFEQ 478
Cdd:cd14878 299 TTDIQYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtldIGILDIFGFEEFQKNEFEQ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 479 LCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIESKgpPTGVLPLLDEEAVLPKSTDESFYSKL 558
Cdd:cd14878 379 LCVNMTNEKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDFFFQK--PSGFLSLLDEESQMIWSVEPNLPKKL 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 559 ISTWDQNSSKFKRSRLKNG------------FILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQpeg 626
Cdd:cd14878 457 QSLLESSNTNAVYSPMKDGngnvalkdqgtaFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ--- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 627 eksssagveanisnqevkksartSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGV 706
Cdd:cd14878 534 -----------------------SKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGV 590
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321812 707 LEGIRLAREGYPNRIAFQEFFQRYRILypensTTTTFSSKLKASTKQNCEFLLtsLQLDTKVYKIGNTKLFFK 779
Cdd:cd14878 591 LEMVKIFRYGYPVRLSFSDFLSRYKPL-----ADTLLGEKKKQSAEERCRLVL--QQCKLQGWQMGVRKVFLK 656
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
90-731 |
3.41e-104 |
|
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: 351.71 E-value: 3.41e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNL-NLYSEDHINLYHNKHNRLSKSRLdeNSHEKLPPHIFAIAEEAYENLL 168
Cdd:cd14899 2 SILNALRLRYERHAIYTHIGDILISINPFQDLpQLYGDEILRGYAYDHNSQFGDRV--TSTDPREPHLFAVARAAYIDIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEGKDQSILVTGESGAGKTENTKKILQYLAsITSGSPSNIAPVSGSSIVE------SFEMKILQSNPILESFGNAQTVRN 242
Cdd:cd14899 80 QNGRSQSILISGESGAGKTEATKIIMTYFA-VHCGTGNNNLTNSESISPPaspsrtTIEEQVLQSNPILEAFGNARTVRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 243 NNSSRFGKFIKIEF-NEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDD---SELKNLRLKSRNVKDYKIL 318
Cdd:cd14899 159 DNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADNNcvsKEQKQVLALSGGPQSFRLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 319 SNS----NQDiipGINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEF--VSDRAEQASFKNDVSAICSNLG 392
Cdd:cd14899 239 NQSlcskRRD---GVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqIPHKGDDTVFADEARVMSSTTG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 393 VDEKDFQTAILRPRSKAG------KEWVSQSKNS-------QQAKFILNALSRNLYERLFGYIVDMIN------------ 447
Cdd:cd14899 316 AFDHFTKAAELLGVSTEAldhaltKRWLHASNETlvvgvdvAHARNTRNALTMECYRLLFEWLVARVNnklqrqasapwg 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 448 ---KNLDHGSATLNYIGLLDIAGFEIFENNSFEQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDlQLTI 524
Cdd:cd14899 396 adeSDVDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 525 DLIESKgpPTGVLPLLDEEAVLPKSTDESFYSKLISTWDQNSS--KFKRSRL---KNGFILKHYAGDVEYTVEGWLSKNK 599
Cdd:cd14899 475 ELFEHR--PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNShpHFRSAPLiqrTTQFVVAHYAGCVTYTIDGFLAKNK 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 600 DPLNDNLLSLLSSSQNDIISKLFQPEGEKSSSAGVEANISNQEVKKSARTSTFKTTSSRHREQQIT-LLNQLASTHPHFV 678
Cdd:cd14899 553 DSFCESAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNeLLSTVRATTPRYV 632
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 6321812 679 RCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYPNRIAFQEFFQRYR 731
Cdd:cd14899 633 RCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
90-779 |
1.12e-101 |
|
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: 343.14 E-value: 1.12e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKhnrlsksRLDEnshekLPPHIFAIAEEAYENLLS 169
Cdd:cd01386 2 SVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGC-------RRED-----MPPHIYASAQSAYRAMLM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 170 EGKDQSILVTGESGAGKTENTKKILQYLASItSGSpsniapVSGSSIVEsfemKILQSNPILESFGNAQTVRNNNSSRFG 249
Cdd:cd01386 70 SRRDQSIVLLGRSGSGKTTNCRHILEYLVTA-AGS------VGGVLSVE----KLNAALTVLEAFGNVRTALNGNATRFS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 250 KFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSrnvkdykILSNSNQDIIPGI 329
Cdd:cd01386 139 QLFSLDFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQ-------LAESNSFGIVPLQ 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 330 NDVE------NFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVsdRAEQASFKNDVSAICSN-----LGVDEKDF 398
Cdd:cd01386 212 KPEDkqkaaaAFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGAT--KAASAGRKQFARPEWAQraaylLGCTLEEL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 399 QTAILRP------------RSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIA 466
Cdd:cd01386 290 SSAIFKHhlsggpqqsttsSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 467 GFEIFE------NNSFEQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIEsKGPPTGVLP-- 538
Cdd:cd01386 370 GFQNPAhsgsqrGATFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALID-QAPQQALVRsd 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 539 -----------LLDEEAVLPKSTDESFYSKL-----ISTWDQNSSKFKRSRLKNGFILKHYAG--DVEYTVEGWLSKNKD 600
Cdd:cd01386 449 lrdedrrgllwLLDEEALYPGSSDDTFLERLfshygDKEGGKGHSLLRRSEGPLQFVLGHLLGtnPVEYDVSGWLKAAKE 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 601 PLndnllsllsSSQNDIisKLFQpegekSSSAGVEAnisnqeVKKSARTSTFKTTSSrhreqqiTLLNQLASTHPHFVRC 680
Cdd:cd01386 529 NP---------SAQNAT--QLLQ-----ESQKETAA------VKRKSPCLQIKFQVD-------ALIDTLRRTGLHFVHC 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 681 IIPNNVKKVKT------------FNRRLILDQLRCNGVLEGIRLAREGYPNRIAFQEFFQRYRILYPENSTTTTFSSKLk 748
Cdd:cd01386 580 LLPQHNAGKDErstsspaagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLNSEV- 658
|
730 740 750
....*....|....*....|....*....|.
gi 6321812 749 ASTKQNCEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd01386 659 ADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
90-735 |
2.75e-100 |
|
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: 335.71 E-value: 2.75e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKHNRlsksrldensheklpPHIFAIAEEAYENLLS 169
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAMKAYLKNYSHVE---------------PHVYDVAEASVQDLLV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 170 EGkDQSILVTGESGAGKTENTKKILQYLASITSGSpsniapvsgssivESFEMKILQSNPILESFGNAQTVRNNNSSRFG 249
Cdd:cd14898 67 HG-NQTIVISGESGSGKTENAKLVIKYLVERTAST-------------TSIEKLITAANLILEAFGNAKTQLNDNSSRFG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 250 KFIKIEFNehGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGlddselKNLRLKSrnvkDYKILSNSNQDIIPGI 329
Cdd:cd14898 133 KRIKLKFD--GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCAS------KRLNIKN----DFIDTSSTAGNKESIV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 330 NDVENFKELLSALNIIGFSKdqIRWIFQVVAIILLIGNIEFVSDRAEQASFKNDVSAICSNLGVDEKDFQTAILRPRSKA 409
Cdd:cd14898 201 QLSEKYKMTCSAMKSLGIAN--FKSIEDCLLGILYLGSIQFVNDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 410 GKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDhGSATLNyIGLLDIAGFEIFENNSFEQLCINYTNEKLQ 489
Cdd:cd14898 279 KGETIEVFNTLKQARTIRNSMARLLYSNVFNYITASINNCLE-GSGERS-ISVLDIFGFEIFESNGLDQLCINWTNEKIQ 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 490 QFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIEskgpPTGVLPLLDEEAVLPKSTDESFYSKLISTwdqnSSKF 569
Cdd:cd14898 357 NDFIKKMFRAKQGMYKEEGIEWPDVEFFDNNQCIRDFEK----PCGLMDLISEESFNAWGNVKNLLVKIKKY----LNGF 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 570 KRSRLKNGFILKHYAGDVEYTVEGWLSKNKdplndnllsllsssqndiisklfqpegEKSSSAGVEANISNQEVKKSART 649
Cdd:cd14898 429 INTKARDKIKVSHYAGDVEYDLRDFLDKNR---------------------------EKGQLLIFKNLLINDEGSKEDLV 481
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 650 STFKTTSSRhreqqitLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYPNRIAFQEFFQR 729
Cdd:cd14898 482 KYFKDSMNK-------LLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEER 554
|
....*.
gi 6321812 730 YRILYP 735
Cdd:cd14898 555 YRILGI 560
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
95-778 |
2.13e-96 |
|
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: 326.43 E-value: 2.13e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 95 LEKRYDCDLIYTYSGLF-LVAINPYHNLNLYSEDHINLYhnkhnrlsKSRLDENSHEK---LPPHIFAIAEEAYENLLSE 170
Cdd:cd14879 10 LASRFRSDLPYTRLGSSaLVAVNPYKYLSSNSDASLGEY--------GSEYYDTTSGSkepLPPHAYDLAARAYLRMRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 171 GKDQSILVTGESGAGKTENTKKILQYLASITSGSPSniapvsGSSIVEsfemKILQSNPILESFGNAQTVRNNNSSRFGK 250
Cdd:cd14879 82 SEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKK------GTKLSS----QISAAEFVLDSFGNAKTLTNPNASRFGR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 251 FIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLksRNVKDYKILSNSNQ---DIIP 327
Cdd:cd14879 152 YTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGL--DDPSDYALLASYGChplPLGP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 328 GINDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDR---AEQASFKN-DVSAICSN-LGVDEKDFQTAi 402
Cdd:cd14879 230 GSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHeggEESAVVKNtDVLDIVAAfLGVSPEDLETS- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 403 LRPRSK-AGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNL-DHGSATLNYIGLLDIAGFEIF---ENNSFE 477
Cdd:cd14879 309 LTYKTKlVRKELCTVFLDPEGAAAQRDELARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRsstGGNSLD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 478 QLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQW---DYIDYGKDLQLTidliesKGPPTGVLPLLDEEA-VLPKSTDES 553
Cdd:cd14879 389 QFCVNFANERLHNYVLRSFFERKAEELEAEGVSVpatSYFDNSDCVRLL------RGKPGGLLGILDDQTrRMPKKTDEQ 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 554 FYSKLISTWDQNSS-----KFKRSRLKNGFILKHYAGDVEYTVEGWLSKNKDPLNdnllsllsssqNDIISkLFQPEGEK 628
Cdd:cd14879 463 MLEALRKRFGNHSSfiavgNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLS-----------PDFVN-LLRGATQL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 629 SSSagveanISnqevkksartstfkttssrhreqqiTLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLE 708
Cdd:cd14879 531 NAA------LS-------------------------ELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPE 579
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 709 GIRLAREGYPNRIAFQEFFQRYrilypeNSTTTTFSSKLKAstkqncEFLLTSLQLDTKVYKIGNTKLFF 778
Cdd:cd14879 580 LAARLRVEYVVSLEHAEFCERY------KSTLRGSAAERIR------QCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
89-779 |
1.35e-94 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 323.91 E-value: 1.35e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRY--------DCDLIYTYSGLFLVAINPYHNLNLYSEDHInlyhnkhnrlskSRLDENSHEKLPPHIFAIA 160
Cdd:cd14887 1 PNLLENLYQRYnkayinkeNRNCIYTYTGTLLIAVNPYRFFNLYDRQWI------------SRFDTEANSRLVPHPFGLA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 161 EEAYENLLSEGKDQSILVTGESGAGKTENTKKILQYLASIT---SGSPSniapvsgssivESFEMKILQSNPILESFGNA 237
Cdd:cd14887 69 EFAYCRLVRDRRSQSILISGESGAGKTETSKHVLTYLAAVSdrrHGADS-----------QGLEARLLQSGPVLEAFGNA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 238 QTVRNNNSSRFGKFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLddselknlrlksrnvkdyki 317
Cdd:cd14887 138 HTVLNANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAA-------------------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 318 LSNSNQDIIPGINDVE--NFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAEQASFKNDVSAI-------- 387
Cdd:cd14887 198 VAAATQKSSAGEGDPEstDLRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSVsvgceeta 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 388 ------------CSNLGVDE------KDFQTAILRPRSKAGKEW---------VSQSKNS---QQAKFILNALSRNLYER 437
Cdd:cd14887 278 adrshssevkclSSGLKVTEasrkhlKTVARLLGLPPGVEGEEMlrlalvsrsVRETRSFfdlDGAAAARDAACKNLYSR 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 438 LFGYIVDMINKNLDHG--------------SATLNYIGLLDIAGFEIFEN---NSFEQLCINYTNEKLQQFFNNHMFVLE 500
Cdd:cd14887 358 AFDAVVARINAGLQRSakpsesdsdedtpsTTGTQTIGILDLFGFEDLRNhskNRLEQLCINYANERLHCFLLEQLILNE 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 501 QSEYLKENIQWDYIDYGKDLQLTIDLIESKGP-------PTGVLPLLDEEAVLPK-----STDESFYSKLISTWD----- 563
Cdd:cd14887 438 HMLYTQEGVFQNQDCSAFPFSFPLASTLTSSPsstspfsPTPSFRSSSAFATSPSlpsslSSLSSSLSSSPPVWEgrdns 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 564 -----------QNSSKFKR-----SRLKNGFILKHYAGDVEYTVEGWLSKNKDPLNDNllsllsssqndiISKLFQpege 627
Cdd:cd14887 518 dlfyeklnkniINSAKYKNitpalSRENLEFTVSHFACDVTYDARDFCRANREATSDE------------LERLFL---- 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 628 kSSSAGVEANISNQEVKKSARTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVL 707
Cdd:cd14887 582 -ACSTYTRLVGSKKNSGVRAISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMS 660
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321812 708 EGIRLAREGYPNRIAFQEFFQRYRILYPEnsttttfSSKLKASTKQNCEFLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14887 661 DLLRVMADGFPCRLPYVELWRRYETKLPM-------ALREALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
91-779 |
5.56e-81 |
|
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: 281.13 E-value: 5.56e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 91 VLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLysedHINLYHNKhnrlsksrldenSHEKLPPHIFAIAEEAYENLLSE 170
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDV----DINEYKNK------------NTNELPPHVYSYAKDAMTDFINT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 171 GKDQSILVTGESGAGKTENTKKILQYLasitsgspsniapVSGSSIVESFEMKILQSNPILESFGNAQTVRNNNSSRFGK 250
Cdd:cd14937 67 KTNQSIIISGESGSGKTEASKLVIKYY-------------LSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 251 FIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDsELKNlRLKSRNVKDYKILSNSNQdIIPGIN 330
Cdd:cd14937 134 YIKIELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQ-ELKN-KYKIRSENEYKYIVNKNV-VIPEID 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 331 DVENFKELLSALNIIGFSkDQIRWIFQVVAIILLIGNIEFvsDRAEQASFKN----------DVSAICSNLGVDEKDFQT 400
Cdd:cd14937 211 DAKDFGNLMISFDKMNMH-DMKDDLFLTLSGLLLLGNVEY--QEIEKGGKTNcseldknnleLVNEISNLLGINYENLKD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 401 AILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATLNYIGLLDIAGFEIFENNSFEQLC 480
Cdd:cd14937 288 CLVFTEKTIANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 481 INYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDlQLTIDLIESKgppTGVLPLLDEEAVLPKSTDESFYSKLIS 560
Cdd:cd14937 368 INIANEEIHSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGK---TSIISILEDSCLGPVKNDESIVSVYTN 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 561 TWDQNS--SKFKRSRLKNgFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQpEGEKSSSAGVEANI 638
Cdd:cd14937 444 KFSKHEkyASTKKDINKN-FVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYE-DVEVSESLGRKNLI 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 639 snqevkksartsTFKttssrHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAReGYP 718
Cdd:cd14937 522 ------------TFK-----YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNISF-FFQ 583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321812 719 NRIAFQEFFQRYRILYPENSTTTTFSSKLKAStkqncefLLTSLQLDTKVYKIGNTKLFFK 779
Cdd:cd14937 584 YKYTFDVFLSYFEYLDYSTSKDSSLTDKEKVS-------MILQNTVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
89-725 |
3.99e-80 |
|
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: 280.25 E-value: 3.99e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNL-NLYSEDHINLYHNKhnrLSKSRLDENSHekLPPHIFAIAEEAYENL 167
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLkELYDQDVMNVYLHK---KSNSAASAAPF--PKAHIYDIANMAYKNM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 168 LSEGKDQSILVTGESGAGKTENTKKILQYLASItsgspsniapvSGSSIVESFEMKILQSNPILESFGNAQTVRNNNSSR 247
Cdd:cd14884 76 RGKLKRQTIVVSGHSGSGKTENCKFLFKYFHYI-----------QTDSQMTERIDKLIYINNILESMSNATTIKNNNSSR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 248 FGKFIKIEFNE---------HGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLkSRNVKDYKIL 318
Cdd:cd14884 145 CGRINLLIFEEventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNL-VRNCGVYGLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 319 SN---------SNQDIIPGIN----------DVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFvsdraeqas 379
Cdd:cd14884 224 NPdeshqkrsvKGTLRLGSDSldpseeekakDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAY--------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 380 fkndvSAICSNLGVDEKDFQTAILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNL--------- 450
Cdd:cd14884 295 -----KAAAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdes 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 451 ---DHGSATLNYIGLLDIAGFEIFENNSFEQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQW--DYIDYGKDLQLTID 525
Cdd:cd14884 370 dneDIYSINEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICcsDVAPSYSDTLIFIA 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 526 LIESKgpptgvlplLDEEAVLP----KSTDESFYSKL-----------------ISTWDQNSSKFKRSRLKNGFILKHYA 584
Cdd:cd14884 450 KIFRR---------LDDITKLKnqgqKKTDDHFFRYLlnnerqqqlegkvsygfVLNHDADGTAKKQNIKKNIFFIRHYA 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 585 GDVEYTVEGWLSKNKDPLndnllsllsssQNDIisklfqpEGEKSSSAGVEANISNQEVKKsartSTFKTTSSRHREQQI 664
Cdd:cd14884 521 GLVTYRINNWIDKNSDKI-----------ETSI-------ETLISCSSNRFLREANNGGNK----GNFLSVSKKYIKELD 578
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321812 665 TLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYPNRIAFQE 725
Cdd:cd14884 579 NLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
92-731 |
3.20e-79 |
|
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: 279.16 E-value: 3.20e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 92 LYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKHNRLSKSRLDenSHEKLPPHIFAIAEEAYENLLSEG 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQTPLYEKD--TVNDAPPHVFALAQNALRCMQDAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 172 KDQSILVTGESGAGKTENTKKILQYLASITSGSPSNIAPVSGSSIVESFEMKILQSNPILESFGNAQTVRNNNSSRFGKF 251
Cdd:cd14893 82 EDQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 252 IKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLD-DSELKNLRLKSRNVKDYKILSNSNQDIIPGIN 330
Cdd:cd14893 162 ISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhDPTLRDSLEMNKCVNEFVMLKQADPLATNFAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 331 DVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSD----RAEQASFKNDVSAICSNLGVDEK---------D 397
Cdd:cd14893 242 DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDpeggKSVGGANSTTVSDAQSCALKDPAqillaakllE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 398 FQTAIL----RPR---SKAGKEWVSQSK--NSQQAKFILNALSRNLYERLFGYIVDMINKNL-------DHGSATLNYIG 461
Cdd:cd14893 322 VEPVVLdnyfRTRqffSKDGNKTVSSLKvvTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdryEKSNIVINSQG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 462 --LLDIAGFEIFEN--NSFEQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWD-------YIDYGKDLQLTIDLIESk 530
Cdd:cd14893 402 vhVLDMVGFENLTPsqNSFDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVEnrltvnsNVDITSEQEKCLQLFED- 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 531 gPPTGVLPLLDEEAVLPKSTDESFYSKLISTWDQ--------NSSKFKRSRLKNG------FILKHYAGDVEYTVEGWLS 596
Cdd:cd14893 481 -KPFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAvgglsrpnMGADTTNEYLAPSkdwrllFIVQHHCGKVTYNGKGLSS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 597 KNKDPLNDNLLSLLSSSQNDIISKLfqpeGEKSSSAGVEANISNQEVKKSARTSTFKTTSSRHRE--------------Q 662
Cdd:cd14893 560 KNMLSISSTCAAIMQSSKNAVLHAV----GAAQMAAASSEKAAKQTEERGSTSSKFRKSASSAREsknitdsaatdvynQ 635
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321812 663 QITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYPNRIAFQEFFQRYR 731
Cdd:cd14893 636 ADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
95-779 |
1.21e-74 |
|
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: 263.88 E-value: 1.21e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 95 LEKRYDCDLIYTYSGLFLVAINPYHNLN-LYSEDHINLYhnkhnrlsksrldeNSHEKLPPHIFAIAEEAYENLLSEGKD 173
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--------------NQRRGLPPHLFALAAKAISDMQDFRRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 174 QSILVTGESGAGKTENTKKILQYLASitsgspsniAPVSGSSIVESFemkILQSNPILESFGNAQTVRNNNSSRFGKFIK 253
Cdd:cd14905 73 QLIFIGGESGSGKSENTKIIIQYLLT---------TDLSRSKYLRDY---ILESGIILESFGHASTDSNHNSSRWGKYFE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 254 IEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKsrNVKDYKILSNSNQDIIPGINDVE 333
Cdd:cd14905 141 MFYSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLG--DINSYHYLNQGGSISVESIDDNR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 334 NFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAE-QASFKNDVSAICSNLGVDEKDFQTAILRPRSKAGKE 412
Cdd:cd14905 219 VFDRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNGKtEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 413 WVSQSknsqqakfilNALSRNLYERLFGYIVDMINKNLDHGSATlNYIGLLDIAGFEIFENNSFEQLCINYTNEKLQQFF 492
Cdd:cd14905 299 AVENR----------DSLARSLYSALFHWIIDFLNSKLKPTQYS-HTLGILDLFGQESSQLNGYEQFSINFLEERLQQIY 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 493 NNHMFVLEQSEYLKENIQWDYIDYGKDLQLTIDLIESkgpptgVLPLLDEEAVLPKSTDESFYSKLISTWDQNSSKFKRS 572
Cdd:cd14905 368 LQTVLKQEQREYQTERIPWMTPISFKDNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFGKKP 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 573 rlkNGFILKHYAGDVEYTVEGWLSKNKDPLndnLLSLLSSSQNDIISKLFQPEGEKSSSAGVEANISNQEVKKSART--- 649
Cdd:cd14905 442 ---NKFGIEHYFGQFYYDVRGFIIKNRDEI---LQRTNVLHKNSITKYLFSRDGVFNINATVAELNQMFDAKNTAKKspl 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 650 -----------------------------------------STFKTTSSRHREqqitlLNQlASTHPHFVRCIIPNNVKK 688
Cdd:cd14905 516 sivkvllscgsnnpnnvnnpnnnsgggggggnsgggsgsggSTYTTYSSTNKA-----INN-SNCDFHFIRCIKPNSKKT 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 689 VKTFNRRLILDQLRCNGVLEGIRLAREGYPNRIAFQEFFQRYRILYPENSTTTTFSSKLKASTKQNCEFLLTSLQldtkv 768
Cdd:cd14905 590 HLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQRNFQNLFEKLKENDINIDSILPPPIQ----- 664
|
730
....*....|.
gi 6321812 769 ykIGNTKLFFK 779
Cdd:cd14905 665 --VGNTKIFLR 673
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
90-738 |
8.99e-74 |
|
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: 260.05 E-value: 8.99e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHN----LNLYSEDHINLYhnkhnrlsksrldensheklpPHIFAIAEEAYE 165
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDvgnpLTLTSTRSSPLA---------------------PQLLKVVQEAVR 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 166 NLLSEGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNIApvsgssivesfeMKILQSN-PILESFGNAQTVRNNN 244
Cdd:cd14881 61 QQSETGYPQAIILSGTSGSGKTYASMLLLRQLFDVAGGGPETDA------------FKHLAAAfTVLRSLGSAKTATNSE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 245 SSRFGKFIKIEFNEhGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSRNVKDYKILSNSN-- 322
Cdd:cd14881 129 SSRIGHFIEVQVTD-GALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSPANLRYLSHGDtr 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 323 QDIIPGINDVENFKELLSALNiIGFSkDQIRwifqVVAIILLIGNIEFVSDRAEQASFK--NDVSAICSNLGVDEKD-FQ 399
Cdd:cd14881 208 QNEAEDAARFQAWKACLGILG-IPFL-DVVR----VLAAVLLLGNVQFIDGGGLEVDVKgeTELKSVAALLGVSGAAlFR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 400 TAILRPRSkAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGS-----ATLNYIGLLDIAGFEIFENN 474
Cdd:cd14881 282 GLTTRTHN-ARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANSLKRLGStlgthATDGFIGILDMFGFEDPKPS 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 475 SFEQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDY-IDYgKDLQLTIDLIESKgpPTGVLPLLDEEAVlPKSTDES 553
Cdd:cd14881 361 QLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLISSL--RTGLLSMLDVECS-PRGTAES 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 554 FYSKlISTWDQNSSKFKRSRLKNG--FILKHYAGDVEYTVEGWLSKNKDPLNDnllsllsssqnDIISKLFQpegeKSSS 631
Cdd:cd14881 437 YVAK-IKVQHRQNPRLFEAKPQDDrmFGIRHFAGRVVYDASDFLDTNRDVVPD-----------DLVAVFYK----QNCN 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 632 AGveanisnqevkksartstFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIR 711
Cdd:cd14881 501 FG------------------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVN 562
|
650 660
....*....|....*....|....*..
gi 6321812 712 LAREGYPNRIAFQEFFQRYRILYPENS 738
Cdd:cd14881 563 LMAGGYPHRMRFKAFNARYRLLAPFRL 589
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
91-735 |
5.47e-70 |
|
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: 248.63 E-value: 5.47e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 91 VLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHnkhnrlsksrldensheklpphIFAIAEEAYENLLS- 169
Cdd:cd14874 3 IAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKCH----------------------ISGVAENALDRIKSm 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 170 EGKDQSILVTGESGAGKTENTKKILQYLasiTSGSPSNIAPVSGSSIvesfemkilqsNPILESFGNAQTVRNNNSSRFG 249
Cdd:cd14874 61 SSNAESIVFGGESGSGKSYNAFQVFKYL---TSQPKSKVTTKHSSAI-----------ESVFKSFGCAKTLKNDEATRFG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 250 KFIKIEFNEHgMINGAHIEWYL-LEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKSRNVKDYKILSNSNQDIIpg 328
Cdd:cd14874 127 CSIDLLYKRN-VLTGLNLKYTVpLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQ-- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 329 iNDVENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRaeQASFKNDVSAICSNLGVD------EKDFQ--T 400
Cdd:cd14874 204 -SDVNHFKHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKR--NPNVEQDVVEIGNMSEVKwvafllEVDFDqlV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 401 AILRPRSKAGkewvsQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATlNYIGLLDIAGFEIFENNSFEQLC 480
Cdd:cd14874 281 NFLLPKSEDG-----TTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHT-GVISILDHYGFEKYNNNGVEEFL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 481 INYTNEKLQQFFNNHMFVLEQSEYLKENIQWDY-----IDYGKdlqlTIDLIESKgpPTGVLPLLDEEAVLPKSTDESFY 555
Cdd:cd14874 355 INSVNERIENLFVKHSFHDQLVDYAKDGISVDYkvpnsIENGK----TVELLFKK--PYGLLPLLTDECKFPKGSHESYL 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 556 SKL-ISTWDQNSSKFKRSRLKNGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFQPEGEKSSSAGV 634
Cdd:cd14874 429 EHCnLNHTDRSSYGKARNKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDMIV 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 635 EaniSNQEVKKSARtstfkttssrhreqqiTLLNQLASTHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAR 714
Cdd:cd14874 509 S---QAQFILRGAQ----------------EIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRI 569
|
650 660
....*....|....*....|.
gi 6321812 715 EGYPNRIAFQEFFQRYRILYP 735
Cdd:cd14874 570 KGYPVKISKTTFARQYRCLLP 590
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
90-779 |
3.54e-69 |
|
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: 246.58 E-value: 3.54e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 90 SVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHinlyHNKHNrlSKSRLDENsheklpPHIFAIAEEAYENLLS 169
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEF----HAKYR--CKSRSDNA------PHIFSVADSAYQDMLH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 170 EGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNiapvsgssivesfEMKILQSNPILESFGNAQTVRNNNSSRFG 249
Cdd:cd14882 70 HEEPQHIILSGESYSGKTTNARLLIKHLCYLGDGNRGA-------------TGRVESSIKAILALVNAGTPLNADSTRCI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 250 KFIKIEFNEHGMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSE-LKNLRLKS-RNVKDYKILSNSNQDIIP 327
Cdd:cd14882 137 LQYQLTFGSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNrLKEYNLKAgRNYRYLRIPPEVPPSKLK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 328 GIND-----VENFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAEQASFKNDV-SAICSNLGVDEKDFQTA 401
Cdd:cd14882 217 YRRDdpegnVERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQNGGYAELENTEIaSRVAELLRLDEKKFMWA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 402 ILRPRSKAGKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMINKNLDHGSATL---NYIGLLDIAGFEIFENNSFEQ 478
Cdd:cd14882 297 LTNYCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPRAVFgdkYSISIHDMFGFECFHRNRLEQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 479 LCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYgKDLQLTIDLIESKgpPTGVLPLLDEEAvlpKSTDESFYskL 558
Cdd:cd14882 377 LMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDQLMTK--PDGLFYIIDDAS---RSCQDQNY--I 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 559 ISTWDQNSSKFKRSRLKNGFILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQNDIISKLFqpegeksssagveani 638
Cdd:cd14882 449 MDRIKEKHSQFVKKHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMF---------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 639 SNQEVKKsartstFKTTSSRHREQQITLLNQLA----STHPHFVRCIIPNNVKKVKTFNRRLILDQLRCNGVLEGIRLAR 714
Cdd:cd14882 513 TNSQVRN------MRTLAATFRATSLELLKMLSiganSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQ 586
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321812 715 EGYPNRIAFQEFFQRYRILYPENSTTTTFssklkasTKQNCEFLLTSLQLDTkvYKIGNTKLFFK 779
Cdd:cd14882 587 KGFSYRIPFQEFLRRYQFLAFDFDETVEM-------TKDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
89-777 |
1.42e-49 |
|
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: 189.66 E-value: 1.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 89 PSVLYNLEKRYDCDLIYTYSGLFLVAINPYHNLNLYSEDHINLYHNKHnrlsksrldenSHEKLPPHIFAIAEEAYENLL 168
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCID-----------CIEDLSLNEYHVVHNALKNLN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 169 SEGKDQSILVTGESGAGKTENTKKILQYLASITSGSPSNIAPVSGSSIVE-----------SFEMKILQSNPILESFGNA 237
Cdd:cd14938 70 ELKRNQSIIISGESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEEDNihneentdyqfNMSEMLKHVNVVMEAFGNA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 238 QTVRNNNSSRFGKFIKIEFNEHgMINGAHIEWYLLEKSRIVHQNSKERNYHIFYQLLSGLDDSELKNLRLKsrNVKDYKI 317
Cdd:cd14938 150 KTVKNNNSSRFSKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLK--NIENYSM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 318 LsnSNQDIIPGINDVE-NFKELLSALNIIGFSKDQIRWIFQVVAIILLIGNIEFVSDRAEQASFK---------NDVSAI 387
Cdd:cd14938 227 L--NNEKGFEKFSDYSgKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKAFRKKSLLMgknqcgqniNYETIL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 388 C-----SNLGVDEK-------------DFQTAILRPRSKA--GKEWVSQSKNSQQAKFILNALSRNLYERLFGYIVDMIN 447
Cdd:cd14938 305 SelensEDIGLDENvknlllackllsfDIETFVKYFTTNYifNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKIN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 448 K---NLDHGSATLNYIGLLDIAGFEIFENNSFEQLCINYTNEKLQQFFNNHMFVLEQSEYLKENIQWDYIDYGKDLQLTI 524
Cdd:cd14938 385 EkctQLQNININTNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLY 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 525 DLIESKGppTGVLPLLDEEAVLPKSTDES-FYSKLISTWDQNS---SKFKRSRLKNGFILKHYAGDVEYTVEGWLSKNKD 600
Cdd:cd14938 465 NLLVGPT--EGSLFSLLENVSTKTIFDKSnLHSSIIRKFSRNSkyiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNID 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 601 PLNDNLLSLLSSSQNDIISKLFQPEGEKSSSAGVEAN-----ISNQEVKKSARTSTFKTTSSRHREQQITLLNQLASTHP 675
Cdd:cd14938 543 ILTNRFIDMVKQSENEYMRQFCMFYNYDNSGNIVEEKrrysiQSALKLFKRRYDTKNQMAVSLLRNNLTELEKLQETTFC 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 676 HFVRCIIPN-NVKKVKTFNRRLILDQLRCNGVLEGIRLAREGYPNRIAFQEFFQRYRilypensttttfssKLKASTKQN 754
Cdd:cd14938 623 HFIVCMKPNeSKRELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFD--------------IKNEDLKEK 688
|
730 740
....*....|....*....|...
gi 6321812 755 CEFLLTSLQLDTKVYKIGNTKLF 777
Cdd:cd14938 689 VEALIKSYQISNYEWMIGNNMIF 711
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
111-254 |
5.20e-37 |
|
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: 137.86 E-value: 5.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 111 FLVAINPYHNLNLYSEDHINLYHNKHNRLSKsrldensheklPPHIFAIAEEAYENLLSEGKDQSILVTGESGAGKTENT 190
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIVFYRGFRRSES-----------QPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETM 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321812 191 KKILQYLASITSGSPSNIAPVSGSSIVESF---EMKILQSNPILESFGNAQTVRNNNSSRFGKFIKI 254
Cdd:cd01363 70 KGVIPYLASVAFNGINKGETEGWVYLTEITvtlEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
95-714 |
2.65e-28 |
|
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: 124.47 E-value: 2.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 95 LEKRYDCDLIYTYSGLFLVAI-NPYHNL------NLYSEDHINLYHNKhnrlsksrldENSHEKLPPHIFAIAEEAYENL 167
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMAVmNPYRLLqtarftSIYDEQVVLTYADT----------ANAETVLAPHPFAIAKQSLVRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 168 -------------------LSEGKDQSILVTGESGAGKTENTKKILQYLASIT----SGSPSNIAPVSGSSI-------- 216
Cdd:cd14894 77 ffdnehtmplpstissnrsMTEGRGQSLFLCGESGSGKTELAKDLLKYLVLVAqpalSKGSEETCKVSGSTRqpkiklft 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 217 ------------------------VESFEMK------------------------------------------------- 223
Cdd:cd14894 157 sstkstiqmrteeartialleakgVEKYEIVlldlhperwdemtsvsrskrlpqvhvdglffgfyeklehledeeqlrmy 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 224 ------------ILQSNPILESFGNAQTVRNNNSSRFGKF--IKIEFNEHG---MINGAHIEWYLLEKSRIVHQNSKER- 285
Cdd:cd14894 237 fknphaakklsiVLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERGRESg 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 286 -----NYHIFYQLLSGLDDSEL-----KNLRLKSRNVKDYKILSNSNQDIIPGIN-------DVENFKELLSALNIIGFS 348
Cdd:cd14894 317 dqnelNFHILYAMVAGVNAFPFmrllaKELHLDGIDCSALTYLGRSDHKLAGFVSkedtwkkDVERWQQVIDGLDELNVS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 349 KDQIRWIFQVVAIILLIGNIEFVSDRAEQASFKNDVSAICS--------NLGVDEKDFQTAILRPRS-KAGKEWVSQSKN 419
Cdd:cd14894 397 PDEQKTIFKVLSAVLWLGNIELDYREVSGKLVMSSTGALNApqkvvellELGSVEKLERMLMTKSVSlQSTSETFEVTLE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 420 SQQAKFILNALSRNLYERLFGYIVDMINK--------------NLDHGSATLNYIGLL---DIAGFEIFENNSFEQLCIN 482
Cdd:cd14894 477 KGQVNHVRDTLARLLYQLAFNYVVFVMNEatkmsalstdgnkhQMDSNASAPEAVSLLkivDVFGFEDLTHNSLDQLCIN 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 483 YTNEKLqqffnnhmfvleqseYLKENiQWDYIDYGKDLQLTI-----DLIESKGPPTGVLPLLDEEAVLPKSTD-----E 552
Cdd:cd14894 557 YLSEKL---------------YAREE-QVIAVAYSSRPHLTArdsekDVLFIYEHPLGVFASLEELTILHQSENmnaqqE 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 553 SFYSKLI--STWDQNSSKFKRSR--LKNG------------FILKHYAGDVEYTVEGWLSKNKDPLNDNLLSLLSSSQND 616
Cdd:cd14894 621 EKRNKLFvrNIYDRNSSRLPEPPrvLSNAkrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSS 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 617 IISKLFQpegeKSSSAGVEANiSNQEVKKSA--RTSTFKTTSSRHREQQITLLNQLASTHPHFVRCIIPNNVKKVKTFNR 694
Cdd:cd14894 701 HFCRMLN----ESSQLGWSPN-TNRSMLGSAesRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNN 775
|
810 820
....*....|....*....|
gi 6321812 695 RLILDQLRCNGVLEGIRLAR 714
Cdd:cd14894 776 DLVEQQCRSQRLIRQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
930-1785 |
1.21e-24 |
|
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: 112.84 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 930 QKQFDDLVSEKDE-----------ISR---EKLEVAQNLEEAHQKIQGLQETIREREATLEKLH---SKNNELIKQISDL 992
Cdd:TIGR02168 143 QGKISEIIEAKPEerraifeeaagISKykeRRKETERKLERTRENLDRLEDILNELERQLKSLErqaEKAERYKELKAEL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 993 ncdiskEQSSQSLIKESKLKLENEIKRLKDVINSKEEEIKSFNDKLSSSEEDLDI---KLVTLEKNCNIAMSRLQSLVTE 1069
Cdd:TIGR02168 223 ------RELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEElrlEVSELEEEIEELQKELYALANE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1070 NSDLRSKNENFKKEKAALNNQLKNKESELLKMKEKIDNHKKELATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQK 1149
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1150 IKEEYSNFQR---ETKEQEQKKRNSLVEslNDSKIKELEARLSQEISLNQYLNKRISGNSVETNISSTRRSTSYSDDPL- 1225
Cdd:TIGR02168 377 LEEQLETLRSkvaQLELQIASLNNEIER--LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQe 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1226 DKEDIIKKYYDLQLAFTEITRNLENEIEEKKNLISRLRFTETRLASSSFEDQKIKAQMKKLKKLIQDMDP---------- 1295
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVlselisvdeg 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1296 -----SIPLDSILNEPLDNcpdkesDINKLMLEVDYLK-----RQLDIETRAHYDAENAISALHSKFRKIQGESSLSSSD 1365
Cdd:TIGR02168 535 yeaaiEAALGGRLQAVVVE------NLNAAKKAIAFLKqnelgRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1366 IYKLKFEAS----------EERVKSLEDKLKTMPLRDRTNLPVGDIIKNRDSISKYEEEIRyyklenyklQEILNESNgK 1435
Cdd:TIGR02168 609 KFDPKLRKAlsyllggvlvVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTN---------SSILERRR-E 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1436 LSQLTLDLRQSKSKEALLSEQLDRLQKDLESTERQKELLSSTIKQQKQQFENcmddlqgnelrlrehihalkqAEEDVKN 1515
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA---------------------LRKDLAR 737
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1516 MASIIEKLKTQNKQKEKLIWEREMERNDSDMQLQETLLELKRVQDVKKILSDDLAHLKERLSAVEDRsqytdeINRLKEE 1595
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA------LDELRAE 811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1596 LncslkaeTNLKKEFATLKYKLETSTNDSEAKisdllkqldhyTKVVEMLNNEKDAISLAEKELYQKYEALNTECESLKG 1675
Cdd:TIGR02168 812 L-------TLLNEEAANLRERLESLERRIAAT-----------ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1676 KIVSLTKIKQELESDLNQKTDALQISNAALSSSTQKNKEITEKIKYLEETL-QLQMEQNSRNGELVKTLQASCNGYKDKF 1754
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLaQLELRLEGLEVRIDNLQERLSEEYSLTL 953
|
890 900 910
....*....|....*....|....*....|.
gi 6321812 1755 DDEKQKNIDLYEENQTLQKLNTDLQLQLKNL 1785
Cdd:TIGR02168 954 EEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
867-1597 |
3.83e-23 |
|
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: 107.83 E-value: 3.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 867 NEQINKLKndlQEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQFDDLVSEKDEISRE 946
Cdd:TIGR02168 199 ERQLKSLE---RQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 947 KLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQSLIKESKLKLENEIKRLKDVINS 1026
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1027 KEEEIKSFNDKLSSSE----------EDLDIKLVTLEKNCNIAMSRLQSLVTENSDLRSKNENFKKEKAALNNQLknKES 1096
Cdd:TIGR02168 356 LEAELEELEAELEELEsrleeleeqlETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL--EEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1097 ELLKMKEKIDNHKKELATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNY----------QKIKEEYSNFQRETKEQEQ 1166
Cdd:TIGR02168 434 ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELaqlqarldslERLQENLEGFSEGVKALLK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1167 KKR--------------------------------NSLVESLNDSK-----IKELEARLSQEISLNQYLNKRISGNSVET 1209
Cdd:TIGR02168 514 NQSglsgilgvlselisvdegyeaaieaalggrlqAVVVENLNAAKkaiafLKQNELGRVTFLPLDSIKGTEIQGNDREI 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1210 nISSTRRSTSYSDDPLDKEDIIKKYYDLQLAFTEITRNLENEIEEKKNLISRLRF--TETRLASSSF--------EDQKI 1279
Cdd:TIGR02168 594 -LKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIvtLDGDLVRPGGvitggsakTNSSI 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1280 KAQMKKLKKLIQDMDPSIPLDSILNEPLDncpDKESDINKLMLEVDYLKRQLDIETRAHYDAENAISALHSKFRKIQGES 1359
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALA---ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1360 SLSSSDIYklkfEASEERVKSLEDKLKTMPLRDRTNlpvGDIIKNRDSISKYEEEIRYYKLENYKLQEILNESNGKLSQL 1439
Cdd:TIGR02168 750 AQLSKELT----ELEAEIEELEERLEEAEEELAEAE---AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1440 TLDLRQSKSKEALLSEQLDRLQKDLESTERQKELLSSTIKQQKQQFENCMDDLQGNELRLREHIHALKQAEEDVKNMASI 1519
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1520 IEKLKTQNKQKEKLIWEREMERNDSDMQLQETLLELKRVQD-VKKILSDDLAHLKERLSAVEDRSQYT-DEINRLKEELN 1597
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQErLSEEYSLTLEEAEALENKIEDDEEEArRRLKRLENKIK 982
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
866-1686 |
9.25e-21 |
|
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: 100.14 E-value: 9.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 866 FNEQINKLKNDLQEMESKkkflEEKNQKTVNELENTQDLLNQEKENLRKNESLLNRV-KTSSETLQKQFDDLVSEKDEIS 944
Cdd:TIGR02169 168 FDRKKEKALEELEEVEEN----IERLDLIIDEKRQQLERLRREREKAERYQALLKEKrEYEGYELLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 945 REKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSK--------NNELIKQISDLNCDISKEQSSQSLIKESKLKLENE 1016
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKikdlgeeeQLRVKEKIGELEAEIASLERSIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1017 IKRLKDVINSKEEEIKSFN-----------------DKLSSSEEDLDIKLVTLEKNCNIAMSRLQSLVTENSDLRSKNEN 1079
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEreieeerkrrdklteeyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1080 FKKEKAALNNQLKNKESELLKMKEKIDNHKKELATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQKIKEEYSNFQR 1159
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1160 ETKEQEQK---------------KRNSLVESLNDSKIKELEARLSQEISLN----------------------------- 1195
Cdd:TIGR02169 484 ELSKLQRElaeaeaqaraseervRGGRAVEEVLKASIQGVHGTVAQLGSVGeryataievaagnrlnnvvveddavakea 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1196 -QYLNKRISGNSveTNISSTRRSTSYSD-DPLDKEDIIKKYYDL-------QLAFTEITRN------------------- 1247
Cdd:TIGR02169 564 iELLKRRKAGRA--TFLPLNKMRDERRDlSILSEDGVIGFAVDLvefdpkyEPAFKYVFGDtlvvedieaarrlmgkyrm 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1248 --LENEIEEKKNLIS----RLRFTETRLASSSFEDQKIKAQMKKLKKLiqdmdpsipLDSILnepldncpdkeSDINKLM 1321
Cdd:TIGR02169 642 vtLEGELFEKSGAMTggsrAPRGGILFSRSEPAELQRLRERLEGLKRE---------LSSLQ-----------SELRRIE 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1322 LEVDYLKRQLDIETRAHYDAENAISALHSKFRKIQGEsslsssdiyklkFEASEERVKSLEDKLKtmplrdrtnlpvgdi 1401
Cdd:TIGR02169 702 NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER------------LEELEEDLSSLEQEIE--------------- 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1402 iKNRDSISKYEEEIRYYKLENYKLQEILNESNGKLS-----QLTLDLRQSKSKEALLSEQLDRLQKDLESTERQKELLSS 1476
Cdd:TIGR02169 755 -NVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1477 TIKQQKQQfencMDDLQGNELRLREHIHALKQAEEDvknMASIIEKLKTQNKQKEKLIWEREMERNDSDMQLQETLLELK 1556
Cdd:TIGR02169 834 EIQELQEQ----RIDLKEQIKSIEKEIENLNGKKEE---LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1557 RVQDVKKILSDDLAHLKERLSAVEDR-SQYTDEINRLKEELNCSLKAEtnlkkefatlkyKLETSTNDSEAKISDL---- 1631
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEElSEIEDPKGEDEEIPEEELSLE------------DVQAELQRVEEEIRALepvn 974
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*
gi 6321812 1632 LKQLDHYTKVVEMLNnekdaislaekELYQKYEALNTECESLKGKIVSLTKIKQE 1686
Cdd:TIGR02169 975 MLAIQEYEEVLKRLD-----------ELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
935-1787 |
1.00e-16 |
|
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: 87.05 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 935 DLVSEKDEISREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNN------------------ELIKQISDLNCDI 996
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaeryqallkekreyegyELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 997 SKEQSSQSLIKESKLKLENEIKRLKDVINSKEEEIKSFNDKLS--SSEEDLDIKlvtlekncniamSRLQSLVTENSDLR 1074
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlGEEEQLRVK------------EKIGELEAEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1075 SKNENFKKEKAALNNQLKNKESELLKMKEKIDNHKKELATFSKQRD--------------DAVSEHGKITAELKETRIQL 1140
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDklteeyaelkeeleDLRAELEEVDKEFAETRDEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1141 TEYKSNYQKIKEEYSNFQRE-TKEQEQKKRNSLVESLNDSKIKELEARLSQEISLNQYLNKRISgnSVETNISSTRRsts 1219
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRElDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK--KQEWKLEQLAA--- 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1220 ysddplDKEDIIKKYYDLQlaftEITRNLENEIEEKKNLISRLrftETRLASSSFEDQKIKAQMKKLKKLIQDMDPSI-- 1297
Cdd:TIGR02169 463 ------DLSKYEQELYDLK----EEYDRVEKELSKLQRELAEA---EAQARASEERVRGGRAVEEVLKASIQGVHGTVaq 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1298 ----------PLDSILNEPLDNCPDKESDINKLMLEvdYLKRqldietrahydaENAISALHSKFRKIQGESSLSSSdIY 1367
Cdd:TIGR02169 530 lgsvgeryatAIEVAAGNRLNNVVVEDDAVAKEAIE--LLKR------------RKAGRATFLPLNKMRDERRDLSI-LS 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1368 KLKFEASEERVKSLEDKLKTM---PLRDRTnlpvgdIIKNRDSISKYEEEIRYYKLENyklqEILnESNGKLSQLTLDLR 1444
Cdd:TIGR02169 595 EDGVIGFAVDLVEFDPKYEPAfkyVFGDTL------VVEDIEAARRLMGKYRMVTLEG----ELF-EKSGAMTGGSRAPR 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1445 QSKSKEALLSEQLDRLQKDLESTERQKELLSSTIKQQKQQFENCMDDLQGNELRLREHIHALKQAEEDVKNMASIIEKLK 1524
Cdd:TIGR02169 664 GGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1525 TQNKQKEKLIWEREMERNDSDMQLQETLLELKRVQDVKKILSDDLAHlkERLSAVEDRSQYTDEINRLKEELNCSLKAET 1604
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKL 821
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1605 N---LKKEFATLKYK-LETSTNDSEAKISDLLKQLDHYTKVVEMLNNEKDAISLAEKELYQKYEALNTECESLKGKIVSL 1680
Cdd:TIGR02169 822 NrltLEKEYLEKEIQeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1681 TKIKQELESDLNQKTDALQISNAALSSSTQKNKEITEKIKYLEE---------TLQLQMEqnsRNGELVKTLQASCNGYK 1751
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelsleDVQAELQ---RVEEEIRALEPVNMLAI 978
|
890 900 910
....*....|....*....|....*....|....*.
gi 6321812 1752 DKFDDEKQKNIDLYEENQTLQKLNTDLQLQLKNLHE 1787
Cdd:TIGR02169 979 QEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
862-1189 |
1.04e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 80.50 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 862 RTKKFNEQINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQFDDLVSEKD 941
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 942 EISREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSK-NNELIKQISDLNCDISKEQSSQSLIK---ESKLK----- 1012
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlSHSRIPEIQAELSKLEEEVSRIEARLreiEQKLNrltle 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1013 ---LENEIKRLKDVINSKEEEIKSFNDKLSSSE---EDLDIKLVTLEKNCNIAMSRLQSLVTENSDLRSKNENFKKEKAA 1086
Cdd:TIGR02169 828 keyLEKEIQELQEQRIDLKEQIKSIEKEIENLNgkkEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1087 LNNQLKNKESELLKMKEKIDNHKKELATFSKQRDDAVSEHG-------------KITAEL--------------KETRIQ 1139
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEeelsledvqaelqRVEEEIralepvnmlaiqeyEEVLKR 987
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 6321812 1140 LTEYKSNYQKIKEEYSNFQRETKEQEQKKRNSLVESLND--SKIKELEARLS 1189
Cdd:TIGR02169 988 LDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAinENFNEIFAELS 1039
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
877-1688 |
1.22e-14 |
|
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: 80.02 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 877 LQEMESKKKFLEEKNQKTVNELENTQdLLNQEKENLRKNESLLNRVKTSSETLQKQFDDLVSEKDEISREKLEVAQNLEE 956
Cdd:pfam02463 202 LKEQAKKALEYYQLKEKLELEEEYLL-YLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 957 ---AHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQSLIKESKLKLENEIKRLKDVINSKEEEIKS 1033
Cdd:pfam02463 281 kklQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1034 FNDKLSSSEEDLDIKLVTlekncniamsrlqslvtensdlrsknenFKKEKAALNNQLKNKESELLKMKEKIDNHKKELA 1113
Cdd:pfam02463 361 LEKLQEKLEQLEEELLAK----------------------------KKLESERLSSAAKLKEEELELKSEEEKEAQLLLE 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1114 TFSKQRDDAVSEHGKITAELKETRIqLTEYKSNYQKIKEEYSNFQRETK-------EQEQKKRNSLVESLNDSKIKELEA 1186
Cdd:pfam02463 413 LARQLEDLLKEEKKEELEILEEEEE-SIELKQGKLTEEKEELEKQELKLlkdelelKKSEDLLKETQLVKLQEQLELLLS 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1187 RLSQEISLNQYLNKRISGNSVETNISSTRRSTSYSDDPLDKED-IIKKYYDLQLAFTEITRNLENEIEEKKNLISRLRFT 1265
Cdd:pfam02463 492 RQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLgVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1266 ETRLASSSFEDQKIKAQMKKLKKLIQDMDPSIPLDSILNEPLDNCPDK-----ESDINKLMLEVDYLKRQLDIETRAHYD 1340
Cdd:pfam02463 572 ELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDkrakvVEGILKDTELTKLKESAKAKESGLRKG 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1341 AENAI------------SALHSKFRKIQGESSLSSSDIYKLKFEASEERVKSLEDKLKTMPLRDRTNLPVGDIIKNRDSI 1408
Cdd:pfam02463 652 VSLEEglaeksevkaslSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1409 SKYEEEIRYYKLENYKLQEILNESNGKLSQLTLDLRQSKSKEALLSEQLDRLQKDLESTERQKELLSSTIKQQKQQFENC 1488
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1489 MDDLQGNELRLREHIHALKQAEEDVKNMASIIEKLKTQNKQKEKLIWEREMERNDSDMQLQETLLELKRVQDVKKILSDD 1568
Cdd:pfam02463 812 EEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESK 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1569 LAHLKERLSAVEDRSQYTDEINRLKEELNCSLKAETNLKKEFATLKYKLETSTNDSEAKISDLLKQLDHY---TKVVEML 1645
Cdd:pfam02463 892 EEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERnkrLLLAKEE 971
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 6321812 1646 NNEKDAISLAEK-ELYQKYEALNTECESLKGKIVSLTKIKQELE 1688
Cdd:pfam02463 972 LGKVNLMAIEEFeEKEERYNKDELEKERLEEEKKKLIRAIIEET 1015
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
861-1479 |
7.77e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 76.98 E-value: 7.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 861 TRTKKFNEQINKLKNDLQEMESKKKFLEeknqKTVNELENTQDLLNQEKENLRKNESLLN-RVKTSSETLQKQFDDLVSE 939
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKNKEKELKNLD----KNLNKDEEKINNSNNKIKILEQQIKDLNdKLKKNKDKINKLNSDLSKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 940 KDEISREKlevaQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKeqssqslIKESKLKLENEIKR 1019
Cdd:TIGR04523 109 NSEIKNDK----EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-------LKKQKEELENELNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1020 LKDVINSKEEEIKSFNDKLSSSEEDLDIKLVTLEKNcniamsrlQSLVTENSDLRSKNENFKKEKAALNNQLKNKESELL 1099
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN--------KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1100 KMKEKIDNHKKELATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQKIK-EEYSNFQRETKEQEQKKRNSLVESLND 1178
Cdd:TIGR04523 250 NTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNnQKEQDWNKELKSELKNQEKKLEEIQNQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1179 -SKIKELEARLSQEISLNQYLNKRISGNSVETNISSTRRSTSYSDDPLDKEDIIKKYYDLQLAFTEITRNLENEIEEKKN 1257
Cdd:TIGR04523 330 iSQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1258 LISRLRFTETRLASSSFEDQKIKAQMKKLKKLIQDMDPSIPLDSILNEPLDNCPDK--------ESDINKLMLEVDYLKR 1329
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESletqlkvlSRSINKIKQNLEQKQK 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1330 QLDIETRAHYDAENAISALHSKFRKIQGESSLSSSDIYKLKFEAS--EERVKSLEDKLKTMPLRDRTNLPVGDIIKNRDS 1407
Cdd:TIGR04523 490 ELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKekESKISDLEDELNKDDFELKKENLEKEIDEKNKE 569
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321812 1408 ISKYEEEIRYYKLENYKLQEILNESNGKLSQLTldlrqskSKEALLSEQLDRLQKDLESTERQKELLSSTIK 1479
Cdd:TIGR04523 570 IEELKQTQKSLKKKQEEKQELIDQKEKEKKDLI-------KEIEEKEKKISSLEKELEKAKKENEKLSSIIK 634
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1242-1900 |
1.41e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.17 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1242 TEITRNLENEIEEKKNLISRLRFTEtrlasssfEDQKIKAQMKKLKKLIQDMDPsipLDSILNEpldncpdKESDINKLM 1321
Cdd:TIGR02168 212 AERYKELKAELRELELALLVLRLEE--------LREELEELQEELKEAEEELEE---LTAELQE-------LEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1322 LEVDYLKRQLDIETRAHYDAENAISALHSKFRKIQGESSLSSSDIYKLKFEASEERVKSLEDKLKTMPLRDRTNLPVGDI 1401
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1402 IKNRDSISKYEEEIRYYKLENYKLQEILNESNGKLSQLtldlrqsKSKEALLSEQLDRLQKDLESTERQKELLSSTIKQQ 1481
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL-------ELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1482 KQQF-ENCMDDLQGNELRLREHIHALKQAEEDVKNMASIIEKLKTQNKQKEKLIwEREMERNDSDMQLQETLLE------ 1554
Cdd:TIGR02168 427 LKKLeEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA-ERELAQLQARLDSLERLQEnlegfs 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1555 --LKRVQDVKKILSDDLAHLKERLSA--------------------VEDRSQYTDEINRLKE-----------------E 1595
Cdd:TIGR02168 506 egVKALLKNQSGLSGILGVLSELISVdegyeaaieaalggrlqavvVENLNAAKKAIAFLKQnelgrvtflpldsikgtE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1596 LNCSLKAETNLKKEFATLKYKLETSTNDSEAKISDLL----------------KQLDHYTKVV----EMLN--------- 1646
Cdd:TIGR02168 586 IQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLggvlvvddldnalelaKKLRPGYRIVtldgDLVRpggvitggs 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1647 NEKDAISLAEKelyQKYEALNTECESLKGKIVSLTKIKQELESDLNQKTDALQISNAALSSSTQKNKEITEKIKYLEETL 1726
Cdd:TIGR02168 666 AKTNSSILERR---REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1727 QLQMEQNSRNGELVKTLQASCNGYKDKFDDEKQKNIDLYEENQTLQKLNTDLQLQLK-------NLHERLSDTTEknawl 1799
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrealdELRAELTLLNE----- 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1800 sKIHELENmvsletdlKYEEMKKNK-SLERAVEELQTKNSQQTDVIELANKNRSEFEEATLKYEAQISDLEKYISQQELE 1878
Cdd:TIGR02168 818 -EAANLRE--------RLESLERRIaATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
730 740
....*....|....*....|..
gi 6321812 1879 MKKSIRDNSSYRDKVQEMAQEI 1900
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKR 910
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
981-1760 |
2.39e-12 |
|
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: 72.77 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 981 KNNELIKQI-SDLNCDISKEQSSQSLIKESKLKLENeikrLKDVINSKEEEIKSFNDKLSSSEEDLDiKLVTLEKNCNIA 1059
Cdd:TIGR00606 186 KALETLRQVrQTQGQKVQEHQMELKYLKQYKEKACE----IRDQITSKEAQLESSREIVKSYENELD-PLKNRLKEIEHN 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1060 MSRLQSLVTENSDLRSKnenfKKEKAALNNQLKNKESELL-----KMKEKIDNHKKELATFSKQRDDAVSEHGKITAELK 1134
Cdd:TIGR00606 261 LSKIMKLDNEIKALKSR----KKQMEKDNSELELKMEKVFqgtdeQLNDLYHNHQRTVREKERELVDCQRELEKLNKERR 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1135 ETRIQLTEYKsnyqkIKEEYSNFQRETKEQEQKKRNSLVESLN-DSKIKELEARLSQEISLNQYLNKRISGNSVETNISS 1213
Cdd:TIGR00606 337 LLNQEKTELL-----VEQGRLQLQADRHQEHIRARDSLIQSLAtRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1214 TRRSTSYSDDPLDKEDIIKkyydLQLAFTEITRNLENEIEEKKNLISRLRFTETRLasssfedQKIKAQMKKLKKLIQDM 1293
Cdd:TIGR00606 412 QLCADLQSKERLKQEQADE----IRDEKKGLGRTIELKKEILEKKQEELKFVIKEL-------QQLEGSSDRILELDQEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1294 DPSIPLDSILnepldncpDKESDINKLMLEVDYLK-RQLDIETRAHYDAENAISALHSKFRKIQGES-----SLSSSDIY 1367
Cdd:TIGR00606 481 RKAERELSKA--------EKNSLTETLKKEVKSLQnEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMltkdkMDKDEQIR 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1368 KLKFEASEERVKSLEDKLKTMPLRDRTNLPVGDIIKNRDSISKYEEEIRYYKLENYKLQEILNESNGKLSQLTLDLRQSK 1447
Cdd:TIGR00606 553 KIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVC 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1448 SKEALLSEqLDRLQKDLESTERQKELLSSTIKQQKQQFENCMDDLQGNELRLREHIHALKQAEEDVKNMASIIEKLKTQN 1527
Cdd:TIGR00606 633 GSQDEESD-LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKL 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1528 KQKEKLIWEREMERND---------SDMQLQETllELKRVQDVKKILSDDLAHLKERLSAVEdrsqytdeinRLKEELNC 1598
Cdd:TIGR00606 712 KSTESELKKKEKRRDEmlglapgrqSIIDLKEK--EIPELRNKLQKVNRDIQRLKNDIEEQE----------TLLGTIMP 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1599 SLKAETNLKKEFATLKyKLETSTNDSEAKISDLLKQLDHY--TKVVEMLNNEKDAISLAEKELYQKYEALNTECESLKGK 1676
Cdd:TIGR00606 780 EEESAKVCLTDVTIME-RFQMELKDVERKIAQQAAKLQGSdlDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQ 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1677 IVSLTKIKQELESDLNQKTDALQISNAALSSSTQKNKEITEKIKYLEET-------LQLQMEQNSRNGELVKTLQASCNG 1749
Cdd:TIGR00606 859 IQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAkeqdsplETFLEKDQQEKEELISSKETSNKK 938
|
810
....*....|.
gi 6321812 1750 YKDKFDDEKQK 1760
Cdd:TIGR00606 939 AQDKVNDIKEK 949
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
870-1190 |
3.71e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.01 E-value: 3.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 870 INKLKNDLQEMESKkkflEEKNQKTVNELENTQDLLNQEKENLRK----NESLLNRVKTSSETLQKQFDDLVSEKDEISR 945
Cdd:TIGR02168 679 IEELEEKIEELEEK----IAELEKALAELRKELEELEEELEQLRKeleeLSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 946 EKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQSLIKESKLKLENEIKRLKDVIN 1025
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1026 SKEEEIKSFNDKLSSSEEdlDIKLVTLEkncniamsrLQSLVTENSDLRSKNENFKKEKAALNNQLKNKESELLKMKEKI 1105
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSE--DIESLAAE---------IEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1106 DNHKKELATFSKQRDDAVSEHGKITAELKETRIQLTEYKsnyQKIKEEYSNFQRETKEQEQKKRNSLVESlnDSKIKELE 1185
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ---ERLSEEYSLTLEEAEALENKIEDDEEEA--RRRLKRLE 978
|
....*
gi 6321812 1186 ARLSQ 1190
Cdd:TIGR02168 979 NKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1128-1880 |
7.66e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.86 E-value: 7.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1128 KITAELKETRIQLteYKSNYQKIKEEYSNFQRETKEQEQKKRNSlveslnDSKIKELEARLSQEISLNQYLNKRIsgnsv 1207
Cdd:TIGR02168 217 ELKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEEL------TAELQELEEKLEELRLEVSELEEEI----- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1208 etnisstrrstsysddpldkEDIIKKYYDLQlafTEITRnLENEIEEKKNlisRLRFTETRLASSSFEDQKIKAQMKKLK 1287
Cdd:TIGR02168 284 --------------------EELQKELYALA---NEISR-LEQQKQILRE---RLANLERQLEELEAQLEELESKLDELA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1288 KLIQDMDPsipldsILNEPLDNCPDKESDINKLMLEVDYLKRQLDietrahyDAENAISALHSKFRKIQGESSLSSSDIy 1367
Cdd:TIGR02168 337 EELAELEE------KLEELKEELESLEAELEELEAELEELESRLE-------ELEEQLETLRSKVAQLELQIASLNNEI- 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1368 klkfEASEERVKSLEDKLKTMPLRDRTNLPVGDIIKNRDSISKYEEEIRyyklENYKLQEILNESNGKLSQLTLDLRQSK 1447
Cdd:TIGR02168 403 ----ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEE----ELEELQEELERLEEALEELREELEEAE 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1448 SKEALLSEQLDRLQKDLESTERQKELLSS------TIKQQKQQFENCMDDL-----------QGNELRLREHIHALkqAE 1510
Cdd:TIGR02168 475 QALDAAERELAQLQARLDSLERLQENLEGfsegvkALLKNQSGLSGILGVLselisvdegyeAAIEAALGGRLQAV--VV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1511 EDVKNMASIIEKLKTQNKQK-----EKLIWEREMERNDSDMQLQET--LLELKRVQDVKKILSDDLAHLKERLSAVEDRS 1583
Cdd:TIGR02168 553 ENLNAAKKAIAFLKQNELGRvtflpLDSIKGTEIQGNDREILKNIEgfLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLD 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1584 QYTDEINRLKEELNC-----------------SLKAETNL---KKEFATLKYKLEtstnDSEAKISDLLKQLDHYTKVVE 1643
Cdd:TIGR02168 633 NALELAKKLRPGYRIvtldgdlvrpggvitggSAKTNSSIlerRREIEELEEKIE----ELEEKIAELEKALAELRKELE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1644 MLNNEKDAISLAEKELYQKYEALNTECESLKGKIVSLTKIKQELESDLNQKTDALQISNAALSSSTQKNKEITEKIKYLE 1723
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1724 ETLQLQMEQNSRNGELVKTLQASCNGYKDKFDDEKQKNIDLYEENQTLQKLNTDLQLQLKNLHERLSdttEKNAWLSKIH 1803
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE---SLAAEIEELE 865
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321812 1804 ELENMVSLETDLKYEEMkknKSLERAVEELQTKNSQQTDVIELANKNRSEFEEATLKYEAQISDLEkyISQQELEMK 1880
Cdd:TIGR02168 866 ELIEELESELEALLNER---ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE--LRLEGLEVR 937
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
885-1196 |
4.36e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 885 KFLEEKnQKTVNELENTQdllnqekENLRKNESLLNRVKTSSETLQKQ------FDDLVSEKDE------------ISRE 946
Cdd:COG1196 169 KYKERK-EEAERKLEATE-------ENLERLEDILGELERQLEPLERQaekaerYRELKEELKEleaellllklreLEAE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 947 KLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCD-------ISKEQSSQSLIKESKLKLENEIKR 1019
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyellaeLARLEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1020 LKDVINSKEEEIKSFNDKLSSSEE---DLDIKLVTLEKNCNIAMSRLQSLVTENSDLRSKNENFKKEKAALNNQLKNKES 1096
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEeleEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1097 ELLKMKEKIDNHKKELATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQKIKEEysNFQRETKEQEQKKRNSLVESL 1176
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE--EEALLELLAELLEEAALLEAA 478
|
330 340
....*....|....*....|
gi 6321812 1177 NDSKIKELEARLSQEISLNQ 1196
Cdd:COG1196 479 LAELLEELAEAAARLLLLLE 498
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1250-1869 |
5.02e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 68.07 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1250 NEIEEKKNLISRL---RFTETRLASSSFEDQKIKAQMKKLKKLIQDMDPSIPLDSILNEPLDNCPDKESDINKLMLEVDY 1326
Cdd:TIGR00618 126 SETEEVIHDLLKLdykTFTRVVLLPQGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1327 LKRQLDIETRAHYDAENAISALHSKFRKIQGESSLSSSDiYKLKFEASEERvKSLEDKLKTMPLRDRTNLPvgdiIKNRD 1406
Cdd:TIGR00618 206 LTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY-LTQKREAQEEQ-LKKQQLLKQLRARIEELRA----QEAVL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1407 SISKYEEEIRYYKLENYKLQEILNESNGKLSQLTLDLRQSKSKEALLSEQLDRLQKDLESTERQKELLSsTIKQQKQQFE 1486
Cdd:TIGR00618 280 EETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ-TLHSQEIHIR 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1487 NCMD------DLQGNELRLREHIHALKQ----AEEDVKNMASIIEKLKTQNKQKEKLIWEREMERNDSDMQLQETLLELK 1556
Cdd:TIGR00618 359 DAHEvatsirEISCQQHTLTQHIHTLQQqkttLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQR 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1557 RVQDVKKILSDDLAHLKERLSAVEDRSQYTDEINRLKEELNCSLKAETNLKKEfaTLKYKLETSTNDSEakisdLLKQLD 1636
Cdd:TIGR00618 439 YAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAV--VLARLLELQEEPCP-----LCGSCI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1637 HYTKVVEMLNNEKDAISLAEKeLYQKYEALNTECESLKGKIVSLTKIKQELESDLNQKTDALQIsnaaLSSSTQKNKEIT 1716
Cdd:TIGR00618 512 HPNPARQDIDNPGPLTRRMQR-GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSI----LTQCDNRSKEDI 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1717 EKIKYLEETLQLQMEQNSRngelvktLQASCNGYKDKFDDEKQKNIDLYEENQTLQKLNTDLQLQLKNLH---ERLSDTT 1793
Cdd:TIGR00618 587 PNLQNITVRLQDLTEKLSE-------AEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHalqLTLTQER 659
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321812 1794 EKNAWL-SKIHELENMVSLETDLKYEEMKKnKSLERAVEELQTKNSQQTDVIELANKNRSEFEEATLKYEAQISDLE 1869
Cdd:TIGR00618 660 VREHALsIRVLPKELLASRQLALQKMQSEK-EQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLA 735
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
862-1152 |
5.67e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 862 RTKKFNEQINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQFDDLVSEKD 941
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 942 EISREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQ-------SLIKESKLKLE 1014
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLeslerriAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1015 NEIKRLKDVINSKEEEIKSFNDKLSSSEEDLDIKLV---TLEKNCNIAMSRLQSLVTENSDLRSKNENFKKEKAALNNQL 1091
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNeraSLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321812 1092 KNKESELLKMKEKIDNHKKELAT-FSKQRDDAVSEHGKITAELKETRIQLTEYKsnyQKIKE 1152
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEeYSLTLEEAEALENKIEDDEEEARRRLKRLE---NKIKE 983
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
944-1171 |
1.94e-10 |
|
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: 64.79 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 944 SREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQSLIKESKLKLENEIKRLKDV 1023
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1024 INSKEEEIKSFNDKLSSSEEDLDIKLVTLEKNCNIAMSRLQSLVTENSDLRSKNENFKKEKAALNNQLKNKESELLKMKE 1103
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321812 1104 KIDNHKKELATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQKIKEEYSNFQRETKEQEQKKRNS 1171
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
853-1290 |
2.89e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.43 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 853 LLTSSNDMTRTKKFNEQINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQ 932
Cdd:TIGR04523 175 LNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQ 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 933 FDDLVSEKDEISREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIkqISDLNCDISKEQSSQSLIKESKLK 1012
Cdd:TIGR04523 255 LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW--NKELKSELKNQEKKLEEIQNQISQ 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1013 LENEIKRLKDVINSKEEEIKSFNDKLSSSEEDLD---IKLVTLEKNCNIAMSRLQSLVTENSDLRSKNENFKKEKAALNN 1089
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSEKQRELEekqNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1090 QLKNKESELLKMKEKIDNHKKELATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQKIKEEYSNFQR--ETKEQEQK 1167
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQnlEQKQKELK 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1168 KRNSLVESLNDSKiKELEARlsqeislNQYLNKRISgnSVETNISSTRRSTSYSDDPLD--KEDIIKKYYDLQlafteiT 1245
Cdd:TIGR04523 493 SKEKELKKLNEEK-KELEEK-------VKDLTKKIS--SLKEKIEKLESEKKEKESKISdlEDELNKDDFELK------K 556
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 6321812 1246 RNLENEIEEKKNLISRLRFTETRLASSSFEDQKIKAQMKKLKKLI 1290
Cdd:TIGR04523 557 ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL 601
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1233-1906 |
3.94e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.47 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1233 KYYDLQ-----LAFTEITRNLENEIEEKKNLISRLRFTETRLASSSFEDQKIKAQMKKLKKLIQDmdpsipldsiLNEPL 1307
Cdd:TIGR02169 212 RYQALLkekreYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE----------LNKKI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1308 DNCPDKE-----SDINKLMLEVDYLKRQLDIETRAHYDAENAISALHSKFRKIQGESSLSSSDI--YKLKFEASEERVKS 1380
Cdd:TIGR02169 282 KDLGEEEqlrvkEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIeeERKRRDKLTEEYAE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1381 LEDKLKTmpLRDRTNLPVGDIIKNRDSISKYEEEIRyyklenyKLQEILNESNGKLSQLTLDLRQSKSKEALLSEQLDRL 1460
Cdd:TIGR02169 362 LKEELED--LRAELEEVDKEFAETRDELKDYREKLE-------KLKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1461 QKDLESTERQKELLSSTIKQQKQQFENCMDDLQGNELRLREHIHALKQAEEDVKNMASIIEKLKTQNKQKEKLIWER--- 1537
Cdd:TIGR02169 433 EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGrav 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1538 EMERNDSDMQLQETLLELKRVqDVKKILSDDLAhLKERLSA--VEDRSQYTDEINRLKEElNCSLKAETNLKKEFATLKY 1615
Cdd:TIGR02169 513 EEVLKASIQGVHGTVAQLGSV-GERYATAIEVA-AGNRLNNvvVEDDAVAKEAIELLKRR-KAGRATFLPLNKMRDERRD 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1616 KLETSTN----------DSEAKISDLLKQLDHYTKVVEMLNNEKDAISLA-----EKELYQKYEALNTECESLKGKIVSL 1680
Cdd:TIGR02169 590 LSILSEDgvigfavdlvEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYrmvtlEGELFEKSGAMTGGSRAPRGGILFS 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1681 TKIKQELESdLNQKTDALQISNAAL-----------SSSTQKNKEITEKIKYLEETLQLQMEQNSRNGELVKTLQASCNG 1749
Cdd:TIGR02169 670 RSEPAELQR-LRERLEGLKRELSSLqselrrienrlDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1750 YKDKFDDEKQKNIDLYEENQTLQKLNTDLQLQLKNLHERLSDT-------------TEKNAWLSKIHELENMVSLETDLK 1816
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSripeiqaelskleEEVSRIEARLREIEQKLNRLTLEK 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1817 YEEMKKNKSLERAVEELQTKNSQQTDVIELANKNRSEFEEATLKYEAQISDLEKYISQQELEMKKSIRDNSSYRDKVQEM 1896
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
730
....*....|
gi 6321812 1897 AQEIEFWKSR 1906
Cdd:TIGR02169 909 EAQIEKKRKR 918
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
869-1173 |
6.01e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 869 QINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQFDDLVSEKDEISREKL 948
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 949 EVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLncdiskeQSSQSLIKESKLKLENEIKRLKDVINSKE 1028
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA-------EEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1029 EEIKSFNDKLSSSEEDldikLVTLEKNCNIAMSRLQSLVTENSDLRSKNENFKKEKAALNNQLKNKESELLKMKEKIDNH 1108
Cdd:COG1196 379 EELEELAEELLEALRA----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321812 1109 KKELATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNY---QKIKEEYSNFQRETKEQEQKKRNSLV 1173
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLlllLEAEADYEGFLEGVKAALLLAGLRGL 522
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1430-1880 |
1.14e-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: 63.60 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1430 NESNGKLSQLTLDLRQSKSKEALLSEQLDRLQKDLESTERQKELLSSTIKQQKQQFENCMDDLQG----NELRLREHIHa 1505
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKlrsrVDLKLQELQH- 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1506 LKQAEEDVKNMASIIEKLKTQNKQKEKLIwerEMERndsdmqlqetllelKRVQDVKKILSDdlaHLKERLSAVEDRSQY 1585
Cdd:pfam15921 536 LKNEGDHLRNVQTECEALKLQMAEKDKVI---EILR--------------QQIENMTQLVGQ---HGRTAGAMQVEKAQL 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1586 TDEINRLKEELncslkaetnlkKEFATLKYKLETSTNDSEAKISDLlkQLDHytkvVEMLNNEKDAISlAEKELYQKYEA 1665
Cdd:pfam15921 596 EKEINDRRLEL-----------QEFKILKDKKDAKIRELEARVSDL--ELEK----VKLVNAGSERLR-AVKDIKQERDQ 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1666 LNTECESLKGKIVSLTKIKQELESDLNQKTDALQISnaalssstqknkeiTEKIKYLEETLQLQMEQnSRNgeLVKTLQA 1745
Cdd:pfam15921 658 LLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETT--------------TNKLKMQLKSAQSELEQ-TRN--TLKSMEG 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1746 ScNGYKDKFDDEKQKNIdlyeenqTLQKLNTD-LQLQLKNLHERLSDTTEKNAWLSkihelENMVSLETDLKYEEMKKNK 1824
Cdd:pfam15921 721 S-DGHAMKVAMGMQKQI-------TAKRGQIDaLQSKIQFLEEAMTNANKEKHFLK-----EEKNKLSQELSTVATEKNK 787
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 6321812 1825 slerAVEELQTKNSQQTDVIELANKNRSEFEEATLKYeAQISDLEKYISQQELEMK 1880
Cdd:pfam15921 788 ----MAGELEVLRSQERRLKEKVANMEVALDKASLQF-AECQDIIQRQEQESVRLK 838
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
861-1190 |
2.09e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.75 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 861 TRTKKFNEQINKLKNDLQEMESKKKFLEEKNQKTVNELENTqdllnqeKENLRKNESLLNRVKTSSETLQKQFDDLVSEK 940
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEA-------REAVEDRREEIEELEEEIEELRERFGDAPVDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 941 DEISREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHS--------------KNNELIKQISDLNCDISKEQSSQSLI 1006
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1007 KESKLKLENEIKRLKDVINSkEEEIKSFNDKLSSSEEDLDIKLVTLEKNcniaMSRLQSLVTENSDLRSKNENfKKEKAA 1086
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELIAERRETIEEK----RERAEELRERAAELEAEAEE-KREAAA 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1087 lnnqlkNKESELLKMKEKIDNHKKELATFSKQRD--DAVSEHGKITAELKETRIQLTEYKSNYQKIKEEysnfQRETKEQ 1164
Cdd:PRK02224 562 ------EAEEEAEEAREEVAELNSKLAELKERIEslERIRTLLAAIADAEDEIERLREKREALAELNDE----RRERLAE 631
|
330 340
....*....|....*....|....*.
gi 6321812 1165 EQKKRNSLVESLNDSKIKELEARLSQ 1190
Cdd:PRK02224 632 KRERKRELEAEFDEARIEEAREDKER 657
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
865-1182 |
2.13e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 62.73 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 865 KFNEQINKLKNDLQEMES----KKKFLEEKNQKtVNELENTQDLLNQEKENLRKNESLLNR----VKTSSETLQKQFDDL 936
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESenseKQRELEEKQNE-IEKLKKENQSYKQEIKNLESQINDLESkiqnQEKLNQQKDEQIKKL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 937 VSEKDEISREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQSLIKESKLKLENE 1016
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1017 IKRLKDVINSKEEEIKSFNDKLSSSEEDLDI----------KLVTLEKNCNIAMSRLQS--LVTENSDLRSKNENFKKEK 1084
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKlesekkekesKISDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQ 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1085 AALNNQLKNKESELLKMKEKIDNHKKELATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQKIKEEYSNFQRETKEQ 1164
Cdd:TIGR04523 578 KSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEI 657
|
330
....*....|....*...
gi 6321812 1165 EQKKRNsLVESLNDSKIK 1182
Cdd:TIGR04523 658 RNKWPE-IIKKIKESKTK 674
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
866-1267 |
2.20e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 866 FNEQINKLKNDLQEMESKKKFLEE--KNQKTVNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQFDdLVSEKDEI 943
Cdd:COG4717 59 FKPQGRKPELNLKELKELEEELKEaeEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-LYQELEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 944 SREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLncDISKEQSSQSLIKE------SKLKLENEI 1017
Cdd:COG4717 138 EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL--SLATEEELQDLAEEleelqqRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1018 KRLKDVINSKEEEIKSFNDKLSSS--EEDLDIKLVTLekncnIAMSRLQSLVTENSDLRSKNEN---------------- 1079
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAalEERLKEARLLL-----LIAAALLALLGLGGSLLSLILTiagvlflvlgllallf 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1080 --FKKEKAALNNQLKnkesELLKMKEKIDNHKKELATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQKIKEEYsnf 1157
Cdd:COG4717 291 llLAREKASLGKEAE----ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1158 qreTKEQEQKKRNSLVESLNDSKIKELEARLSQeisLNQYLNKRISGNSVETNISSTRRSTSYSDDPLDKEDIIKKYYDL 1237
Cdd:COG4717 364 ---QLEELEQEIAALLAEAGVEDEEELRAALEQ---AEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEEL 437
|
410 420 430
....*....|....*....|....*....|
gi 6321812 1238 QLAFTEITRNLENEIEEKKNLISRLRFTET 1267
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEE 467
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
867-1596 |
2.90e-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: 62.29 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 867 NEQINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLRKnESLLNRVKTSSETLQKQFDDLVSEKDEISRE 946
Cdd:TIGR00618 211 PCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKK-QQLLKQLRARIEELRAQEAVLEETQERINRA 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 947 K-----LEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLncdiskeqssqslikESKLKLENEIKRLK 1021
Cdd:TIGR00618 290 RkaaplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSI---------------EEQRRLLQTLHSQE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1022 DVINSKEEEIKSFNDKLSSSEEDLDiklvtlekncniamsRLQSLvtensdlrsknenfKKEKAALNNQLKNKESELLKM 1101
Cdd:TIGR00618 355 IHIRDAHEVATSIREISCQQHTLTQ---------------HIHTL--------------QQQKTTLTQKLQSLCKELDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1102 KEKIDNHKKELATFSKQRDDAVSEHGKITAELKETRIQ----LTEYKSNYQKIKEEYSNFQReTKEQEQKKRNSLVESLN 1177
Cdd:TIGR00618 406 QREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCaaaiTCTAQCEKLEKIHLQESAQS-LKEREQQLQTKEQIHLQ 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1178 DSKIKELEARLSQEISLNQYLnkrISGNSVETNISSTRRSTSYSDDPLdKEDIIKKYYDLQLAFTEITRNLE---NEIEE 1254
Cdd:TIGR00618 485 ETRKKAVVLARLLELQEEPCP---LCGSCIHPNPARQDIDNPGPLTRR-MQRGEQTYAQLETSEEDVYHQLTserKQRAS 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1255 KKNLISRLRFTETRLASssfEDQKIKAQMKKLKKLIQDMDPSIPLDsilnepldncpDKESDinKLMLEVDYLKRQLDIE 1334
Cdd:TIGR00618 561 LKEQMQEIQQSFSILTQ---CDNRSKEDIPNLQNITVRLQDLTEKL-----------SEAED--MLACEQHALLRKLQPE 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1335 trahydAENAISALHSKFRKIQGESSLSSSDIYKLKFEASEERVKSLEDK-LKTMPLRDRTNLPvgDIIKNRDSISKYEE 1413
Cdd:TIGR00618 625 ------QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRvLPKELLASRQLAL--QKMQSEKEQLTYWK 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1414 EIRYYKLEnyKLQEILnESNGKLSQLTLDLRQ-SKSKEALLSEQLDRLQKDLESTERQ-KELLSSTIKQQKQQFENCMDD 1491
Cdd:TIGR00618 697 EMLAQCQT--LLRELE-THIEEYDREFNEIENaSSSLGSDLAAREDALNQSLKELMHQaRTVLKARTEAHFNNNEEVTAA 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1492 LQgnelRLREHIHALKQAEEDVKNMASIIEKLKTQNKQKEKLIWEREMERNDSDMQLQEtllELKRVQDVKKILSDDLAH 1571
Cdd:TIGR00618 774 LQ----TGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQ---EEEQFLSRLEEKSATLGE 846
|
730 740
....*....|....*....|....*
gi 6321812 1572 LKERLSAVEDRSQYTDEINRLKEEL 1596
Cdd:TIGR00618 847 ITHQLLKYEECSKQLAQLTQEQAKI 871
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
860-1126 |
1.32e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 860 MTRTKKFNEQINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQE------------KENLRKNESLLNRV--KTS 925
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSripeiqaelsklEEEVSRIEARLREIeqKLN 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 926 SETLQKQF-----DDLVSEKDEISREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQ 1000
Cdd:TIGR02169 823 RLTLEKEYlekeiQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1001 SSQSLIKESKLKLENEIKRLKDVINSKEEEIKSFNDKL----SSSEEDLDIKlvTLEKNCNIAMSRLQSLvtENSDLRSK 1076
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKgedeEIPEEELSLE--DVQAELQRVEEEIRAL--EPVNMLAI 978
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 6321812 1077 NEnFKKEKAALN------NQLKNKESELLKMKEKIDNHKKE--LATFskqrdDAVSEH 1126
Cdd:TIGR02169 979 QE-YEEVLKRLDelkekrAKLEEERKAILERIEEYEKKKREvfMEAF-----EAINEN 1030
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1479-1854 |
1.77e-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: 60.07 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1479 KQQKQQFENCMDDLQGNELRLREHIHALKQAEEDVKNMASIIEK---LKTQNKQKEKLIWEREMERNDSdmQLQETLLEL 1555
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykeLKAELRELELALLVLRLEELRE--ELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1556 KRVQDVKKILSDDLAHLKERLSAVEDrsqytdEINRLKEELNCSLKAETNLKKEFATLKYKLETStndsEAKISDLLKQL 1635
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRL------EVSELEEEIEELQKELYALANEISRLEQQKQIL----RERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1636 DHYTKVVEMLNNEKDAISLAEKELYQKYEALNTECESLKGKIVSLTKIKQELESDLNQKTDALQISNAALSSSTQKNKEI 1715
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1716 TEKIKYLEETLQlQMEQNsrngelvktlqascngyKDKFDDEKQKNIDLYEENQtLQKLNTDLQLQLKNLHERLSDTTEK 1795
Cdd:TIGR02168 399 NNEIERLEARLE-RLEDR-----------------RERLQQEIEELLKKLEEAE-LKELQAELEELEEELEELQEELERL 459
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 6321812 1796 NAWLSKIHELENMVSLETDLKYEEMKKNKSLERAVEELQTKNSQQTDVIELANKNRSEF 1854
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL 518
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
870-1158 |
1.77e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 59.75 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 870 INKLKNDLQEmesKKKFLEEKNQKtVNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQfddlVSEKD---EISRE 946
Cdd:pfam15921 498 VSDLTASLQE---KERAIEATNAE-ITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQ----MAEKDkviEILRQ 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 947 KLEVAQNLEEAHQKIQG--------LQETIREREATLEKLH-------SKNNELIKQISDLNCDISK--EQSSQSL---- 1005
Cdd:pfam15921 570 QIENMTQLVGQHGRTAGamqvekaqLEKEINDRRLELQEFKilkdkkdAKIRELEARVSDLELEKVKlvNAGSERLravk 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1006 -IKESKLKLENEIKRLKDVINSKEEEIKSFNDKLSSSEEDLDIKLVTLEKNCNIAMSRLQSLVTENSDLRSKNENFKKEK 1084
Cdd:pfam15921 650 dIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVA 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1085 AALNNQLKNKESELLKMKEKIDNHKKELATFSKQRDDAVSEHGKITAELKETRI-------QLTEYKSNYQKIKEEYSNF 1157
Cdd:pfam15921 730 MGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATeknkmagELEVLRSQERRLKEKVANM 809
|
.
gi 6321812 1158 Q 1158
Cdd:pfam15921 810 E 810
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1453-1801 |
1.83e-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: 59.69 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1453 LSEQLDRLQKDLESTERQKELlsstikqqKQQFENCMDDLQGneLRLREHIHALKQAEEDVKNMASIIEKLKTQNKQKEK 1532
Cdd:TIGR02168 198 LERQLKSLERQAEKAERYKEL--------KAELRELELALLV--LRLEELREELEELQEELKEAEEELEELTAELQELEE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1533 LIWEREMERNDSDMQLQETLLELKRVQDVKKILSDDLAHLKERLSAVE-DRSQYTDEINRLKEELNCSLKAETNLKKEFA 1611
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLErQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1612 TLKykletstndseAKISDLLKQLDHYTKVVEMLNNekdaislAEKELYQKYEALNTECESLKGKIVSLTKIKQELESDL 1691
Cdd:TIGR02168 348 ELK-----------EELESLEAELEELEAELEELES-------RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1692 NQKTDALQ-----ISNAALSSSTQKNKEITEKIKYLEETLQLQMEQNSRNGELVKTLQAScngykdkfddEKQKNIDLYE 1766
Cdd:TIGR02168 410 ERLEDRRErlqqeIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE----------LEEAEQALDA 479
|
330 340 350
....*....|....*....|....*....|....*..
gi 6321812 1767 ENQTLQKLNTDLQLqLKNLHERLSDTTE--KNAWLSK 1801
Cdd:TIGR02168 480 AERELAQLQARLDS-LERLQENLEGFSEgvKALLKNQ 515
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
867-1046 |
3.05e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 867 NEQINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQFDDLVSEKDEISRE 946
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 947 KLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQSLIKESKLKLENEIKRLKDVINS 1026
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
170 180
....*....|....*....|
gi 6321812 1027 KEEEIKSFNDKLSSSEEDLD 1046
Cdd:COG1196 468 LLEEAALLEAALAELLEELA 487
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
888-1556 |
3.46e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 888 EEKNQKTVNELENTQDLLNQEKeNLRKNESLLNRVKTSSETLQKQ---FDDLVSEKDEISREKLEVAQNLEEAHQKIQGL 964
Cdd:PRK03918 144 DESREKVVRQILGLDDYENAYK-NLGEVIKEIKRRIERLEKFIKRtenIEELIKEKEKELEEVLREINEISSELPELREE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 965 QETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQSLIKESKLKLENEIKRLKDvinsKEEEIKSFNDKlssseED 1044
Cdd:PRK03918 223 LEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE----KVKELKELKEK-----AE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1045 LDIKLVTLEKNCNiamSRLQSLVTENSDLRSKNENFKKEKAALNNqLKNKESELLKMKEKIDNHKKELATFSKQRDDAVS 1124
Cdd:PRK03918 294 EYIKLSEFYEEYL---DELREIEKRLSRLEEEINGIEERIKELEE-KEERLEELKKKLKELEKRLEELEERHELYEEAKA 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1125 ehgkITAELKETRIQLTEYksNYQKIKEEYSNFQRETKEQEQkkrnslveslndsKIKELEARLSQeislnqyLNKRIsg 1204
Cdd:PRK03918 370 ----KKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEE-------------EISKITARIGE-------LKKEI-- 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1205 NSVETNISSTRRSTSY------SDDPLDKEDIIKKYydlqlafteiTRNLENEIEEKKNLISRLRftetrlasssfedqK 1278
Cdd:PRK03918 422 KELKKAIEELKKAKGKcpvcgrELTEEHRKELLEEY----------TAELKRIEKELKEIEEKER--------------K 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1279 IKAQMKKLKKLIQDMDPSIPLDSILNEpLDNCPDKESDINKLMLEVDYLKRQLdietrahydaenaisaLHSKFRKIQGE 1358
Cdd:PRK03918 478 LRKELRELEKVLKKESELIKLKELAEQ-LKELEEKLKKYNLEELEKKAEEYEK----------------LKEKLIKLKGE 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1359 SSLSSSDIYKLkfEASEERVKSLEDKLKTMPlRDRTNLPVGDIIKNRDSISKYEEEIRyyklenyKLQEILNESNgKLSQ 1438
Cdd:PRK03918 541 IKSLKKELEKL--EELKKKLAELEKKLDELE-EELAELLKELEELGFESVEELEERLK-------ELEPFYNEYL-ELKD 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1439 LTLDLRQSKSKEALLSEQLDRLQKDLESTERQKELLSSTIKQQKQQF-ENCMDDLQGNELRLREHIHA----LKQAEEDV 1513
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYsEEEYEELREEYLELSRELAGlraeLEELEKRR 689
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 6321812 1514 KNMASIIEKLKTQNKQKEKLIWERE-MERNDSDMQ-LQETLLELK 1556
Cdd:PRK03918 690 EEIKKTLEKLKEELEEREKAKKELEkLEKALERVEeLREKVKKYK 734
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1450-1783 |
3.99e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1450 EALLSE---QLDRLQKDLESTERQKELlsstiKQQKQqfencmddlqgnELRLREHIHALKQAEEDVKNMASIIEKLKTQ 1526
Cdd:COG1196 192 EDILGElerQLEPLERQAEKAERYREL-----KEELK------------ELEAELLLLKLRELEAELEELEAELEELEAE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1527 NKQKEKLIWEREMERNDSDMQLQETLLELKRVQDVKKILSDDLAHL-KERLSAVEDRSQYTDEINRLKEELNCSLKAETN 1605
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLeQDIARLEERRRELEERLEELEEELAELEEELEE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1606 LKKEFATLKYKLEtstnDSEAKISDLLKQLDHYTKVVEMLNNEKDAISLAEKELYQKYEALNTECESLKGKIVSLTKIKQ 1685
Cdd:COG1196 335 LEEELEELEEELE----EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1686 ELESDLNQKTDALQISNAALSSSTQKNKEITEKIKYLEETLQLQMEQNSRNGELVKTLQASCNGYKDKFDDEKQKNIDLY 1765
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
330
....*....|....*...
gi 6321812 1766 EENQTLQKLNTDLQLQLK 1783
Cdd:COG1196 491 ARLLLLLEAEADYEGFLE 508
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
925-1705 |
5.01e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 58.19 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 925 SSETLQKQFDDLVSEKDEISREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDlncdisKEQSSQS 1004
Cdd:pfam05483 72 NSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEE------EIQENKD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1005 LIKESklkleNEIKRLKDVInsKEEEIKSFNDKLSSSEEDLDIKLVTLEKNCNIamsrlQSLVTENSDLRSKNENFKKEk 1084
Cdd:pfam05483 146 LIKEN-----NATRHLCNLL--KETCARSAEKTKKYEYEREETRQVYMDLNNNI-----EKMILAFEELRVQAENARLE- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1085 aaLNNQLKNKESELLKMKEKidnHKKELATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQKIkEEYSNFQRETKEQ 1164
Cdd:pfam05483 213 --MHFKLKEDHEKIQHLEEE---YKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQL-EEKTKLQDENLKE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1165 EQKKRNSLVESLNDSKIkELEARLSQEISLNQYLNkrisgnsvetnISSTRRSTSYSDDPLDKEDIIKKYYDLQLAFTEI 1244
Cdd:pfam05483 287 LIEKKDHLTKELEDIKM-SLQRSMSTQKALEEDLQ-----------IATKTICQLTEEKEAQMEELNKAKAAHSFVVTEF 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1245 TRNLENEIEEKKNLISRLRFTETRLASSSFEDQKIKAQMKKLKKLIQDMDPSIP-LDSILNEPlDNCPDKESDINKLMLE 1323
Cdd:pfam05483 355 EATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEeLKKILAED-EKLLDEKKQFEKIAEE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1324 VDYLKRQLDIETRAHydaENAISALHSKFRKIQGESSLSSSDIYKLKFEASEERVKSLEdklktmplrdrtnlpvgdIIK 1403
Cdd:pfam05483 434 LKGKEQELIFLLQAR---EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE------------------LTA 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1404 NRDSISkyeeeiryykLENYKLQEILNESNGKLSQLTLDLRQSKSKEALLSEQLDRLQkdlESTERQKELLSSTIKQQKQ 1483
Cdd:pfam05483 493 HCDKLL----------LENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVREEFIQ 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1484 QFENCMDDLQGNELRLREHIHALKQAEEDVKNMASIIEKLKTQNKQKEKLIWEREMERNDSDMQLQETLLELKRVQDVKK 1563
Cdd:pfam05483 560 KGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVN 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1564 ILSDDLAHLKERLSAVEDRSQYTDEINRLKEE-LNCSLKAETNLKKEFATLKYKLETSTNDSEAKISDLLKQLDH-YTKV 1641
Cdd:pfam05483 640 KLELELASAKQKFEEIIDNYQKEIEDKKISEEkLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHqYDKI 719
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321812 1642 VEMLNNEKDAISLAEKELYQKYEALNTECESLKGKIVSLTKiKQELESDLNQKTDALQISNAAL 1705
Cdd:pfam05483 720 IEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKK-QLEIEKEEKEKLKMEAKENTAI 782
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1370-1919 |
5.87e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.11 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1370 KFEASEERVKSLEDKLKTMplRDRTNLPVGDIIKNRDSISKYEEEIRYYKLENYKLQEILNESNGKLSQLTLDLRQSKSK 1449
Cdd:TIGR04523 76 KIKILEQQIKDLNDKLKKN--KDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1450 EALLSEQLDRLQKDLESTERQKELLsstiKQQKQQFENCMDDLQGNELRLREHIHALKQAEEDVKNMASIIEKLKTQNKQ 1529
Cdd:TIGR04523 154 LEKLNNKYNDLKKQKEELENELNLL----EKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQ 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1530 KEKLIWEREMERNDSDMQLQETLLELKRV----QDVKKILSDDLAHLKERLSAVEDRSQYTDEINRLKEELNCSLKAETN 1605
Cdd:TIGR04523 230 LKDNIEKKQQEINEKTTEISNTQTQLNQLkdeqNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWN 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1606 --LKKEFATLKYKLETSTND---SEAKISDLLKQLDHYTKVVEMLNNEKDAISLAEKELYQKYEALNTECESLKGKIVSL 1680
Cdd:TIGR04523 310 keLKSELKNQEKKLEEIQNQisqNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1681 TKIKQELESDLNQKTDALQISNAALSSSTQKNKEITEKIKYLEETLQLQMEQNSRNGELVKTLQASCNGYKDKFDDEKQK 1760
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1761 ----NIDLYEENQTLQKLNTDLQL---QLKNLHERLSDTTEKNAWL-SKIHELENMVSLETDLKYEEMKKNKSLERAVEE 1832
Cdd:TIGR04523 470 lkvlSRSINKIKQNLEQKQKELKSkekELKKLNEEKKELEEKVKDLtKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1833 LQT--KNSQQTDVIELANKNRSEFEEATLKYEAQISDLEKYISQQELEMKKSIRDNSSYRDKVQEMAQEIEFWKSRYEST 1910
Cdd:TIGR04523 550 DDFelKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKL 629
|
....*....
gi 6321812 1911 MIGSKNIDS 1919
Cdd:TIGR04523 630 SSIIKNIKS 638
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1017-1921 |
1.08e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 57.37 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1017 IKRLKDVINSKE----EEIKSFNDKLSSSEEDLDIKLVT-----LEKNCNIAMSRLQSLVTENSDLRSKNENFKKEKAAL 1087
Cdd:TIGR01612 502 MKDFKDIIDFMElykpDEVPSKNIIGFDIDQNIKAKLYKeieagLKESYELAKNWKKLIHEIKKELEEENEDSIHLEKEI 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1088 NNqLKNKESEL-----------LKMKEKIDN--HKKELATFSKQRDDAVSEHGKITAELKETR-IQLTEYKSN----YQK 1149
Cdd:TIGR01612 582 KD-LFDKYLEIddeiiyinklkLELKEKIKNisDKNEYIKKAIDLKKIIENNNAYIDELAKISpYQVPEHLKNkdkiYST 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1150 IKEEYSNFQRETKEQEQKKRNSLVESlNDSKIKELEARLSQEISLNQYLNKRISGNSVETNISSTRRSTSYSDDPLDKED 1229
Cdd:TIGR01612 661 IKSELSKIYEDDIDALYNELSSIVKE-NAIDNTEDKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIV 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1230 IIKKYYdlqlaFTEITRNLENEIEEKKNLISRLRFTETRLASSSFEDQKIKAQMKKLKKLIQDmdpSIPLDSILNEPLDN 1309
Cdd:TIGR01612 740 EIKKHI-----HGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYND---QINIDNIKDEDAKQ 811
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1310 CPD-----------KESDINKLMLEVDYLKRQLDIETRAHYDAEN----AISALHSKF----RKIQGESSLSSSDIYKLK 1370
Cdd:TIGR01612 812 NYDkskeyiktisiKEDEIFKIINEMKFMKDDFLNKVDKFINFENnckeKIDSEHEQFaeltNKIKAEISDDKLNDYEKK 891
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1371 FEASEERVKSLEDKLKTMPLRDRTNLPVGDIIKNRDSISkyeEEIRYYKLENYKLQEILNESNGKLSQLTLDLRQSKSK- 1449
Cdd:TIGR01612 892 FNDSKSLINEINKSIEEEYQNINTLKKVDEYIKICENTK---ESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKf 968
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1450 EALLSEQLDRLQKDLesterqKELLSSTIKQQKQQFENCMDDLQGNELRLREHIhALKQAEEDVKNMASIIEKLKTQNKQ 1529
Cdd:TIGR01612 969 DNTLIDKINELDKAF------KDASLNDYEAKNNELIKYFNDLKANLGKNKENM-LYHQFDEKEKATNDIEQKIEDANKN 1041
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1530 K---EKLIWEREMERNDSDMQLQETLLELKRVQDVKKILSD--DLAHLKERLS-------AVEDRSQYTDEINRLKEEL- 1596
Cdd:TIGR01612 1042 IpniEIAIHTSIYNIIDEIEKEIGKNIELLNKEILEEAEINitNFNEIKEKLKhynfddfGKEENIKYADEINKIKDDIk 1121
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1597 NCSLKAETNLKkEFATLKYKLETSTNDSEAKISDLLKQLDH--YTKVVEMLNNEKDAISLA---EKELYQKYEALNTECE 1671
Cdd:TIGR01612 1122 NLDQKIDHHIK-ALEEIKKKSENYIDEIKAQINDLEDVADKaiSNDDPEEIEKKIENIVTKidkKKNIYDEIKKLLNEIA 1200
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1672 SLKGKIVSLTKIK-------QELESDLNQKTDALQISNAALSSSTQKNKEITEKIKYLEETLQLQMEQNSRNGELVKTLQ 1744
Cdd:TIGR01612 1201 EIEKDKTSLEEVKginlsygKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFN 1280
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1745 ASCNGYKDKF----------DDEKQKNIDLYEENQTLQKLNTDLQLQLKNLHERLSDTTEKNAWLSKIHELENMVSL--- 1811
Cdd:TIGR01612 1281 ISHDDDKDHHiiskkhdeniSDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNILKLnki 1360
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1812 --------ETDLKYEEMKKN-KSLERAVEELQTKNSQQTDVIELANKNRSEFEEATLKYEAQ-ISDLEKYISQQELEMKK 1881
Cdd:TIGR01612 1361 kkiidevkEYTKEIEENNKNiKDELDKSEKLIKKIKDDINLEECKSKIESTLDDKDIDECIKkIKELKNHILSEESNIDT 1440
|
970 980 990 1000
....*....|....*....|....*....|....*....|
gi 6321812 1882 SIRDNSSYRDKVQEMAQEIEFWKSRYESTMIGSKNIDSNN 1921
Cdd:TIGR01612 1441 YFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATND 1480
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1455-1700 |
2.01e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1455 EQLDRLQKDLESTERQKELLSstikqqkqqfencmddlqgnelRLREHIHALKQAEEDVKNMASIIEKLKTQNKQKEKLI 1534
Cdd:COG4913 235 DDLERAHEALEDAREQIELLE----------------------PIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1535 WEREMERNDSdmQLQETLLELKRVQDVKKILSDDLAHLKERLSAV--EDRSQYTDEINRLKEELNCSLKAETNLKKEFAT 1612
Cdd:COG4913 293 LEAELEELRA--ELARLEAELERLEARLDALREELDELEAQIRGNggDRLEQLEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1613 LKYKLETSTNDSEAKISDLLKQLDHYTKVVEMLNNEKDAISLAEKELYQKYEALNTECESLKGKIVS----LTKIKQELE 1688
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNiparLLALRDALA 450
|
250
....*....|..
gi 6321812 1689 SDLNQKTDALQI 1700
Cdd:COG4913 451 EALGLDEAELPF 462
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
860-1595 |
2.43e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 860 MTRTKKFNEQINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQFDDLVSE 939
Cdd:TIGR02169 356 TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 940 KDEISREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQSLIKESklklENEIKR 1019
Cdd:TIGR02169 436 INELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER----VRGGRA 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1020 LKDVINSKEEEIKSFNDKLSSSEEDLDIKLVTlekncnIAMSRLQSLVTENSDLRSKNENFKKEKAA-------LNnqlk 1092
Cdd:TIGR02169 512 VEEVLKASIQGVHGTVAQLGSVGERYATAIEV------AAGNRLNNVVVEDDAVAKEAIELLKRRKAgratflpLN---- 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1093 nkesellKMKekidnhkkelatfSKQRD-DAVSEHGKItaelkETRIQLTEYKSNYQKIkeeYSNFQRETkeqeqkkrnS 1171
Cdd:TIGR02169 582 -------KMR-------------DERRDlSILSEDGVI-----GFAVDLVEFDPKYEPA---FKYVFGDT---------L 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1172 LVESLNDSKIKELEARLsqeISLNQYLNKR---ISGNSVETNISSTRRSTSYSDDPLDKEDIIKKYYDLQLAFTEITRnL 1248
Cdd:TIGR02169 625 VVEDIEAARRLMGKYRM---VTLEGELFEKsgaMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRR-I 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1249 ENEIEEKKNLISRLrftETRLASSSFEDQKIKAQMKKLKKLIQDMDPSIpldSILNEPLDNcpdKESDINKLMLEVDYLK 1328
Cdd:TIGR02169 701 ENRLDELSQELSDA---SRKIGEIEKEIEQLEQEEEKLKERLEELEEDL---SSLEQEIEN---VKSELKELEARIEELE 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1329 RQLDietrAHYDAENAISA--LHSKFRKIQGESSlsssdiyKLKFEAS--EERVKSLEDKLKTMP-----LRDRTNLPVG 1399
Cdd:TIGR02169 772 EDLH----KLEEALNDLEArlSHSRIPEIQAELS-------KLEEEVSriEARLREIEQKLNRLTlekeyLEKEIQELQE 840
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1400 DIIKNRDSISKYEEEIRYYKLENYKLQEILNESNGKLSQLtldlrqsKSKEALLSEQLDRLQKDLESTERQKELLSSTIK 1479
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL-------ESRLGDLKKERDELEAQLRELERKIEELEAQIE 913
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1480 QQKQQFENCMDDLQGNELRLREHIHALKQAEEDVKNMASiIEKLKtqnKQKEKLiwEREMER-NDSDMQLQEtllELKRV 1558
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQ---AELQRV--EEEIRAlEPVNMLAIQ---EYEEV 984
|
730 740 750
....*....|....*....|....*....|....*..
gi 6321812 1559 QDVKKILSDDLAHLKERLSAVEDRsqyTDEINRLKEE 1595
Cdd:TIGR02169 985 LKRLDELKEKRAKLEEERKAILER---IEEYEKKKRE 1018
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
922-1157 |
3.25e-07 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 55.32 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 922 VKTSSETLQK----QFDDLvseKDEISREKLEvaqnleEAHQKIQGLQETIrereATLEKLHSKNNELIKQISDLncdis 997
Cdd:PRK05771 18 KDEVLEALHElgvvHIEDL---KEELSNERLR------KLRSLLTKLSEAL----DKLRSYLPKLNPLREEKKKV----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 998 KEQSSQSLIKESK---LKLENEIKRLKDVINSKEEEIKSFNDKLSSSE--EDLDIKLVTL--EKNCNIAMSRLQSLVTEN 1070
Cdd:PRK05771 80 SVKSLEELIKDVEeelEKIEKEIKELEEEISELENEIKELEQEIERLEpwGNFDLDLSLLlgFKYVSVFVGTVPEDKLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1071 SDLRSKNENFKKEK----------AALNNQLKNKESELLKM-------------KEKIDNHKKELATFSKQRDDAVSEHG 1127
Cdd:PRK05771 160 LKLESDVENVEYIStdkgyvyvvvVVLKELSDEVEEELKKLgferleleeegtpSELIREIKEELEEIEKERESLLEELK 239
|
250 260 270
....*....|....*....|....*....|
gi 6321812 1128 KITAELKETRIQLTEYKSNYQKIKEEYSNF 1157
Cdd:PRK05771 240 ELAKKYLEELLALYEYLEIELERAEALSKF 269
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
862-1187 |
5.45e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.14 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 862 RTKKFNEQINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQFDDLVSEKD 941
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 942 EISREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDIsKEQSSQSLIKESKLKLENEIKRLK 1021
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL-QALSEAEAEQALDELLKEANRNAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1022 DVINSKEEEIKSFNDKLSSSEEDLDIKLVTLEKNCNIAMSRLQSLVTENSDLRSKNENFKKEKAALNNQLKNKESELLKM 1101
Cdd:COG4372 198 KEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1102 KEKIDNHKKELATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQKIKEEYSNFQRETKEQEQKKRNSLVESLNDSKI 1181
Cdd:COG4372 278 LEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLE 357
|
....*.
gi 6321812 1182 KELEAR 1187
Cdd:COG4372 358 LLSKGA 363
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
870-1160 |
6.01e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.05 E-value: 6.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 870 INKLKNDLQEMESKKKFLEEKNQKTVNELENTQdlLNQEKEN----LRKNESLLNRVKTSSETLQKQFDDLVSEKDEISR 945
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQAAKLQGSDLDRTVQQ--VNQEKQEkqheLDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKS 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 946 EKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQSLIKESKLKLENEIKRLKDVIN 1025
Cdd:TIGR00606 872 EKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVK 951
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1026 SKEEEIKSFNDKLSSSEEDLDIKLVTLEKNCNIAMSRLQSLVTE-NSDLRSKNENF---KKEKAALNNQLKnkeseLLKM 1101
Cdd:TIGR00606 952 NIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKiNEDMRLMRQDIdtqKIQERWLQDNLT-----LRKR 1026
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 6321812 1102 KEKIDNHKKELATFSKQRDDavsehgkitaelketrIQLTEYKSNYQKIKEEYSNFQRE 1160
Cdd:TIGR00606 1027 ENELKEVEEELKQHLKEMGQ----------------MQVLQMKQEHQKLEENIDLIKRN 1069
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1435-1651 |
6.34e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1435 KLSQLTLDLRQSKSKEALLSEQLDRLQKDLESTERQKELLSSTIKQQKQQfencMDDLQGNELRLREhihALKQAEEDVK 1514
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE----IDKLQAEIAEAEA---EIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1515 NMAsiieklktqnkqkekliweREMERNDSDMQLQETLLE-------LKRVQDVKKILSDDLAHLKERLSAVEdrsqytd 1587
Cdd:COG3883 90 ERA-------------------RALYRSGGSVSYLDVLLGsesfsdfLDRLSALSKIADADADLLEELKADKA------- 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321812 1588 EINRLKEELNCSLKAETNLKKEFATLKYKLETSTNDSEAKISDLLKQLDHYTKVVEMLNNEKDA 1651
Cdd:COG3883 144 ELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1033-1442 |
6.42e-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: 54.69 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1033 SFNDKLSSSEEDLDIKLVTLEKNCNIAMSRLQSLVTENSDLRSKNENFKKEKAALNNQLKNKESELLKMKEKIDNHKKEL 1112
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1113 ATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQKIKEEYSNFQRETKEQEQKKRNSLVESLnDSKIKELEARLSQEI 1192
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRI-EARLREIEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1193 SLNQYLNKRISGnsvetnisstrrSTSYSDDPLDKEDIIKKYYDLQLAFTEitrNLENEIEEKKNlisRLRFTETRLASS 1272
Cdd:TIGR02169 826 LEKEYLEKEIQE------------LQEQRIDLKEQIKSIEKEIENLNGKKE---ELEEELEELEA---ALRDLESRLGDL 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1273 SFEDQKIKAQMKKLKKLIQDMDPSI----PLDSILNEPLDNCPDKESDINKLMLE-VDYLKRQLDIET-RAHYDA-ENAI 1345
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEAQIekkrKRLSELKAKLEALEEELSEIEDPKGEdEEIPEEELSLEDvQAELQRvEEEI 967
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1346 SALHS-KFRKIQgesslsssdiyklKFEASEERVKSLEDKLKTMpLRDRTNLpvgdiiknRDSISKYEEEIRYYKLE--- 1421
Cdd:TIGR02169 968 RALEPvNMLAIQ-------------EYEEVLKRLDELKEKRAKL-EEERKAI--------LERIEEYEKKKREVFMEafe 1025
|
410 420
....*....|....*....|...
gi 6321812 1422 --NYKLQEILNESNGKLSQLTLD 1442
Cdd:TIGR02169 1026 aiNENFNEIFAELSGGTGELILE 1048
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1607-1901 |
7.51e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 7.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1607 KKEfaTLKyKLEtSTNDSEAKISDLL----KQLDH----------YTKVVEMLNN-EKDAISLAEKELYQKYEALNTECE 1671
Cdd:COG1196 174 KEE--AER-KLE-ATEENLERLEDILgeleRQLEPlerqaekaerYRELKEELKElEAELLLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1672 SLKGKIVSLTKIKQELESDLNQKTDALQISNAALSSSTQKNKEITEKIKYLEETLQLQMEQNSRNGELVKTLQASCNGYK 1751
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1752 DKFDDEKQKNIDLYEENQTLQKLNTDLQLQLKNLHERLSD-TTEKNAWLSKIHELENMVSLETDLKYEEMKKNKSLERAV 1830
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEaEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321812 1831 EELQTKNSQQTDVIELANKNRSEFEEATLKYEAQISDLEKYISQQELEMKKSIRDNSSYRDKVQEMAQEIE 1901
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1071-1789 |
8.88e-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: 53.96 E-value: 8.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1071 SDLRSKNENFKKEKAALNNQLKNKESELLKMKEKIDNHKKELATF-------SKQRDDAVSEHGKITAELKETRIQLTEY 1143
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELqfenekvSLKLEEEIQENKDLIKENNATRHLCNLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1144 KSNYQKIKEEYSNFQRETKEQEQ------KKRNSLVESLNDSKIKELEARLSQEISLNQYLNKrisgnsvetnISSTRRS 1217
Cdd:pfam05483 161 KETCARSAEKTKKYEYEREETRQvymdlnNNIEKMILAFEELRVQAENARLEMHFKLKEDHEK----------IQHLEEE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1218 TsysddpldKEDIIKKYYDLQLAFTEITrnleneieEKKNLISRLRF--TETRLASSSFEdQKIKAQMKKLKKLIQDMDP 1295
Cdd:pfam05483 231 Y--------KKEINDKEKQVSLLLIQIT--------EKENKMKDLTFllEESRDKANQLE-EKTKLQDENLKELIEKKDH 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1296 sipldsiLNEPLDncpDKESDINKLMLEVDYLKRQLDIETRAHYDAENAISALHSKFRKIQGESSLSSSDIyklkfeasE 1375
Cdd:pfam05483 294 -------LTKELE---DIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEF--------E 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1376 ERVKSLEDKLKTMPLRdrtnlpvgdIIKNRDSISKYEEEIRYYKLENYKLQEILNESNGKLSQLTLDLRQsksKEALLSE 1455
Cdd:pfam05483 356 ATTCSLEELLRTEQQR---------LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE---DEKLLDE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1456 --QLDRLQKDLESTERQKELLSSTIKQQKQQFENCMDDLQGNELrlrehiHALKQaeedVKNMASIIEKLKTQNKQKEKL 1533
Cdd:pfam05483 424 kkQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEE------HYLKE----VEDLKTELEKEKLKNIELTAH 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1534 IWEREMERNDSDMQLQETLLELKRVQ-DVKKILSDDLAHLKERLSAVEDRSQYTDEINRLKEEL-------NCSLKAETN 1605
Cdd:pfam05483 494 CDKLLLENKELTQEASDMTLELKKHQeDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFiqkgdevKCKLDKSEE 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1606 LKKEFATLKYKLETSTNDSEAKISDLLKQLDHYTKVVEMLNNEKDAISLAEKELYQKYEALNTECESLKGKIVSLTKIKQ 1685
Cdd:pfam05483 574 NARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFE 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1686 ELESDLNQKTDALQISNAALSSSTQKNKEITEKIKYLEETLQLQMEQnsRNGELVKTLQASCNGYkDKFDDEKQKNIDLY 1765
Cdd:pfam05483 654 EIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQH--KIAEMVALMEKHKHQY-DKIIEERDSELGLY 730
|
730 740
....*....|....*....|....*
gi 6321812 1766 EENQTLQ-KLNTDLQLQLKNLHERL 1789
Cdd:pfam05483 731 KNKEQEQsSAKAALEIELSNIKAEL 755
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1122-1926 |
9.65e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.21 E-value: 9.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1122 AVSEHGKITAELKETRIQLTEYKSNYQKIKEEYSNFQRETKEQEQKKrnslvesLNDSKIKELEARLSQEISLNQYLNKR 1201
Cdd:pfam02463 163 AGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKA-------LEYYQLKEKLELEEEYLLYLDYLKLN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1202 ISgnsvetnisstrRSTSYSDDPLDKEDIIKKYYDLQLAFTEITRNLENEIEEKKNLISRLRFTETRLASSSFEDQKIKA 1281
Cdd:pfam02463 236 EE------------RIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1282 QMKKLKKLIQDmdpsipldsILNEPLDNCPDKESDINKLMLEVDYLKRQLDIETRAHYDAENAISALhskfRKIQGESSL 1361
Cdd:pfam02463 304 KLERRKVDDEE---------KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL----EKLQEKLEQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1362 SSSDIYKLKFEASEERVKSLEDKLKTMPLRDRTNLPVGDIIKNRDSI-SKYEEEIRYYKLENYKLQEILNESNGKLSQLT 1440
Cdd:pfam02463 371 LEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLeDLLKEEKKEELEILEEEEESIELKQGKLTEEK 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1441 LDLRQSKSKEALLSEQLDRLQKDLESTerQKELLSSTIKQQKQQFENCMDDLQGNELRLREHIHALKQAEEDVKNMASII 1520
Cdd:pfam02463 451 EELEKQELKLLKDELELKKSEDLLKET--QLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAH 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1521 EKLKTQNKQKEKLIWEREMERNDSDMQLQETLLELKRVQDVKKILSDDLAHLKERLSAVE--DRSQYTDEINRLKEELNc 1598
Cdd:pfam02463 529 GRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKlpLKSIAVLEIDPILNLAQ- 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1599 slkaetnlkKEFATLKYKLETSTNDSEAKISDLLKQLDHYTKVVEMLNNEKDAISLAEKELYQKYEALNTECESLKGKIV 1678
Cdd:pfam02463 608 ---------LDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEI 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1679 SLTKIKQELESDLNQKTDALQ-ISNAALSSSTQKNKEITEKIKYLEETLQLQMEQNSRNGELVKTLQASCNGYKDKFDDE 1757
Cdd:pfam02463 679 QELQEKAESELAKEEILRRQLeIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1758 KQKNIDLYEENQTLQKLNTDLQLQLKNLHERLSDTTEKNAWLSKIHELENMVSLETDLKYEEMKK-----NKSLERAVEE 1832
Cdd:pfam02463 759 KEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLieqeeKIKEEELEEL 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1833 LQTKNSQQTDVIELANKNRSEFEEATLKYEAQISDLEKYISQQELEMKKsirdNSSYRDKVQEMAQEIEFWKSRYESTMI 1912
Cdd:pfam02463 839 ALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDE----LESKEEKEKEEKKELEEESQKLNLLEE 914
|
810
....*....|....
gi 6321812 1913 GSKNIDSNNAQSKI 1926
Cdd:pfam02463 915 KENEIEERIKEEAE 928
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
894-1169 |
9.84e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.61 E-value: 9.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 894 TVNELENTQDLLNQEKENLRKnesLLNRVKTSSETLQKQFDDLVSEKDEISREKLEVAQNLEEAHQKIQGLQETIREREA 973
Cdd:COG1340 2 KTDELSSSLEELEEKIEELRE---EIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 974 TLEKLHSKNNELIKQISDLNCDISKEQSSQSLIKESKLKLENEIKRLKDVINSKEEEIKSFnDKLSSSEEDLDIKLVTLE 1053
Cdd:COG1340 79 ERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELV-EKIKELEKELEKAKKALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1054 KNcniamSRLQSLVTENSDLRSKNENFKKEKAALNNQLKNKESELLKMKEKIDNHKKELATFSKQRDDAVSEHGKITAEL 1133
Cdd:COG1340 158 KN-----EKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEI 232
|
250 260 270
....*....|....*....|....*....|....*.
gi 6321812 1134 KETRIQLTEYKSNYQKIKEEYSNFQRETKEQEQKKR 1169
Cdd:COG1340 233 IELQKELRELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
864-1184 |
1.14e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 864 KKFNEQINKLKNDLQEMESKKKflEEKNQKTVNELENTQDLlNQEKENLRKNESLLNRVKTSSETLQKQFDDLVSEKDEI 943
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKK--AEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK 1546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 944 SREKLEVAQNLEEAHQKIQGLQETIRE--------REATLEKLHSKNNELIKQISDLNCDISKEQ---SSQSLIKESKLK 1012
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEEAKKAEedknmalrKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakkAEEAKIKAEELK 1626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1013 LENEIKRLKDVINSKEEEIKSFNDKLSSSEEDLDIKLVTLEKNCNIAMSRLQSLVTENSDLRSKNENFKK--EKAALNNQ 1090
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKeaEEAKKAEE 1706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1091 LKNKESELLKMKEKIDNHKKELATFSKQRDDAVSEHGKITAELK---ETRIQLTEYKSNYQKIKEEYSNFQRETKEQEQK 1167
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKkdeEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
330
....*....|....*..
gi 6321812 1168 KRNSLVESLNDSKIKEL 1184
Cdd:PTZ00121 1787 EEDEKRRMEVDKKIKDI 1803
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1401-1907 |
1.55e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1401 IIKNRDSISKYEEEI-RYYKLENY--KLQEILNESNGKLSQLTLDLRQSKSKEALLSEQLDRLQ------KDLESTERQK 1471
Cdd:PRK03918 140 ILESDESREKVVRQIlGLDDYENAykNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEevlreiNEISSELPEL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1472 ELLSSTIKQQKQQFENCMDDLQGNELRLREHIHALKQAEEDVKNMASIIEKLKTQNKQKEKLIweREMERNDSDMQLQET 1551
Cdd:PRK03918 220 REELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV--KELKELKEKAEEYIK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1552 LLELKR-VQDVKKILSDDLAHLKERLSAVEDRsqyTDEINRLKEELNCSLKAETNLKKEFATLKYKLETSTndseaKISD 1630
Cdd:PRK03918 298 LSEFYEeYLDELREIEKRLSRLEEEINGIEER---IKELEEKEERLEELKKKLKELEKRLEELEERHELYE-----EAKA 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1631 LLKQLDHYTK-----VVEMLNNEKDAISLAEKELYQKYEALNTECESLKGKIVSLTKIKQELES------------DLNQ 1693
Cdd:PRK03918 370 KKEELERLKKrltglTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelTEEH 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1694 KTDALQISNAALSSSTQKNKEITEKIKYLE------ETLQLQMEQNSRNGELVKTLQASCNGYKdKFDDEKQKniDLYEE 1767
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELKEIEEKERKLRkelrelEKVLKKESELIKLKELAEQLKELEEKLK-KYNLEELE--KKAEE 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1768 NQTLQKLNTDLQLQLKNLHERLSdtteknawlsKIHELENMVSLETDLKYEEMKKNKSLERAVEELQTKNsqqtdvIELA 1847
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELE----------KLEELKKKLAELEKKLDELEEELAELLKELEELGFES------VEEL 590
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321812 1848 NKNRSEFEEATLKY------EAQISDLEKYISQQELEMKKSIRDNSSYRDKVQEMAQEIEFWKSRY 1907
Cdd:PRK03918 591 EERLKELEPFYNEYlelkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
910-1137 |
1.59e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 910 ENLRKNESLLNRVKTSSETLQKQFDDLVSEKDEISREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQI 989
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 990 SDLNCDISKE-QSSQSLIKESKLKLENEIKRLKDVINSkEEEIKSFNDKLSSSEEDLDIKLVTLEKNcniamsrLQSLVT 1068
Cdd:COG4942 100 EAQKEELAELlRALYRLGRQPPLALLLSPEDFLDAVRR-LQYLKYLAPARREQAEELRADLAELAAL-------RAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321812 1069 ENSDLRSKNENFKKEKAALNNQLKNKESELLKMKEKIDNHKKELATFSKQRDDAVSEHGKITAELKETR 1137
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1327-1876 |
1.60e-06 |
|
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: 53.30 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1327 LKRQLDIETRAhyDAENAISALHSKFRKIQGESSlSSSDIYKLKFEASEERVKSLEDKLKTmpLRDRTNlpvGDIIKNRD 1406
Cdd:pfam12128 244 TKLQQEFNTLE--SAELRLSHLHFGYKSDETLIA-SRQEERQETSAELNQLLRTLDDQWKE--KRDELN---GELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1407 SISKYEEEIryyklenyklqEILNESNGKLSQLTLDlrqsksKEALLSEQLDRLQKDLESTERQKELLSSTIKQQKQQF- 1485
Cdd:pfam12128 316 AVAKDRSEL-----------EALEDQHGAFLDADIE------TAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYn 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1486 -------ENCMDDLQGNELRL---REHIHALKQAEEDVknmasiIEKLKTQ-NKQKEKLIwereMERNDSDMQLQETLLE 1554
Cdd:pfam12128 379 rrrskikEQNNRDIAGIKDKLakiREARDRQLAVAEDD------LQALESElREQLEAGK----LEFNEEEYRLKSRLGE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1555 LKRVQDVKKILSDDLahlkerlsavEDRSQYTDEINRLKEELNCSLKAETNLKKEFATLKYKLEtstndseakisdllKQ 1634
Cdd:pfam12128 449 LKLRLNQATATPELL----------LQLENFDERIERAREEQEAANAEVERLQSELRQARKRRD--------------QA 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1635 LDHYTKVVEMLNNEKDAISLAEKELYQK----YEALNTECESLKGKIVSLTKIKQELESDLNQKTDALQISNAA------ 1704
Cdd:pfam12128 505 SEALRQASRRLEERQSALDELELQLFPQagtlLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELnlygvk 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1705 -------LSSSTQKNKEITEKIKYLEETLQLQMEQNSRNGELVKTLQASCNGYKDKFDDEKQ--KNID-----LYEENQT 1770
Cdd:pfam12128 585 ldlkridVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTalKNARldlrrLFDEKQS 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1771 LQ-KLNTDLQLQLKNLHERLSDTT--------EKNAWLSKIHE--LEN-MVSLETDLKYEEMKKNK--SLERAVEELQTK 1836
Cdd:pfam12128 665 EKdKKNKALAERKDSANERLNSLEaqlkqldkKHQAWLEEQKEqkREArTEKQAYWQVVEGALDAQlaLLKAAIAARRSG 744
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 6321812 1837 NSQQTDVIELANKN----RSEFEEATLKYEAQISDLEKYISQQE 1876
Cdd:pfam12128 745 AKAELKALETWYKRdlasLGVDPDVIAKLKREIRTLERKIERIA 788
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
916-1484 |
1.61e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.58 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 916 ESLLNRVKTSSETLQKQFDDLVSEKdeISREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCD 995
Cdd:pfam15921 248 EALKSESQNKIELLLQQHQDRIEQL--ISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLEST 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 996 ISKEQSSqslIKESKLKLENEIKRLKD---VINSKEEEIKSFNDKLSSSEEDLDIKLVTLEKNCNIAMSRLQSLVTENSD 1072
Cdd:pfam15921 326 VSQLRSE---LREAKRMYEDKIEELEKqlvLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKR 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1073 LRSKN-------ENFKKEKAALNNQLKNKESELLKMKEKIDNHKKELATFSKQRDDAVSEHGKITAELKETRIQLteyks 1145
Cdd:pfam15921 403 LWDRDtgnsitiDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEML----- 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1146 nyQKIKEEYSNfQRETKEQEQKKRNSLVESLND---------SKIKELEARLSQEISLNQYL-NKRISGNSVETNISSTR 1215
Cdd:pfam15921 478 --RKVVEELTA-KKMTLESSERTVSDLTASLQEkeraieatnAEITKLRSRVDLKLQELQHLkNEGDHLRNVQTECEALK 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1216 RSTSYSDDPLD--------KEDIIKKYYDLQLAFTEITRNLENEIEEKknlisRLRFTETRLasssFEDQKiKAQMKKLK 1287
Cdd:pfam15921 555 LQMAEKDKVIEilrqqienMTQLVGQHGRTAGAMQVEKAQLEKEINDR-----RLELQEFKI----LKDKK-DAKIRELE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1288 KLIQDMD-PSIPLDSILNEPLDNCPDKESDINKLMLEVDYLKRQLDIETRAHydaenaiSALHSKFRKIQGESSLSSSDI 1366
Cdd:pfam15921 625 ARVSDLElEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDY-------EVLKRNFRNKSEEMETTTNKL 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1367 yKLKFEASEERVKSLEDKLKTMPLRDRTNLPVG-----DIIKNRDSISKYEEEIRYYK---LENYKLQEILNESNGKLSQ 1438
Cdd:pfam15921 698 -KMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAmgmqkQITAKRGQIDALQSKIQFLEeamTNANKEKHFLKEEKNKLSQ 776
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 6321812 1439 -----------LTLDLRQSKSKEALLSEQLDRLQKDLESTERQKELLSSTIKQQKQQ 1484
Cdd:pfam15921 777 elstvateknkMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQE 833
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
879-1039 |
1.64e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.86 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 879 EMESKKKFLE--EKNQKTVNELENTqdlLNQEKENLRKNEsllNRVKTSSETLQKQFDDLvsekdeisrEKLEvaQNLEE 956
Cdd:PRK12704 52 EAIKKEALLEakEEIHKLRNEFEKE---LRERRNELQKLE---KRLLQKEENLDRKLELL---------EKRE--EELEK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 957 AHQKIQGLQETIREREATLEKLHSKNNELIKQISDLncdiSKEQSSQSLIKESKLKLENEIKRLkdvINSKEEEIKSFND 1036
Cdd:PRK12704 115 KEKELEQKQQELEKKEEELEELIEEQLQELERISGL----TAEEAKEILLEKVEEEARHEAAVL---IKEIEEEAKEEAD 187
|
...
gi 6321812 1037 KLS 1039
Cdd:PRK12704 188 KKA 190
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
868-1808 |
1.82e-06 |
|
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: 53.26 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 868 EQINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQFDDLVSEKDEISREK 947
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 948 LEVAQNLEEAHQKIQGLQETIREREATLEKLH---------------------SKNNELIKQ------------------ 988
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQlekvtteakikkleedillleDQNSKLSKErklleeriseftsnlaee 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 989 -----------------ISDLNCDISKEQSSQSLIKESKLKLENEIKRLKDVINSKEEEIKSFNDKLSSSEEDLDIKLVT 1051
Cdd:pfam01576 172 eekakslsklknkheamISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALAR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1052 LEKNC---NIAMSRLQSLVTENSDL----------RSKNENFKK----EKAALNNQLKN--------------KESELLK 1100
Cdd:pfam01576 252 LEEETaqkNNALKKIRELEAQISELqedleseraaRNKAEKQRRdlgeELEALKTELEDtldttaaqqelrskREQEVTE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1101 MKEKIDNHKKelaTFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQKIK----EEYSNFQRETK-------EQEQKKR 1169
Cdd:pfam01576 332 LKKALEEETR---SHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKqaleSENAELQAELRtlqqakqDSEHKRK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1170 NSlveslnDSKIKELEARLSQEISLNQYLNKRISG------------NSVETNISSTRRSTSYSDDPL-DKEDIIKKYYD 1236
Cdd:pfam01576 409 KL------EGQLQELQARLSESERQRAELAEKLSKlqselesvssllNEAEGKNIKLSKDVSSLESQLqDTQELLQEETR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1237 LQLAFTEITRNLEneiEEKKNLISRLRFTETRLASSSFEDQKIKAQMKKLKKLIQDMDPSIPLdsilnepldncpdKESD 1316
Cdd:pfam01576 483 QKLNLSTRLRQLE---DERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA-------------LEEG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1317 INKLMLEVDYLKRQLDiETRAHYDaenaisALHSKFRKIQGESSLSSSDIYKLKfeaseERVKSLEDKLKTMP--LRDRT 1394
Cdd:pfam01576 547 KKRLQRELEALTQQLE-EKAAAYD------KLEKTKNRLQQELDDLLVDLDHQR-----QLVSNLEKKQKKFDqmLAEEK 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1395 NLPVgdiiKNRDSISKYEEEIRYYKLENYKLQEILNESNGKLSQLTLDLRQSKSK-EALLSEQlDRLQKDLESTERQKEL 1473
Cdd:pfam01576 615 AISA----RYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEmEDLVSSK-DDVGKNVHELERSKRA 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1474 LSSTIKQQKQQFENCMDDLQGNE---LRLREHIHALK-QAEEDVKNMASIIEKLKTQ-NKQKEKLIWEREMERND----- 1543
Cdd:pfam01576 690 LEQQVEEMKTQLEELEDELQATEdakLRLEVNMQALKaQFERDLQARDEQGEEKRRQlVKQVRELEAELEDERKQraqav 769
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1544 ----------SDMQLQ---------ETLLELKRVQ-----------DVK-----------------KILSDDLAHLKERL 1576
Cdd:pfam01576 770 aakkkleldlKELEAQidaankgreEAVKQLKKLQaqmkdlqreleEARasrdeilaqskesekklKNLEAELLQLQEDL 849
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1577 SAVED-RSQYTDEINRLKEELNCSLKAETNLKKEfatlKYKLetstndsEAKISDLLKQLDHYTKVVEMLNNEKdaisla 1655
Cdd:pfam01576 850 AASERaRRQAQQERDELADEIASGASGKSALQDE----KRRL-------EARIAQLEEELEEEQSNTELLNDRL------ 912
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1656 eKELYQKYEALNTECESLKGKIVSLTKIKQELESDLNQKTDALQISNAALSSSTQKNKEITE-KIKYLEETLQLQMEQNS 1734
Cdd:pfam01576 913 -RKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEaKIAQLEEQLEQESRERQ 991
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321812 1735 RNGELVKTLQASCNGYKDKFDDEKqKNIDLYEENqtLQKLNTDLQLQLKNLHERLSDTTEKNAWLSKIH-ELENM 1808
Cdd:pfam01576 992 AANKLVRRTEKKLKEVLLQVEDER-RHADQYKDQ--AEKGNSRMKQLKRQLEEAEEEASRANAARRKLQrELDDA 1063
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1370-1881 |
1.89e-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: 53.10 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1370 KFEASEERVKSLEDKLKTMPLRDRTNLPvgDIIKNRDSISKYEEEIRYYKLENYKLQEILNESNGKLSQLTLDLRQSKSK 1449
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDK--NLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1450 EALLSEQLDRLQKDLESTERQKELLSSTIKQQKQQFENCMDDLQgnelRLREHIHALKQAEEDVKNMASIIEKLKTQNKQ 1529
Cdd:TIGR04523 112 IKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELE----KLNNKYNDLKKQKEELENELNLLEKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1530 KEKLIweremerNDSDMQLQETLLELKRVQDVKKILSDDLAHLKERLSAVEDR-SQYTDEINRLKEELNCSLKAETNLKK 1608
Cdd:TIGR04523 188 NIDKI-------KNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNiEKKQQEINEKTTEISNTQTQLNQLKD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1609 EFATLKYKLETSTNDSE---AKISDLLKQLDHYTKVVEMLNNEKDAISLAEkelyqkyeaLNTECESLKGKIVSLTKIKQ 1685
Cdd:TIGR04523 261 EQNKIKKQLSEKQKELEqnnKKIKELEKQLNQLKSEISDLNNQKEQDWNKE---------LKSELKNQEKKLEEIQNQIS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1686 ELESDLNQKTDALQISNAALSSSTQKNKEITEKIKYLEETLQLQMEQNSRNGELVKTLQASCNGYKDKFDDEKQKNIDLY 1765
Cdd:TIGR04523 332 QNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKD 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1766 EENQTLQKLNTDLQLQLKNLHERLSDTTEKNAWL-SKIHELENMVSLETDLKYEEMKKNKSLERAVEELQTKNSQQTDVI 1844
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLtNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
490 500 510
....*....|....*....|....*....|....*..
gi 6321812 1845 ELANKNRSEFEEATLKYEAQISDLEKYISQQELEMKK 1881
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK 528
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1313-1614 |
1.97e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1313 KESDINKLMLEVDYLKRQLDIETRAHYDAENAISALHSKFRKIQGESSLSSSDIYKLKFEASEERvksledklktmplrd 1392
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ--------------- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1393 rtnlpvGDIIKNRDSISKYEEEIRYyklenykLQEILNESNGKLSQLTLDLRQSKSKEALLSEQLDRLQKDLESTERQKE 1472
Cdd:COG1196 288 ------AEEYELLAELARLEQDIAR-------LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1473 LLSSTIKQQKQQFENCMDDLQGNELRLREHIHALKQAEEDVKNMASIIEKLKTQNKQKEKLIWEREMERNDSDMQLQETL 1552
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321812 1553 LELKRVQD-VKKILSDDLAHLKERLSAVEDRSQYTDEINRLKEELNCSLKAETNLKKEFATLK 1614
Cdd:COG1196 435 EEEEEEEEaLEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1409-1899 |
2.17e-06 |
|
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: 52.87 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1409 SKYEEEIRYYKLENYKLQEILNESNGKLSQLTLDLRQSKSKEALLSEQLDRLQKDLESTERQKELLSStikqQKQQFENC 1488
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAA----RKQELEEI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1489 MDDLqgnELRLREHIHALKQAEEDVKNMASIIEKLKT---------QNKQKEKLIWEREMERNDSDMQLQETllELKRVQ 1559
Cdd:pfam01576 77 LHEL---ESRLEEEEERSQQLQNEKKKMQQHIQDLEEqldeeeaarQKLQLEKVTTEAKIKKLEEDILLLED--QNSKLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1560 DVKKILSDDLAHLKERLSAVEDRSQYTDEINRLKE----ELNCSLKAETNLKKEFATLKYKLETSTNDSEAKISDLLKQL 1635
Cdd:pfam01576 152 KERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEamisDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1636 dhytkvvemlnnEKDAISLAEKElyQKYEALNTECESLKGKIVSLTKIKQELESDLNQKTDALQISNAALSSSTQKNKEI 1715
Cdd:pfam01576 232 ------------AELRAQLAKKE--EELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1716 TEKIKY----LEETL-------QLQMEQNSRNGELVKTLQASCNGYKDKFDDEKQKNidlyeeNQTLQKLNTDLQlQLKN 1784
Cdd:pfam01576 298 GEELEAlkteLEDTLdttaaqqELRSKREQEVTELKKALEEETRSHEAQLQEMRQKH------TQALEELTEQLE-QAKR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1785 LHERLSDTteKNAWLSKIHELENMVSLETDLKYEEMKKNKSLERAVEELQTKNSQqtdvielANKNRSEFEEATLKYEAQ 1864
Cdd:pfam01576 371 NKANLEKA--KQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE-------SERQRAELAEKLSKLQSE 441
|
490 500 510
....*....|....*....|....*....|....*...
gi 6321812 1865 ISDLEKYISQQELEMKKSIRDNSSYRDK---VQEMAQE 1899
Cdd:pfam01576 442 LESVSSLLNEAEGKNIKLSKDVSSLESQlqdTQELLQE 479
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1372-1872 |
2.18e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1372 EASEERVKSLEDKLKTM-PLRDRTNlpvgDIIKNRDSISKYEEEIRYYKLenYKLQEILNESNGKLSQLTLDLRQSKSKE 1450
Cdd:COG4913 238 ERAHEALEDAREQIELLePIRELAE----RYAAARERLAELEYLRAALRL--WFAQRRLELLEAELEELRAELARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1451 ALLSEQLDRLQKDLESTERQ--------KELLSSTIKQQKQQfencMDDLQGNELRLREHIHALKQAEED--------VK 1514
Cdd:COG4913 312 ERLEARLDALREELDELEAQirgnggdrLEQLEREIERLERE----LEERERRRARLEALLAALGLPLPAsaeefaalRA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1515 NMASIIEKLKTQNKQKEKLIWEREMERNDSDMQLQETLLELKRVQDVKKILSDDLAHLKERLSA---------------- 1578
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEalgldeaelpfvgeli 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1579 -------------------------VEDR--SQYTDEINRLK-------EELNCSLKAETNLKKEFATLKYKLETSTNDS 1624
Cdd:COG4913 468 evrpeeerwrgaiervlggfaltllVPPEhyAAALRWVNRLHlrgrlvyERVRTGLPDPERPRLDPDSLAGKLDFKPHPF 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1625 EAKISDLLKQLDHYTKV--VEMLNNEKDAISLA--------------EKELYQKY----------EALNTECESLKGKIV 1678
Cdd:COG4913 548 RAWLEAELGRRFDYVCVdsPEELRRHPRAITRAgqvkgngtrhekddRRRIRSRYvlgfdnraklAALEAELAELEEELA 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1679 SLTKIKQELESDLNQKTDALQISN--AALSSSTQKNKEITEKIKYLEETLQlQMEQNsrNGELvKTLQASCNGYKDKFDD 1756
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELE-RLDAS--SDDL-AALEEQLEELEAELEE 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1757 EKQKNIDLYEENQTLQKLNTDLQLQLKNLHERLSDTTEKNAWLSKIhELENMVS-LETDLKYEEMKKNksLERAVEELQT 1835
Cdd:COG4913 704 LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA-LLEERFAaALGDAVERELREN--LEERIDALRA 780
|
570 580 590
....*....|....*....|....*....|....*...
gi 6321812 1836 K-NSQQTDVIELANKNRSEFEEATLKYEAQISDLEKYI 1872
Cdd:COG4913 781 RlNRAEEELERAMRAFNREWPAETADLDADLESLPEYL 818
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
877-1188 |
2.21e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.59 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 877 LQEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQF-------DDLVSEKDEISREKLE 949
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYkelsassEELSEEKDALLAQRAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 950 VAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISD---------------------LNCDISKEQSSQSLIKE 1008
Cdd:pfam07888 127 HEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEeeaerkqlqaklqqteeelrsLSKEFQELRNSLAQRDT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1009 SKLKLENEIKRLKDVINS---KEEEIKSFNDKLSSSEEdldiKLVTLEKNCNIAMSRLQSLVTENSDLRSKNENFKKEKA 1085
Cdd:pfam07888 207 QVLQLQDTITTLTQKLTTahrKEAENEALLEELRSLQE----RLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1086 ALNNQLKN-------------KESELL-----KMKEKIDNHKKELATFSKQRDDAVSEHGKITAELKE----TRIQLTEY 1143
Cdd:pfam07888 283 QLTLQLADaslalregrarwaQERETLqqsaeADKDRIEKLSAELQRLEERLQEERMEREKLEVELGRekdcNRVQLSES 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 6321812 1144 KSNYQKIKEEYSNFQREtKEQEQKKRNSLVESlndskIKELEARL 1188
Cdd:pfam07888 363 RRELQELKASLRVAQKE-KEQLQAEKQELLEY-----IRQLEQRL 401
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
934-1038 |
2.52e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 52.55 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 934 DDLVSEKDEISREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQ--SLIKESKL 1011
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEErrEIRKDREI 467
|
90 100
....*....|....*....|....*...
gi 6321812 1012 -KLENEIKRLKDVINSKEEEIKSFNDKL 1038
Cdd:COG2433 468 sRLDREIERLERELEEERERIEELKRKL 495
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
861-1190 |
3.90e-06 |
|
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: 52.05 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 861 TRTKKFNEQINKLKNDLQEMESKKKFLEEKNQKtVNELENTQDLLNQEkenlrkneslLNRVKTSSETLQKQFDDLVSEK 940
Cdd:pfam05557 66 EAEEALREQAELNRLKKKYLEALNKKLNEKESQ-LADAREVISCLKNE----------LSELRRQIQRAELELQSTNSEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 941 DEISREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISD--LNCDISKEQSSQSLIKESKLKLENEIK 1018
Cdd:pfam05557 135 EELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDseIVKNSKSELARIPELEKELERLREHNK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1019 RLKDVINSK---EEEIKSFNDKLsSSEEDLDIKLVTLE-KN----------CNIAMSRLQSLVTEnSDLRSK-------N 1077
Cdd:pfam05557 215 HLNENIENKlllKEEVEDLKRKL-EREEKYREEAATLElEKekleqelqswVKLAQDTGLNLRSP-EDLSRRieqlqqrE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1078 ENFKKEKAALNNQLKNKESELLKMKEKIDNHKKELATFSKQRDdavsEHGKITAELKETRIQLTEYKSNYQKIKEEYSNF 1157
Cdd:pfam05557 293 IVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLK----RHKALVRRLQRRVLLLTKERDGYRAILESYDKE 368
|
330 340 350
....*....|....*....|....*....|....*..
gi 6321812 1158 QRETKEQEQKKRN--SLVESLNDSKIK--ELEARLSQ 1190
Cdd:pfam05557 369 LTMSNYSPQLLERieEAEDMTQKMQAHneEMEAQLSV 405
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
946-1175 |
4.06e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 946 EKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKeqssqslikesklkLENEIKRLKDVIN 1025
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK--------------LQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1026 SKEEEIKSFNDKLSSSEEDLDIKLVTLE-KNCNIAMSRLQSLVTENSDLRSKNENFKKEKAalnnQLKNKESELLKMKEK 1104
Cdd:COG3883 83 ERREELGERARALYRSGGSVSYLDVLLGsESFSDFLDRLSALSKIADADADLLEELKADKA----ELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321812 1105 IDNHKKELATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQKIKEEYSNFQRETKEQEQKKRNSLVES 1175
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1413-1878 |
4.48e-06 |
|
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: 52.10 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1413 EEIRYyKLENYK--LQEILNESNGKL-------SQLTLDLRQSKSKEALLSEQLDRlqkdlESTERQK---ELLSSTIKQ 1480
Cdd:pfam01576 60 EEMRA-RLAARKqeLEEILHELESRLeeeeersQQLQNEKKKMQQHIQDLEEQLDE-----EEAARQKlqlEKVTTEAKI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1481 QKQQFENCMDDLQGNEL---------RLREHIHALKQAEEDVKN-----------MASIIEKLKTQNKQKEKLI-WEREM 1539
Cdd:pfam01576 134 KKLEEDILLLEDQNSKLskerklleeRISEFTSNLAEEEEKAKSlsklknkheamISDLEERLKKEEKGRQELEkAKRKL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1540 ERNDSDMQ-----LQETLLELkRVQDVKKI--LSDDLAHLKE----RLSAVEDRSQYTDEINRLKEEL-------NCSLK 1601
Cdd:pfam01576 214 EGESTDLQeqiaeLQAQIAEL-RAQLAKKEeeLQAALARLEEetaqKNNALKKIRELEAQISELQEDLeseraarNKAEK 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1602 AETNLKKEFATLKYKLETSTNDSEAKISDLLKQLDHYTKVVEMLNNEKDAISLAEKELYQKY----EALNTECESLKGKI 1677
Cdd:pfam01576 293 QRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHtqalEELTEQLEQAKRNK 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1678 VSLTKIKQELESDLNQKTDALQISNAALSSSTQKNKEITEKIKYLEETLQLQMEQNSRNGELVKTLQASCNGYKDKFDDE 1757
Cdd:pfam01576 373 ANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1758 KQKNIDLYEENQTLQKLNTDLQLQLKnlherlSDTTEKNAWLSKIHELEN-MVSLETDLKyEEMKKNKSLERAVEELQT- 1835
Cdd:pfam01576 453 EGKNIKLSKDVSSLESQLQDTQELLQ------EETRQKLNLSTRLRQLEDeRNSLQEQLE-EEEEAKRNVERQLSTLQAq 525
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 6321812 1836 ------KNSQQTDVIELANKNR----SEFEEATLKYE---AQISDLEKYIS--QQELE 1878
Cdd:pfam01576 526 lsdmkkKLEEDAGTLEALEEGKkrlqRELEALTQQLEekaAAYDKLEKTKNrlQQELD 583
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1473-1727 |
6.13e-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: 50.53 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1473 LLSSTIKQQKQQFENCMDDLQGNELRLREHIHALKQAEEDVKNMASIIEKLKTQNKQKEKLIWEREMERNDSDMQLQETL 1552
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1553 LELKRvqdvkkiLSDDLAHLKERLSAVEDRSQYTDEINRLKEELNCSlkaetnlkkefatlkykletstndseaKISDLL 1632
Cdd:COG4942 90 KEIAE-------LRAELEAQKEELAELLRALYRLGRQPPLALLLSPE---------------------------DFLDAV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1633 KQLDHYTKVVEMLNNEKDAISLAEKELYQKYEALNTECESLKGKIVSLTKIKQELESDLNQKTDALQISNAALSSSTQKN 1712
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
250
....*....|....*
gi 6321812 1713 KEITEKIKYLEETLQ 1727
Cdd:COG4942 216 AELQQEAEELEALIA 230
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1403-1928 |
6.30e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.26 E-value: 6.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1403 KNRDSISKYEEEIRYYKLENYKLQEILNESNGKLSQLTLDLRQSKSKEALLSEQLDRLQKDLESTERQKEL-------LS 1475
Cdd:pfam05483 110 ENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREEtrqvymdLN 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1476 STIKQQKQQFENCMddLQGNELRLREHIhalkQAEEDVKNMASIIEKLKTQNKQKEKL-------IWEREMERNDSDMQL 1548
Cdd:pfam05483 190 NNIEKMILAFEELR--VQAENARLEMHF----KLKEDHEKIQHLEEEYKKEINDKEKQvsllliqITEKENKMKDLTFLL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1549 QETLLELKRVQDVKKILSDDLAHLKERlsavedRSQYTDEINRLKEELNCSLKAETNLKKEFATLKYKLETSTNDSEAKI 1628
Cdd:pfam05483 264 EESRDKANQLEEKTKLQDENLKELIEK------KDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQM 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1629 SDLLKQLDHYTKVV-----------EMLNNEKDAISLAEKELyqkyEALNTECESLKGKIVSLTKIKQELESDLNQKTDA 1697
Cdd:pfam05483 338 EELNKAKAAHSFVVtefeattcsleELLRTEQQRLEKNEDQL----KIITMELQKKSSELEEMTKFKNNKEVELEELKKI 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1698 LQISNAALSSSTQKNKeITEKIKYLEETLQLQM---EQNSRNGELVKTLQASCNGY--------KDKFDDEKQKNIDLYE 1766
Cdd:pfam05483 414 LAEDEKLLDEKKQFEK-IAEELKGKEQELIFLLqarEKEIHDLEIQLTAIKTSEEHylkevedlKTELEKEKLKNIELTA 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1767 -------ENQTLQKLNTDLQLQLKNLHERLSDTTEKNAWLSKihELENMVSLETDLKYEemkknksLERAVEELQTKNSQ 1839
Cdd:pfam05483 493 hcdklllENKELTQEASDMTLELKKHQEDIINCKKQEERMLK--QIENLEEKEMNLRDE-------LESVREEFIQKGDE 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1840 QTDVIELANKNRSEFEEATLKYEAQISDLEKYISQqeleMKKSIRDNSSYRDKVQEMAQEIEfWKSRYESTMIGSKNIDS 1919
Cdd:pfam05483 564 VKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN----LKKQIENKNKNIEELHQENKALK-KKGSAENKQLNAYEIKV 638
|
....*....
gi 6321812 1920 NNAQSKIFS 1928
Cdd:pfam05483 639 NKLELELAS 647
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
868-1054 |
6.57e-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: 50.53 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 868 EQINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQFDDLVSEKDEISRE- 946
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 947 --------------KLEV---AQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQSLIKES 1009
Cdd:COG4942 107 aellralyrlgrqpPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6321812 1010 KLKLENEIKRLKDVINSKEEEIKSFN---DKLSSSEEDLDIKLVTLEK 1054
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAaelAELQQEAEELEALIARLEA 234
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
912-1164 |
6.67e-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: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 912 LRKNESLLNRVKTSSETLQKQFDDLVSEKDEISREKLEVAQNLEEAHQKIQGLQETIREREATLEKlhsKNNELIKQISD 991
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE---RREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 992 LncdiSKEQSSQSLIKEsklkleneikrlkdVINSkeeeiKSFNDKLSsseedldiKLVTLEKncniAMSRLQSLVTENS 1071
Cdd:COG3883 95 L----YRSGGSVSYLDV--------------LLGS-----ESFSDFLD--------RLSALSK----IADADADLLEELK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1072 DLRSKNENFKKEKAALNNQLKNKESELLKMKEKIDNHKKE----LATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNY 1147
Cdd:COG3883 140 ADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEqealLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
250
....*....|....*..
gi 6321812 1148 QKIKEEYSNFQRETKEQ 1164
Cdd:COG3883 220 AAAAAAAAAAAAAAAAA 236
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
896-1048 |
6.82e-06 |
|
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: 51.18 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 896 NELENTQDLLNQEKENLRKNESLLNRVKTSSE---TLQKQFDDLVSEKDEISREKLEVAQNLEEAHQKIQGLQETIRERE 972
Cdd:pfam05667 304 EKLQFTNEAPAATSSPPTKVETEEELQQQREEeleELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 973 ATLeKLHSKNNELIKQ----ISDLNCDIskEQSSQSLIK------ESKLKLENEIKRLKDVINSKE-------EEIKSFN 1035
Cdd:pfam05667 384 KQY-KVKKKTLDLLPDaeenIAKLQALV--DASAQRLVElagqweKHRVPLIEEYRALKEAKSNKEdesqrklEEIKELR 460
|
170
....*....|...
gi 6321812 1036 DKLSSSEEDLDIK 1048
Cdd:pfam05667 461 EKIKEVAEEAKQK 473
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1439-1677 |
7.55e-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: 50.53 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1439 LTLDLRQSKSKEALLSEQLDRLQKDLESTERQKELLSSTIKQQKQQFENCMDDLQGNELRLREHIHALKQAEEDVKNMAS 1518
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1519 IIEKLKTQNKQKEKLIweREMERNDSDMQLQETLLELkrvqdvkkILSDDLAHLKERLSAVEdrsQYTDEINRLKEELNC 1598
Cdd:COG4942 91 EIAELRAELEAQKEEL--AELLRALYRLGRQPPLALL--------LSPEDFLDAVRRLQYLK---YLAPARREQAEELRA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321812 1599 SLKAETNLKKEFATLKYKLETSTNDSEAKISDLLKQLDHYTKVVEMLNNEKDAISLAEKELYQKYEALNTECESLKGKI 1677
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
870-1918 |
8.38e-06 |
|
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: 51.21 E-value: 8.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 870 INKLKNDLQE----MESKKKFLE---------EKNQKTVNELENTQDLlnQEKENLRKNESLLNRVKTS-SETLQKQFDD 935
Cdd:TIGR01612 598 INKLKLELKEkiknISDKNEYIKkaidlkkiiENNNAYIDELAKISPY--QVPEHLKNKDKIYSTIKSElSKIYEDDIDA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 936 LVSEKDEISREK----LEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIK-QISDLNCDISKEQSSQslikesk 1010
Cdd:TIGR01612 676 LYNELSSIVKENaidnTEDKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKnELLDIIVEIKKHIHGE------- 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1011 lkLENEIKRLKDVINSKEEEIKSFNDKLSSSEEDLdiklvtlekncNIAMSRLQSLVTENSDlRSKNENFKKEKAALN-- 1088
Cdd:TIGR01612 749 --INKDLNKILEDFKNKEKELSNKINDYAKEKDEL-----------NKYKSKISEIKNHYND-QINIDNIKDEDAKQNyd 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1089 ------NQLKNKESELLKMKEKIDNHKKElatFSKQRDDAVSEHGKITAELKETRIQLTEYKSnyqKIKEEYSNFQRETK 1162
Cdd:TIGR01612 815 kskeyiKTISIKEDEIFKIINEMKFMKDD---FLNKVDKFINFENNCKEKIDSEHEQFAELTN---KIKAEISDDKLNDY 888
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1163 EQEQKKRNSLVESLNDSKIKELEaRLSQEISLNQYLnkRISGNSVETnISSTRRSTSYSDDPLDKE-DIIKKYYDLQLAF 1241
Cdd:TIGR01612 889 EKKFNDSKSLINEINKSIEEEYQ-NINTLKKVDEYI--KICENTKES-IEKFHNKQNILKEILNKNiDTIKESNLIEKSY 964
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1242 TEitrNLENEIEEKKNLISRLrFTETRLASSSFEDQKIKAQMKKLKKliqdmDPSIPLDSILNEPLDncpDKESDINKLM 1321
Cdd:TIGR01612 965 KD---KFDNTLIDKINELDKA-FKDASLNDYEAKNNELIKYFNDLKA-----NLGKNKENMLYHQFD---EKEKATNDIE 1032
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1322 LE-VDYLKRQLDIETRAH---YDAENAISALHSKFRKIQGESSLSSSDIYKLKFEASEERVK------------------ 1379
Cdd:TIGR01612 1033 QKiEDANKNIPNIEIAIHtsiYNIIDEIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLKhynfddfgkeenikyade 1112
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1380 --SLEDKLKTMPLRDRTNLPVGDIIKNRDSISKYEEEIRYYKLENYKLQEILNESNGKLSQLTLDLRQSKSKEALLSEQL 1457
Cdd:TIGR01612 1113 inKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEI 1192
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1458 DRLQKDLESTERQKELLSStIKQQKQQFENCMddlqgNELRLREHIHALKQAEEDVKNMASIIEKLKTQNKQKEKLIWER 1537
Cdd:TIGR01612 1193 KKLLNEIAEIEKDKTSLEE-VKGINLSYGKNL-----GKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEM 1266
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1538 --EMERNDSDMQLQETLLELKRVQDVKKILSDDLAHLKER-LSAVEDRSQYTDeINRLKEELNCSLKAETNLKKEFATLK 1614
Cdd:TIGR01612 1267 giEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKsLKIIEDFSEESD-INDIKKELQKNLLDAQKHNSDINLYL 1345
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1615 YKLETSTNDSEA-KISDLLKQLDHYTKVVEMLN-NEKDAISLAEKELYQKYEalNTECESLKGKIVS----------LTK 1682
Cdd:TIGR01612 1346 NEIANIYNILKLnKIKKIIDEVKEYTKEIEENNkNIKDELDKSEKLIKKIKD--DINLEECKSKIEStlddkdidecIKK 1423
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1683 IKQELESDLNQKTDalqiSNAALSSSTQKNKEITEKIKYLE---ETLQLQMEQNSRNG---------ELVKTLQAScNGY 1750
Cdd:TIGR01612 1424 IKELKNHILSEESN----IDTYFKNADENNENVLLLFKNIEmadNKSQHILKIKKDNAtndhdfninELKEHIDKS-KGC 1498
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1751 KDKFDDEK---QKNIDLYEE--NQTLQKLNTDLQLQLKNLHERLSDttEKNAWLSKIHELENMVSLETDLKYEEMKKNKS 1825
Cdd:TIGR01612 1499 KDEADKNAkaiEKNKELFEQykKDVTELLNKYSALAIKNKFAKTKK--DSEIIIKEIKDAHKKFILEAEKSEQKIKEIKK 1576
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1826 LERAVEELQTKNSQQTDVIELANKNRSEFEEATLKyeaqISDLEKYISQ-----QELEMKKSIRDNSSYRDKVQEMAQEI 1900
Cdd:TIGR01612 1577 EKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLK----ISDIKKKINDclketESIEKKISSFSIDSQDTELKENGDNL 1652
|
1130
....*....|....*...
gi 6321812 1901 EFWKSRYESTMIGSKNID 1918
Cdd:TIGR01612 1653 NSLQEFLESLKDQKKNIE 1670
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
861-1054 |
9.35e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 9.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 861 TRTKKFNEQINKLKNDL----QEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQFDDL 936
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIdhiqQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 937 VSE----KDEISREKLEVA-------------------QNLEEAHQKIQGLQETIREREATLEKLHSKNNEL-------- 985
Cdd:PHA02562 254 SAAlnklNTAAAKIKSKIEqfqkvikmyekggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELeeimdefn 333
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321812 986 --IKQISDLNCDISKEQSSQSLIKESKLKLENEIKRLKDVINSKEEEIKSFNDKLssseEDLDIKLVTLEK 1054
Cdd:PHA02562 334 eqSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDEL----DKIVKTKSELVK 400
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
857-1784 |
1.20e-05 |
|
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: 50.82 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 857 SNDMTRTKKFNEQINKLKNDLQEMesKKKFLEEKNqktvneLENTQDllNQEKENLRKNESLLNRVKTSSETLQKQFDDL 936
Cdd:TIGR01612 768 SNKINDYAKEKDELNKYKSKISEI--KNHYNDQIN------IDNIKD--EDAKQNYDKSKEYIKTISIKEDEIFKIINEM 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 937 VSEKDEIsREKLEVAQNLEEAHQkiqglqETIREREATLEKLhskNNELIKQISD--LNCDISKEQSSQSLIKESKLKLE 1014
Cdd:TIGR01612 838 KFMKDDF-LNKVDKFINFENNCK------EKIDSEHEQFAEL---TNKIKAEISDdkLNDYEKKFNDSKSLINEINKSIE 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1015 NE---IKRLKDV------INSKEEEIKSFNDKLSSSEEDLDIKLVTLEKNCNIAMSRLQSLvtENSDLRSKNENFKKEKA 1085
Cdd:TIGR01612 908 EEyqnINTLKKVdeyikiCENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKF--DNTLIDKINELDKAFKD 985
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1086 ALNNQLKNKESELLK----MKEKIDNHKKElaTFSKQRDdavsEHGKITAELKETRIQLTEYKSNYQ-KIKEEYSNFQRE 1160
Cdd:TIGR01612 986 ASLNDYEAKNNELIKyfndLKANLGKNKEN--MLYHQFD----EKEKATNDIEQKIEDANKNIPNIEiAIHTSIYNIIDE 1059
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1161 TKEQEQKKrnslVESLNDSKIKELEARLSQEISLNQYLNK-RISGNSVETNISSTRRSTSYSDDPLDKEDIIKKYYDlql 1239
Cdd:TIGR01612 1060 IEKEIGKN----IELLNKEILEEAEINITNFNEIKEKLKHyNFDDFGKEENIKYADEINKIKDDIKNLDQKIDHHIK--- 1132
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1240 AFTEITRNLENEIEEKKNLISRLRftetRLASSSFEDQKIKAQMKKLKKLIQDMDPSIPLDSILNEPLDNCPDKESD--- 1316
Cdd:TIGR01612 1133 ALEEIKKKSENYIDEIKAQINDLE----DVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDkts 1208
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1317 --------------INKLMLE-VDYLKRQLDIETRAHYDAENAISALHSKFRKIQGESSLS------------SSDIYKL 1369
Cdd:TIGR01612 1209 leevkginlsygknLGKLFLEkIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEmdikaemetfniSHDDDKD 1288
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1370 KFEASEERVKSLEDklktmpLRDRTnLPVGDIIKNRDSISKYEEEIRYYKLENYKLQEILNESNGKLSQLTLDLRQSKSK 1449
Cdd:TIGR01612 1289 HHIISKKHDENISD------IREKS-LKIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNILKLNKIK 1361
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1450 EAL-----LSEQLDRLQKDLESTERQKELLSSTIKQQ------KQQFENCMDDLQGNEL-----RLREHIHA-------- 1505
Cdd:TIGR01612 1362 KIIdevkeYTKEIEENNKNIKDELDKSEKLIKKIKDDinleecKSKIESTLDDKDIDECikkikELKNHILSeesnidty 1441
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1506 LKQAEEDVKNMASIIEKLKTQNKQKEKLIwerEMERNDSDMQLQETLLELKRVQDVKKILSDDLAHLKERLSAVEDR-SQ 1584
Cdd:TIGR01612 1442 FKNADENNENVLLLFKNIEMADNKSQHIL---KIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELfEQ 1518
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1585 YTDEINRL---------KEELNCSLKAETNLKKEFATLKYKLETSTNDSEAKISDLLKQldHYTKVVEMLNNEKDAISLA 1655
Cdd:TIGR01612 1519 YKKDVTELlnkysalaiKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKE--KFRIEDDAAKNDKSNKAAI 1596
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1656 EkelyqkyeaLNTECESLKGKIVSLTKIKQELeSDLNQKTDALQISNAALSSSTQKNKEitekikyleetlqlqmeqnSR 1735
Cdd:TIGR01612 1597 D---------IQLSLENFENKFLKISDIKKKI-NDCLKETESIEKKISSFSIDSQDTEL-------------------KE 1647
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*....
gi 6321812 1736 NGELVKTLQASCNGYKDKFDDEKQKNIDLYEENQTLQKLNTDLQLQLKN 1784
Cdd:TIGR01612 1648 NGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKN 1696
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1248-1727 |
1.24e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1248 LENEIEEK--KNLISRLRFTETRLASSS-----FEDQKIKAQMKKLKkliqdmdpsipLDSILN---EPLDNCPDKESDI 1317
Cdd:PRK02224 192 LKAQIEEKeeKDLHERLNGLESELAELDeeierYEEQREQARETRDE-----------ADEVLEeheERREELETLEAEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1318 NKLMLEVDYLKRQLDIETRAHYDAENAISALHSKFRKIQGESSLSSSDIyklkfEASEERVKSLEDKLKTmpLRDRTNLP 1397
Cdd:PRK02224 261 EDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADA-----EAVEARREELEDRDEE--LRDRLEEC 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1398 VGDIIKNRDSISKYEEEIRYYKLENYKLQEILNESNGKLSQLTLDLRQSKSKEALLSEQLDRLQK-------DLESTERQ 1470
Cdd:PRK02224 334 RVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgdapvDLGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1471 KELLSSTIKQQKQQFENCMDDLQGNELRLRE---------------------HIHALKQAEEDVKNMASIIEKLKTQNKQ 1529
Cdd:PRK02224 414 LEELREERDELREREAELEATLRTARERVEEaealleagkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEE 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1530 KEkliweremERNDSDMQLQETLLELKRVQDVKKILSDDLAHLKERLsavEDRSQYTDEINRLKEELNCSL--------K 1601
Cdd:PRK02224 494 VE--------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETI---EEKRERAEELRERAAELEAEAeekreaaaE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1602 AETNLKK---EFATLKYKLETSTN--DSEAKISDLLKQLDHYTKVVEMLNNEKDAISLAEKELYQKYEALNTECESLKGK 1676
Cdd:PRK02224 563 AEEEAEEareEVAELNSKLAELKEriESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAE 642
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321812 1677 -----IVSLTKIKQELES----------DLNQKTDALQISNAALSSSTQKNKEITEKIKYLEETLQ 1727
Cdd:PRK02224 643 fdearIEEAREDKERAEEyleqveekldELREERDDLQAEIGAVENELEELEELRERREALENRVE 708
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1073-1881 |
1.35e-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: 50.36 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1073 LRSKNENFKKEKAALNNQLKNKESELLKMKEKIDNHKKELATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQKIKE 1152
Cdd:pfam02463 178 LIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1153 EYSNFQRETKEQEQKKRNSLVESLNDSKIKELEARLSQEISLNQYLNKRISGNSVETNISSTRRSTSYSDDPLDKEDIIK 1232
Cdd:pfam02463 258 QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1233 KYYDLQLAFTEITRNLENEIEEKKNLISRLrftetrlasssfEDQKIKAQMKKLKKLIQDMDPSIPLDSILNEPLDNCPD 1312
Cdd:pfam02463 338 EELEKELKELEIKREAEEEEEEELEKLQEK------------LEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1313 KESDINKLMLEVDYLKRQLdIETRAHYDAENAISALHSKFRKIQGESSLSSSDIYKLKFEASEERVKSLEDKLKTMPLRD 1392
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEE-KKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1393 RTNLPVGDIIKNRDSISKYEEEIRYYKLENYKLQEILNESNGKLSQLTLDLRQSKSKEA--LLSEQLDRLQKDLESTERQ 1470
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVaiSTAVIVEVSATADEVEERQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1471 KELLSST-IKQQKQQFENCMDDLQGNELRLREHIHALKQAEedVKNMASIIEKLKTQNKQKEKLIWEREMERNDSDMQLQ 1549
Cdd:pfam02463 565 KLVRALTeLPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL--AQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1550 ETLLELKRVQDVKKILSDDLAHLKERLSAVEDRSQYTDEINRLKEELNCSLKAETNLKKEFATLKYKLETSTNDSEAKIS 1629
Cdd:pfam02463 643 AKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1630 DLLKQLDHYTKVVEMLNNEKDAISLAEKELyqkyealntECESLKGKIVSLTKIKQELESDLNQKTDALQISNAALSSST 1709
Cdd:pfam02463 723 LADRVQEAQDKINEELKLLKQKIDEEEEEE---------EKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKE 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1710 QKNKEITEKIKYLEETLQLQMEQNSRNGELVKTLQASCNGYKDKFDDEKQKNIDLYEENQTLQKLNTDLQLQLKNLhERL 1789
Cdd:pfam02463 794 EKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELL-QEL 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1790 SDTTEKNAWLSKIHELENMVSLETDLKYEEMKKNKSLERAVEELQTKNSQQTDVIELANKNRSEFEEATLKYEAQISDLE 1869
Cdd:pfam02463 873 LLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEE 952
|
810
....*....|..
gi 6321812 1870 KYISQQELEMKK 1881
Cdd:pfam02463 953 NNKEEEEERNKR 964
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1269-1535 |
1.65e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1269 LASSSFEDQKIKAQMKKLKKLIQDMDpsipldsilnepldncpDKESDINKLMLEVDYLKRQLDietrahyDAENAISAL 1348
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIA-----------------ELEKELAALKKEEKALLKQLA-------ALERRIAAL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1349 HSKFRKIQGESSLSSSDIYKLKFEAS------EERVKSLEDKLKTMPLRDRTNLPvgDIIKNRDSISKYEEEIRYYK-LE 1421
Cdd:COG4942 68 ARRIRALEQELAALEAELAELEKEIAelraelEAQKEELAELLRALYRLGRQPPL--ALLLSPEDFLDAVRRLQYLKyLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1422 NYKLQEI--LNESNGKLSQLTLDLRQSKSKEALLSEQLDRLQKDLESTERQKELLSSTIKQQKQQFENCMDDLQGNELRL 1499
Cdd:COG4942 146 PARREQAeeLRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
250 260 270
....*....|....*....|....*....|....*.
gi 6321812 1500 REHIHALKQAEEDVKNMASIieklKTQNKQKEKLIW 1535
Cdd:COG4942 226 EALIARLEAEAAAAAERTPA----AGFAALKGKLPW 257
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1411-1901 |
1.85e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.12 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1411 YEEEIRYYKLENYKLQEILNESNGKLSQLTLDLRQSkskeallseqLDRLQKDLESTERQKELLSSTIKQQKQQFENCMD 1490
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQS----------VIDLQTKLQEMQMERDAMADIRRRESQSQEDLRN 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1491 DLQGNelrlrehIHALKQAEEDVKNMasiiekLKTQNKQKEKLiwEREMERNDSDMQLQETLLELKRVQDVKKIlsddla 1570
Cdd:pfam15921 146 QLQNT-------VHELEAAKCLKEDM------LEDSNTQIEQL--RKMMLSHEGVLQEIRSILVDFEEASGKKI------ 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1571 HLKERLSAVEDRSQYTdEINRLKEELNCSLkaeTNLKKEFATLKYKLETSTNDSEAKISDLLKQldHYTKVVEMLNNEKD 1650
Cdd:pfam15921 205 YEHDSMSTMHFRSLGS-AISKILRELDTEI---SYLKGRIFPVEDQLEALKSESQNKIELLLQQ--HQDRIEQLISEHEV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1651 AISlaekELYQKYEALNTECESLKGKIVSLTKIKQELESDLNQKTDALQISNAALSSSTQKNKEITE-KIKYLEETLQLQ 1729
Cdd:pfam15921 279 EIT----GLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEdKIEELEKQLVLA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1730 meqnsrNGELVKTLQAscngyKDKFDDEkQKNIDlyeenQTLQKLNTDLQLQLKNLheRLSDTTEKNAWlskIHELENMV 1809
Cdd:pfam15921 355 ------NSELTEARTE-----RDQFSQE-SGNLD-----DQLQKLLADLHKREKEL--SLEKEQNKRLW---DRDTGNSI 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1810 SL-----ETDLKYEEMKKNKSLERAVE-ELQTKNSQQTDVIELANKNRSEFEEATLKYEAQISDLEKYISQ---QELEMK 1880
Cdd:pfam15921 413 TIdhlrrELDDRNMEVQRLEALLKAMKsECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEEltaKKMTLE 492
|
490 500
....*....|....*....|.
gi 6321812 1881 KSIRDNSSYRDKVQEMAQEIE 1901
Cdd:pfam15921 493 SSERTVSDLTASLQEKERAIE 513
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
839-1062 |
1.87e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.90 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 839 KEDPWFNLFIRIKpLLTSSNDMTRTKKFNEQINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLRKNESL 918
Cdd:PRK01156 566 KRTSWLNALAVIS-LIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKIL 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 919 LNRVKTSSETLQKQF---DDLVSEKDEISREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCD 995
Cdd:PRK01156 645 IEKLRGKIDNYKKQIaeiDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINET 724
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321812 996 IskeqssqslikESKLKLENEIKRLKDVINSKEEE------IKSFNDKLSS------SEEDLDIKLVTLEKNCNIAMSR 1062
Cdd:PRK01156 725 L-----------ESMKKIKKAIGDLKRLREAFDKSgvpamiRKSASQAMTSltrkylFEFNLDFDDIDVDQDFNITVSR 792
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
861-989 |
2.05e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 861 TRTKKFNEQINKLKNDLQEMESKKKFLE---EKNQKTVNELENTQDLLNQE----KENLRKNESLLNRVKTSSE--TLQK 931
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEarlEAAKTELEDLEKEIKRLELEieevEARIKKYEEQLGNVRNNKEyeALQK 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 6321812 932 QFDDLVSEKDEISREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQI 989
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
929-1132 |
2.12e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.24 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 929 LQKQFDDLVSEKDEIsREKLEVAQNLEEAHQK-----IQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQ 1003
Cdd:PHA02562 179 LNQQIQTLDMKIDHI-QQQIKTYNKNIEEQRKkngenIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1004 SLIKESKLKLENEIKRLKDVI-------------------NSKEEEIKSFNDKLSSSEEDLDIKLVTLEKncniAMSRLQ 1064
Cdd:PHA02562 258 NKLNTAAAKIKSKIEQFQKVIkmyekggvcptctqqisegPDRITKIKDKLKELQHSLEKLDTAIDELEE----IMDEFN 333
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321812 1065 SLVTENSDLRSKNENFKKEKAALNNQLKNKESELLKMKEKIDNHKKELATFSKQRDDAVSEHGKITAE 1132
Cdd:PHA02562 334 EQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
835-1191 |
2.37e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.40 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 835 NRLVKEDPWFNLFIRIKPLLTSSNDM-TRTKKFNEQINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQEkenlr 913
Cdd:pfam01576 378 AKQALESENAELQAELRTLQQAKQDSeHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEA----- 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 914 knESLLNRVKTSSETLQKQFDDLVSEKDEISREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLN 993
Cdd:pfam01576 453 --EGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMK 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 994 CDISKEQSSQSLIKESKLKLENEIKRLKDVINSKEEEIKSFNDKLSSSEEDLDIKLVTLEKNCNI-------------AM 1060
Cdd:pfam01576 531 KKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLvsnlekkqkkfdqML 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1061 SRLQSLVTENSDLRSKNENFKKEKAALNNQLKNKESELLKMKEKIDNHKK----ELATFSKQRDDA---VSEHGK----I 1129
Cdd:pfam01576 611 AEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKqlraEMEDLVSSKDDVgknVHELERskraL 690
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321812 1130 TAELKETRIQLTEYKSNYQ-----KIKEEY------SNFQRETK---EQEQKKRNSLVEslndsKIKELEARLSQE 1191
Cdd:pfam01576 691 EQQVEEMKTQLEELEDELQatedaKLRLEVnmqalkAQFERDLQardEQGEEKRRQLVK-----QVRELEAELEDE 761
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
854-1550 |
2.55e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.35 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 854 LTSSNDMTRTKKF--NEQINKLKNDLQEMESKK--------------KFLEEKNQKTVNELENT----QDLL---NQEKE 910
Cdd:pfam15921 94 LNESNELHEKQKFylRQSVIDLQTKLQEMQMERdamadirrresqsqEDLRNQLQNTVHELEAAkclkEDMLedsNTQIE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 911 NLRK----NESLLNRVKTSSETLQKQFDDLVSEKDEISREKLE-----VAQNLEEAHQKIQGLQETIREREATLEKLHSK 981
Cdd:pfam15921 174 QLRKmmlsHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRslgsaISKILRELDTEISYLKGRIFPVEDQLEALKSE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 982 NN---ELIKQ---------ISDLNCDIS------KEQSSQSLIKESKLKLENEIKRLKDV-----INSKEEEIKSFNDKL 1038
Cdd:pfam15921 254 SQnkiELLLQqhqdrieqlISEHEVEITgltekaSSARSQANSIQSQLEIIQEQARNQNSmymrqLSDLESTVSQLRSEL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1039 SSSEEDLDIKLVTLEKNCNIAMSRLQSLVTENSDLRSKNENFKKEKAALNNQLKNKESELLKMKEK-------------- 1104
Cdd:pfam15921 334 REAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQnkrlwdrdtgnsit 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1105 IDNHKKELatfskqrDDAVSEHGKITAELKETriqlteyKSNYQ-KIKEEYSNFQreTKEQEQKKRNSLVESLNDSkiKE 1183
Cdd:pfam15921 414 IDHLRREL-------DDRNMEVQRLEALLKAM-------KSECQgQMERQMAAIQ--GKNESLEKVSSLTAQLEST--KE 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1184 LEARLSQEISLnqylnKRISGNSVETNISSTRRSTSYSDDPLDKEDiikkyydlqlafTEITRnLENEIEEKKNLISRLR 1263
Cdd:pfam15921 476 MLRKVVEELTA-----KKMTLESSERTVSDLTASLQEKERAIEATN------------AEITK-LRSRVDLKLQELQHLK 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1264 FTETRLASSSFEDQKIKAQMKKLKKLIQdmdpsipldsILNEPLDNCPD---------KESDINKLMLEVDYLKRQLDI- 1333
Cdd:pfam15921 538 NEGDHLRNVQTECEALKLQMAEKDKVIE----------ILRQQIENMTQlvgqhgrtaGAMQVEKAQLEKEINDRRLELq 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1334 ETRAHYDAENAisalhsKFRKIqgESSLSSSDIYKLKF-EASEERVKSLEDklktmpLRDRTNLPVGDIIKNRDSISKYE 1412
Cdd:pfam15921 608 EFKILKDKKDA------KIREL--EARVSDLELEKVKLvNAGSERLRAVKD------IKQERDQLLNEVKTSRNELNSLS 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1413 EEIRYYK-----------LENYKLQEILNESNGKLSQLTLDLRQSKSKEALLSEQLDRLQKDLESTERQKELLSSTIkqq 1481
Cdd:pfam15921 674 EDYEVLKrnfrnkseemeTTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKI--- 750
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321812 1482 kQQFENCMDDLQGNELRLREHIHALKQAEEDV---KN-MASIIEKLKTQNKQKEKLIWEREMERNDSDMQLQE 1550
Cdd:pfam15921 751 -QFLEEAMTNANKEKHFLKEEKNKLSQELSTVateKNkMAGELEVLRSQERRLKEKVANMEVALDKASLQFAE 822
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1424-1901 |
2.61e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1424 KLQEILNESNGKLSQLTLDLRQS-----------KS--KEALLSEQLDRLQKDLES----TERQKELLSSTIKQQKQQfe 1486
Cdd:COG4717 2 KIKELEIYGFGKFRDRTIEFSPGlnviygpneagKStlLAFIRAMLLERLEKEADElfkpQGRKPELNLKELKELEEE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1487 ncMDDLQGNELRLREHIHALKQAEEDVKNMASIIEKLKTQNKQKEKLIweremerndsdmQLQETLLELKRVQDVKKILS 1566
Cdd:COG4717 80 --LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL------------QLLPLYQELEALEAELAELP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1567 DDLAHLKERLSAVEDRSQytdEINRLKEELNcslKAETNLKKEFATLKYKLETSTNDSEAKISDLLKQLDHYTKVVEMLN 1646
Cdd:COG4717 146 ERLEELEERLEELRELEE---ELEELEAELA---ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1647 NEKDAISLAEKELYQKYEALNTEcESLK---------GKIVSLTKIKQELESDLNQKTDALQISNAALS-SSTQKNKEIT 1716
Cdd:COG4717 220 EELEELEEELEQLENELEAAALE-ERLKearlllliaAALLALLGLGGSLLSLILTIAGVLFLVLGLLAlLFLLLAREKA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1717 EKIKYLEETLQLQMEQNSRNGELVKTLQAscngYKDKFDDEKQKNIDLYEENQTLQKLNTDL-----QLQLKNLHERLS- 1790
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAA----LGLPPDLSPEELLELLDRIEELQELLREAeeleeELQLEELEQEIAa 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1791 -----DTTEKNAWLSKIHELENMVSLETDLkyeemkknKSLERAVEELQTKNSQQTDVIELAN-KNRSEFEEATLK-YEA 1863
Cdd:COG4717 375 llaeaGVEDEEELRAALEQAEEYQELKEEL--------EELEEQLEELLGELEELLEALDEEElEEELEELEEELEeLEE 446
|
490 500 510
....*....|....*....|....*....|....*...
gi 6321812 1864 QISDLEKYISQQELEMKKSIRDnssyrDKVQEMAQEIE 1901
Cdd:COG4717 447 ELEELREELAELEAELEQLEED-----GELAELLQELE 479
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
896-1104 |
2.71e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 896 NELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQFDDLVSEKDEISREKLEVAQNLEEAHQKIQGLQETIREREATL 975
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 976 EKLHSKNNELIK------QISDLNCDISKEQSSQSL--------IKESKLKLENEIKRLKDVINSKEEEIKSFNDKLSSS 1041
Cdd:COG4942 100 EAQKEELAELLRalyrlgRQPPLALLLSPEDFLDAVrrlqylkyLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321812 1042 EEDLDIKLVTLEKNCNIAMSRLQSLVTENSDLRSKNENFKKEKAALNNQLKNKESELLKMKEK 1104
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
886-1140 |
2.91e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 886 FLEEKNQKTVNELENTQDLLNQEKENLRKN----ESLLN--RVKTSSETLQKQFDDLVSEKDEISREKLEVAQNLEEAHQ 959
Cdd:COG3206 161 YLEQNLELRREEARKALEFLEEQLPELRKEleeaEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 960 KIQGLQETIREREATLEKL--HSKNNELIKQISDLNcdiskeqssQSLIKESKLKLEN--EIKRLKDVINSKEEEIKSFN 1035
Cdd:COG3206 241 RLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELE---------AELAELSARYTPNhpDVIALRAQIAALRAQLQQEA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1036 DKLssseedldikLVTLEKNCNIAMSRLQSLVTENSDLRSKnenfkkekaalNNQLKNKESELLKMKEKIDNHKKELATF 1115
Cdd:COG3206 312 QRI----------LASLEAELEALQAREASLQAQLAQLEAR-----------LAELPELEAELRRLEREVEVARELYESL 370
|
250 260
....*....|....*....|....*
gi 6321812 1116 SKQRDDAvsehgKITAELKETRIQL 1140
Cdd:COG3206 371 LQRLEEA-----RLAEALTVGNVRV 390
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
868-1190 |
2.97e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 868 EQINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQEKEnlrKNESLlnrvktssETLQKQFDDLVSEKDEISREK 947
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEE---RREEL--------ETLEAEIEDLRETIAETERER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 948 LEvaqnleeahqkiqgLQETIREREATLEKLHSKNNELIKqisdlncDISKEQSSQSLIKESKLKLENEIKRLKDVINSK 1027
Cdd:PRK02224 275 EE--------------LAEEVRDLRERLEELEEERDDLLA-------EAGLDDADAEAVEARREELEDRDEELRDRLEEC 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1028 EEEIKSFNDKLSSSEEDLDiklvTLEkncniamsrlqslvTENSDLRSKNENFKKEKAALNNQLKNKESELLKMKEKIDN 1107
Cdd:PRK02224 334 RVAAQAHNEEAESLREDAD----DLE--------------ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1108 HKKELATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQKIK---EEYSNFQRETK--EQEQKKRNS-LVESLNDS-- 1179
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARervEEAEALLEAGKcpECGQPVEGSpHVETIEEDre 475
|
330
....*....|.
gi 6321812 1180 KIKELEARLSQ 1190
Cdd:PRK02224 476 RVEELEAELED 486
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
868-1190 |
3.58e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 868 EQINKLKNDLQEMESKKKFLEEKnqktVNELENTQDLLNQEKENLRkNESLLNRVktSSETLQKQFDDLVSEKDEISREK 947
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEE----VRDLRERLEELEEERDDLL-AEAGLDDA--DAEAVEARREELEDRDEELRDRL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 948 LEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQSlikesklKLENEIKRLKDVINSK 1027
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE-------ELEEEIEELRERFGDA 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1028 E---EEIKSFNDKLSSSEEDLDIKLVTLEKNcniaMSRLQSLVTENSDLRSKN------------------ENFKKEKAA 1086
Cdd:PRK02224 404 PvdlGNAEDFLEELREERDELREREAELEAT----LRTARERVEEAEALLEAGkcpecgqpvegsphvetiEEDRERVEE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1087 LNNQLKNKESELLKMKEKIDNHK------KELATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQKIKEEysnfQRE 1160
Cdd:PRK02224 480 LEAELEDLEEEVEEVEERLERAEdlveaeDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE----AEE 555
|
330 340 350
....*....|....*....|....*....|
gi 6321812 1161 TKEQEQKKRNSLVESLndSKIKELEARLSQ 1190
Cdd:PRK02224 556 KREAAAEAEEEAEEAR--EEVAELNSKLAE 583
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
869-1276 |
3.77e-05 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 48.89 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 869 QINKLKNDLQEMESKKKFLEEKnqktvneLENTQDLLNQEKENLrknesllnrVKTSSETLQKQFDDLVSEKDEISREKL 948
Cdd:PTZ00108 1000 LLGKLERELARLSNKVRFIKHV-------INGELVITNAKKKDL---------VKELKKLGYVRFKDIIKKKSEKITAEE 1063
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 949 EVAQNLEEAhqkiqglqETIREREATLEKLHSKNNELIKQISdlncdiskeqssqSLIKESKLKLENEikrlkdvINSKE 1028
Cdd:PTZ00108 1064 EEGAEEDDE--------ADDEDDEEELGAAVSYDYLLSMPIW-------------SLTKEKVEKLNAE-------LEKKE 1115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1029 EEIksfnDKLSSSE------EDLDIKLVTLEKncniamSRLQSLVTENSDLRSKNENFKKEKAALNNQLKNKESELLKMK 1102
Cdd:PTZ00108 1116 KEL----EKLKNTTpkdmwlEDLDKFEEALEE------QEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSS 1185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1103 EKIDNHKKELATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQKIKEEYSNFQRETKEQEQKKRNSLVESLNDSKIK 1182
Cdd:PTZ00108 1186 ADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDL 1265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1183 ELEARLSQEI---SLNQYLNKRISGNS-VETNISSTRRSTSYSDDPLDKEDIIKKYYDLQLAFTEITRNLENEIEEKKNL 1258
Cdd:PTZ00108 1266 SKEGKPKNAPkrvSAVQYSPPPPSKRPdGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKTRVKQAS 1345
|
410
....*....|....*...
gi 6321812 1259 ISRLRFTETRLASSSFED 1276
Cdd:PTZ00108 1346 ASQSSRLLRRPRKKKSDS 1363
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1372-1899 |
4.80e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.58 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1372 EASEERVKSlEDKLKTMPLRDRTNlPVGDIIKNRDSISKYEEEiRYYKLENyKLQEILNESNGKLsQLTLDLRQSKSKEA 1451
Cdd:pfam15921 198 EASGKKIYE-HDSMSTMHFRSLGS-AISKILRELDTEISYLKG-RIFPVED-QLEALKSESQNKI-ELLLQQHQDRIEQL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1452 L---------LSEQLDRLQKDLESTERQKELLSSTIKQQKQQFENCMDDLQGNELRLREHIHALKQAEEDVknmasiIEK 1522
Cdd:pfam15921 273 IseheveitgLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDK------IEE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1523 LKTQ----NKQKEKLIWEREM---ERNDSDMQLQETLLEL--------------KRVQDVKKILSDDLAHLKERLsavED 1581
Cdd:pfam15921 347 LEKQlvlaNSELTEARTERDQfsqESGNLDDQLQKLLADLhkrekelslekeqnKRLWDRDTGNSITIDHLRREL---DD 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1582 RSQytdEINRLkEELNCSLKAETN--LKKEFATLKYKletstNDSEAKISDLLKQLDH----YTKVVEMLNNEKDAISLA 1655
Cdd:pfam15921 424 RNM---EVQRL-EALLKAMKSECQgqMERQMAAIQGK-----NESLEKVSSLTAQLEStkemLRKVVEELTAKKMTLESS 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1656 EKELyqkyealnteceslkgkivsltkikQELESDLNQKTDALQISNAalssstqknkEITEKIKYLEetLQLQMEQNSR 1735
Cdd:pfam15921 495 ERTV-------------------------SDLTASLQEKERAIEATNA----------EITKLRSRVD--LKLQELQHLK 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1736 N-GELVKTLQASCNGYKDKFDdEKQKNIDLYEEnqtlqklntdlqlqlknlherlsdtteknawlskihELENMVSLETD 1814
Cdd:pfam15921 538 NeGDHLRNVQTECEALKLQMA-EKDKVIEILRQ------------------------------------QIENMTQLVGQ 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1815 LKyeemkknksleRAVEELQTKNSQQTDVIelaNKNRSEFEEATL---KYEAQISDLEKYISQQELEMKKSIRDNSSYRD 1891
Cdd:pfam15921 581 HG-----------RTAGAMQVEKAQLEKEI---NDRRLELQEFKIlkdKKDAKIRELEARVSDLELEKVKLVNAGSERLR 646
|
....*...
gi 6321812 1892 KVQEMAQE 1899
Cdd:pfam15921 647 AVKDIKQE 654
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
841-1620 |
4.82e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.50 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 841 DPWFNLFIRIKPLLTS----SNDMTRTKKFNEQINKLKNDLQEMESKKKF--------LEEKNQKTVNELENTQDLLNQE 908
Cdd:TIGR00606 248 DPLKNRLKEIEHNLSKimklDNEIKALKSRKKQMEKDNSELELKMEKVFQgtdeqlndLYHNHQRTVREKERELVDCQRE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 909 KENLRKNESLLNRVKTSSET----LQKQFDDLVSEKDEISREKLEVAQNLE--------EAHQKIQGLQETIREREATLE 976
Cdd:TIGR00606 328 LEKLNKERRLLNQEKTELLVeqgrLQLQADRHQEHIRARDSLIQSLATRLEldgfergpFSERQIKNFHTLVIERQEDEA 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 977 KLHSKNnelikqISDLNCDISKEQSSQSLIKESKLKLENEIKRLKDVINSKEEEIKSFNDKLSSSEEDLDiKLVTLEKNC 1056
Cdd:TIGR00606 408 KTAAQL------CADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD-RILELDQEL 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1057 NIAMSRLqSLVTENSDLRSKNENFKKEKAALNNQLKNKESELLKMKEKiDNHK---KELATFSKQRDDAVSEHGKITAEL 1133
Cdd:TIGR00606 481 RKAEREL-SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQL-NHHTttrTQMEMLTKDKMDKDEQIRKIKSRH 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1134 KETRIQLTEYKSNYQKIKEEYSNFQRETKEQEQKKRN-----SLVESLNDSKIKELEARLSQEISLNQYLNKRISGNSVE 1208
Cdd:TIGR00606 559 SDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKlnkelASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEE 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1209 TNISSTrrstsysddpldKEDIIKKYYDLQLafteitrnLENEIEEKKNLISRLRFTETRLASSSFEDQKIKAQMKKLKK 1288
Cdd:TIGR00606 639 SDLERL------------KEEIEKSSKQRAM--------LAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFIS 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1289 LIQDMDPSIPldsilneplDNCPDKESDINKLMLEVDYLKRQLDIETRAHYDAENAISALHSKFRKIQGESSLSSSDIYK 1368
Cdd:TIGR00606 699 DLQSKLRLAP---------DKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1369 LK--FEASEERVKSLEDKLKTMPLRDRTNLPVGDI---IKNRDSISKYEEEIRYYKLENYKLQEILNESNGKLSQLTLDL 1443
Cdd:TIGR00606 770 QEtlLGTIMPEEESAKVCLTDVTIMERFQMELKDVerkIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNR 849
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1444 RQSKSKEallsEQLDRLQKDLESTERQKELLSSTIkQQKQQFENCMDDLQGnelRLREHIHALKQAEEDVKNMASIIEKL 1523
Cdd:TIGR00606 850 KLIQDQQ----EQIQHLKSKTNELKSEKLQIGTNL-QRRQQFEEQLVELST---EVQSLIREIKDAKEQDSPLETFLEKD 921
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1524 KTQNkqkEKLIWEREMERNDSDMQLQETLLELKRVQDVKKILSDDLAHLKERLsavedRSQYTDEINRLKEELNCSLKAE 1603
Cdd:TIGR00606 922 QQEK---EELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDY-----LKQKETELNTVNAQLEECEKHQ 993
|
810
....*....|....*..
gi 6321812 1604 TNLKKEFATLKYKLETS 1620
Cdd:TIGR00606 994 EKINEDMRLMRQDIDTQ 1010
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
868-1205 |
6.75e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.97 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 868 EQINKLKNDLQEMeskkkfLEEKNQKTVNELENTQDLLnqekENLRKNESLLNRVKTSSetlQKQFDDLVSEKDEISREK 947
Cdd:PLN02939 106 EAIAAIDNEQQTN------SKDGEQLSDFQLEDLVGMI----QNAEKNILLLNQARLQA---LEDLEKILTEKEALQGKI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 948 LEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQSLIKESKLKLENEIKRLK-DVINS 1026
Cdd:PLN02939 173 NILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKaELIEV 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1027 KEEE----------------IKSFNDKLSSSEEDLdIKLVTLEKNCniAMSRLQSLvtenSDLRSKNENfKKEKAAL--- 1087
Cdd:PLN02939 253 AETEervfklekerslldasLRELESKFIVAQEDV-SKLSPLQYDC--WWEKVENL----QDLLDRATN-QVEKAALvld 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1088 -NNQLKNKESELLKMKEKIDNHK--KELATFSKQRDDAVSEHGKITAELKETRIQLteyksnYQKIKEEYSNFQRETKEQ 1164
Cdd:PLN02939 325 qNQDLRDKVDKLEASLKEANVSKfsSYKVELLQQKLKLLEERLQASDHEIHSYIQL------YQESIKEFQDTLSKLKEE 398
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 6321812 1165 EQKKrnSLVESLNDSKiKELEARLSQEISlNQYLNKRISGN 1205
Cdd:PLN02939 399 SKKR--SLEHPADDMP-SEFWSRILLLID-GWLLEKKISNN 435
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
868-996 |
7.01e-05 |
|
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: 45.97 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 868 EQINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLRKN----ESLLNRVKTSSETLQKQFDDLVsekDEI 943
Cdd:pfam06785 58 EDALKEKFEKSFLEEKEAKLTELDAEGFKILEETLEELQSEEERLEEElsqkEEELRRLTEENQQLQIQLQQIS---QDF 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 6321812 944 SREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDI 996
Cdd:pfam06785 135 AEFRLESEEQLAEKQLLINEYQQTIEEQRSVLEKRQDQIENLESKVRDLNYEI 187
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
865-1718 |
8.10e-05 |
|
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: 48.12 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 865 KFNEQINKLKN---DLQEMESKKKFLEEKNqkTVNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKqFDDLVSEKD 941
Cdd:TIGR01612 868 QFAELTNKIKAeisDDKLNDYEKKFNDSKS--LINEINKSIEEEYQNINTLKKVDEYIKICENTKESIEK-FHNKQNILK 944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 942 EISREKLEVAQN---LEEAHQ---------KIQGLQETIREreATLEKLHSKNNELIKQISDLNCDISKEQSSQslikes 1009
Cdd:TIGR01612 945 EILNKNIDTIKEsnlIEKSYKdkfdntlidKINELDKAFKD--ASLNDYEAKNNELIKYFNDLKANLGKNKENM------ 1016
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1010 klkLENEIKRLKDVINSKEEEIKSFNDKLSSSEEDLDIKLVT----LEKNCNIAMSRLQSLVTENSDLRSKNENFKKEKA 1085
Cdd:TIGR01612 1017 ---LYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNiideIEKEIGKNIELLNKEILEEAEINITNFNEIKEKL 1093
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1086 ALNNQLKNKESELLKMKEKIDNHKKELATFSKQRDDAVSEHGKITaelKETRIQLTEYKSNYQKIKE--EYSNFQRETKE 1163
Cdd:TIGR01612 1094 KHYNFDDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIK---KKSENYIDEIKAQINDLEDvaDKAISNDDPEE 1170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1164 QEQKKRNSLVESLNDSKIKELEARLSQEI--------SLNQYLNKRIS-GNSVETNISSTRRSTSYSDDPLDK--EDIIK 1232
Cdd:TIGR01612 1171 IEKKIENIVTKIDKKKNIYDEIKKLLNEIaeiekdktSLEEVKGINLSyGKNLGKLFLEKIDEEKKKSEHMIKamEAYIE 1250
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1233 KYYDLQLAFTEITRNLENEIEEKKNL----ISRLRFTETRLASSSfEDQKIKAQMKKLKKLIQDMDPSIPLDSILNEPLD 1308
Cdd:TIGR01612 1251 DLDEIKEKSPEIENEMGIEMDIKAEMetfnISHDDDKDHHIISKK-HDENISDIREKSLKIIEDFSEESDINDIKKELQK 1329
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1309 NCPDKE---SDINKLMLEVDYLKRQLDIetrahydaeNAISALHSKFRKIQGESSLSSSDIyKLKFEASEERVKSLED-- 1383
Cdd:TIGR01612 1330 NLLDAQkhnSDINLYLNEIANIYNILKL---------NKIKKIIDEVKEYTKEIEENNKNI-KDELDKSEKLIKKIKDdi 1399
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1384 KLKTMPLRDRTNLPVGDIIKNRDSISKYEEEIRYYKLENYKLQEILNESNGKLSQLTLDLRQSKSKeallSEQLDRLQKD 1463
Cdd:TIGR01612 1400 NLEECKSKIESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNK----SQHILKIKKD 1475
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1464 LESTERQKELlsSTIKQQKQQFENCMDDLQGNELRLREHIHALKQAEEDVKNMASIIEKLKTQN------KQKEKLIWER 1537
Cdd:TIGR01612 1476 NATNDHDFNI--NELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNkfaktkKDSEIIIKEI 1553
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1538 EMERNDSDMQLQETLLELKRVQDVKKILSDDLAHLKERLSA-------VEDRSQYTDEINRLKEELNCSLKAETNLKKEF 1610
Cdd:TIGR01612 1554 KDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAaidiqlsLENFENKFLKISDIKKKINDCLKETESIEKKI 1633
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1611 ATLkykletSTNDSEAKISDLLKQLDHYTKVVEMLNNEKDAISLAEKELyqkyEALNTECESLKgkiVSLTKIKQELESD 1690
Cdd:TIGR01612 1634 SSF------SIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKEL----DELDSEIEKIE---IDVDQHKKNYEIG 1700
|
890 900
....*....|....*....|....*...
gi 6321812 1691 LNQKTDALQISNAALSSSTQKNKEITEK 1718
Cdd:TIGR01612 1701 IIEKIKEIAIANKEEIESIKELIEPTIE 1728
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
877-1332 |
8.43e-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: 47.79 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 877 LQEMESKKKFLEEKNQKTVNELENTQDLL---NQEKENLRKNESLLnrvktssetlqkqfddlvsekdeisreklevaqn 953
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEINDKEKQVSLLliqITEKENKMKDLTFL---------------------------------- 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 954 LEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQSLI-----------------KESKLKLENE 1016
Cdd:pfam05483 263 LEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALeedlqiatkticqlteeKEAQMEELNK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1017 IK--------RLKDVINSKEEEIKSFNDKLSSSEEDLDIKLVTLEK-------------NCNIAMSRLQSLVTENSDLRS 1075
Cdd:pfam05483 343 AKaahsfvvtEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKksseleemtkfknNKEVELEELKKILAEDEKLLD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1076 KNENFKKekaaLNNQLKNKESE---LLKMKEK-IDNHKKELATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQKIK 1151
Cdd:pfam05483 423 EKKQFEK----IAEELKGKEQElifLLQAREKeIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1152 EEYSNFQRETKEQEQKKRNSLVESLNDSK-----IKELEARLSQEISLNQYLnKRISGNSVETNISSTRRSTSYSDDPLD 1226
Cdd:pfam05483 499 LENKELTQEASDMTLELKKHQEDIINCKKqeermLKQIENLEEKEMNLRDEL-ESVREEFIQKGDEVKCKLDKSEENARS 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1227 KEDIIKKYYDLQLAFTEITRNLENEIEEKKNLISRLRFTETRL-ASSSFEDQKIKAQMKKLKKLIQDMDPSI-PLDSILN 1304
Cdd:pfam05483 578 IEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALkKKGSAENKQLNAYEIKVNKLELELASAKqKFEEIID 657
|
490 500
....*....|....*....|....*...
gi 6321812 1305 EPLDNCPDKESDINKLMLEVDYLKRQLD 1332
Cdd:pfam05483 658 NYQKEIEDKKISEEKLLEEVEKAKAIAD 685
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
868-1172 |
1.01e-04 |
|
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: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 868 EQINKLKNDLQEMESKKKFLEEK------------NQKTVNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQFDD 935
Cdd:COG4913 624 EELAEAEERLEALEAELDALQERrealqrlaeyswDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEE 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 936 LVSEKDEISREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKnnELIKQISDLNCDiskeqssqSLIKESKLKLEN 1015
Cdd:COG4913 704 LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LLEERFAAALGD--------AVERELRENLEE 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1016 EIKRLKDVINSKEEEI----KSFNDKLSSSEEDLDIKLVTLEKncniAMSRLQSLvtENSDLRSKNENFKKekaALNNQL 1091
Cdd:COG4913 774 RIDALRARLNRAEEELeramRAFNREWPAETADLDADLESLPE----YLALLDRL--EEDGLPEYEERFKE---LLNENS 844
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1092 KNKESELL-KMKEKIDNHKKELATfskqrddavsehgkITAELK------ETRIQL-------TEYKSNYQKIKEEYSNF 1157
Cdd:COG4913 845 IEFVADLLsKLRRAIREIKERIDP--------------LNDSLKripfgpGRYLRLearprpdPEVREFRQELRAVTSGA 910
|
330
....*....|....*
gi 6321812 1158 QRETKEQEQKKRNSL 1172
Cdd:COG4913 911 SLFDEELSEARFAAL 925
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
938-1112 |
1.11e-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: 45.69 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 938 SEKDEISREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQSLIKESK--LKLEN 1015
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1016 EIKRLKDVINSKEEEIKSFNDKLSSSEEDLDiklvtlekncniamsrlqslvTENSDLRSKNENFKKEKAALNNQLKNKE 1095
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELA---------------------ELEAELAELEAELEEKKAELDEELAELE 155
|
170
....*....|....*..
gi 6321812 1096 SELLKMKEKIDNHKKEL 1112
Cdd:COG1579 156 AELEELEAEREELAAKI 172
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
897-1097 |
1.15e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 897 ELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQFDDLVSEKDEISREKLEVAQNLEEAHQKIQGLQETIREREATLE 976
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 977 K-----------LHSKN-NELIKQISDLNCDISKEQSSQSLIKESKLKLENEIKRLKDvinsKEEEIKSFNDKLSSSEED 1044
Cdd:COG3883 97 RsggsvsyldvlLGSESfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEA----KLAELEALKAELEAAKAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6321812 1045 LDIKLVTLEKncniamsRLQSLVTENSDLRSKNENFKKEKAALNNQLKNKESE 1097
Cdd:COG3883 173 LEAQQAEQEA-------LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1574-1884 |
1.22e-04 |
|
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: 47.37 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1574 ERLSAVEDrsQYTDEINRLKEELNCSLKAETNLKKEFATLKYKLETSTNDSEAKISDLLKQLDHYTKVVEMLNNEKDAIS 1653
Cdd:TIGR02169 187 ERLDLIID--EKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1654 LAEKELYQKYEALNTECESL-KGKIVSLTKIKQELESDLNQKTDALQISNAALSSSTQKNKEITEKI-KYLEETLQLQME 1731
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIdKLLAEIEELERE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1732 QNSRNGELVKtlqascngYKDKFDDEKQKNIDLYEENQTLQKLNTDLQLQLKNLHERLSDTTEKNAWLSKIHELENMVSL 1811
Cdd:TIGR02169 345 IEEERKRRDK--------LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ 416
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321812 1812 ETDLKYEEMK-KNKSLERAVEELQTKNSQQTDVIELANKNRSEFEEATLKYEAQISDLEKYISQQELEMKKSIR 1884
Cdd:TIGR02169 417 RLSEELADLNaAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1491-1666 |
1.36e-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: 45.30 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1491 DLQGNELRLREHIHALKQAEEDVKNMASIIEKLKTQ--NKQKEKLIWEREMERNDSDMQLQETLLE-----LKRVQDVK- 1562
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARleAAKTELEDLEKEIKRLELEIEEVEARIKkyeeqLGNVRNNKe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1563 -KILSDDLAHLKERLSAVEDR-SQYTDEINRLKEELNCSLKAETNLKKEFATLKYKLETSTNDSEAKISDLLKQLDHYTK 1640
Cdd:COG1579 91 yEALQKEIESLKRRISDLEDEiLELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
170 180
....*....|....*....|....*.
gi 6321812 1641 VVemlnnekdaislaEKELYQKYEAL 1666
Cdd:COG1579 171 KI-------------PPELLALYERI 183
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
856-1516 |
1.56e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 856 SSNDMTRTKKFNEQINKLKNDLQEMESKKKFLEEKNQ------KTVNELENTQDLLNQEKENLRKNESLLNRVKTSS--E 927
Cdd:TIGR00606 418 QSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEelkfviKELQQLEGSSDRILELDQELRKAERELSKAEKNSltE 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 928 TLQKQFDDLVSEKDEISREKLEVAQNLEEAHQKIQGLQET--IREREATLEKLHSKNN-----ELIKQISDLNCDISKEQ 1000
Cdd:TIGR00606 498 TLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMemLTKDKMDKDEQIRKIKsrhsdELTSLLGYFPNKKQLED 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1001 SSQSLIKESKL-------------KLENEIKRLKDVINSKEEEIKSFNDKL--SSSEEDLDIKLVTLEKN---------- 1055
Cdd:TIGR00606 578 WLHSKSKEINQtrdrlaklnkelaSLEQNKNHINNELESKEEQLSSYEDKLfdVCGSQDEESDLERLKEEieksskqram 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1056 ----CNIAMSRLQSLVTENSDLRSKNENFKKEKAALNNQLKNKESELLKMKEKIDNHKKELATFSKQRDDAVSEHGKITA 1131
Cdd:TIGR00606 658 lagaTAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQS 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1132 ELKETRIQLTEYKSNYQKIKEEYSNFQRETKEQEqkkrnSLVESLNDSkiKELEARLSQEISLNQYLNKRISgnSVETNI 1211
Cdd:TIGR00606 738 IIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQE-----TLLGTIMPE--EESAKVCLTDVTIMERFQMELK--DVERKI 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1212 SSTRRSTSYSDDPLDKEDIIKKYYDLQLAFTEITRNLE----------NEIEEKKNLISRLRFTETRLASSSFEDQKIKA 1281
Cdd:TIGR00606 809 AQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIElnrkliqdqqEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEE 888
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1282 QMKKLKKLIQDMDPSIP------------LDSILNEPLDNCPDKESDINKLMLEVDYLKRQLDIETRAHYDAENAISALH 1349
Cdd:TIGR00606 889 QLVELSTEVQSLIREIKdakeqdspletfLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK 968
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1350 SKFRKiQGESSLSSSDIyklKFEASEERVKSLEDKLKTMPLRDRTNLPVGDIIKNRDSISKYEEEIRyyklenyKLQEIL 1429
Cdd:TIGR00606 969 DDYLK-QKETELNTVNA---QLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELK-------EVEEEL 1037
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1430 NESNGKLSQltLDLRQSKSKEALLSEQLDRLQKDLESTERQKELLSSTIKQQKQQFENcmDDLQGNELRLREHIHALKQA 1509
Cdd:TIGR00606 1038 KQHLKEMGQ--MQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE--PQFRDAEEKYREMMIVMRTT 1113
|
....*..
gi 6321812 1510 EEDVKNM 1516
Cdd:TIGR00606 1114 ELVNKDL 1120
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
870-1566 |
1.60e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 870 INKLKNDLQEMESKKkflEEKNQKTVNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQFDDLVSEKDEISR---- 945
Cdd:TIGR00606 410 AAQLCADLQSKERLK---QEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKaere 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 946 -EKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNE-------------LIKQISDLNCDISKEQSSQSLIKESKL 1011
Cdd:TIGR00606 487 lSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQlnhhtttrtqmemLTKDKMDKDEQIRKIKSRHSDELTSLL 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1012 KLENEIKRLKDVINSKEEEIKSFNDKLSsseeDLDIKLVTLEKNCNIAMSRLQSLVTENSDLrsknenfkKEKAALNNQL 1091
Cdd:TIGR00606 567 GYFPNKKQLEDWLHSKSKEINQTRDRLA----KLNKELASLEQNKNHINNELESKEEQLSSY--------EDKLFDVCGS 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1092 KNKESELLKMKEKIDNHKKELA----------TFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQKIKEEYSNFQRET 1161
Cdd:TIGR00606 635 QDEESDLERLKEEIEKSSKQRAmlagatavysQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKST 714
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1162 KEQEQKKRNSLVE------------SLNDSKIKELEARLSQEISLNQYLNKRISGNsvETNISSTRRSTSYSDDPLDKED 1229
Cdd:TIGR00606 715 ESELKKKEKRRDEmlglapgrqsiiDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ--ETLLGTIMPEEESAKVCLTDVT 792
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1230 IIKKyydLQLAFTEITRNLENEIEEKKNLISRLRFTETR--LASSSFEDQKIKAQMKKLKKLIQDMDPSIP-LDSILNE- 1305
Cdd:TIGR00606 793 IMER---FQMELKDVERKIAQQAAKLQGSDLDRTVQQVNqeKQEKQHELDTVVSKIELNRKLIQDQQEQIQhLKSKTNEl 869
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1306 ---------PLDNCPDKESDINKLMLEVDYLKRQLDietrahyDAENAISALHSKFRKIQGESSLSSSdiyklkfeASEE 1376
Cdd:TIGR00606 870 kseklqigtNLQRRQQFEEQLVELSTEVQSLIREIK-------DAKEQDSPLETFLEKDQQEKEELIS--------SKET 934
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1377 RVKSLEDKLKTMPLRdrtnlpVGDIIKNRDSISKYEEEIRyyklENYKLQEILNesngkLSQLTLDLRQSKSKEALLSEQ 1456
Cdd:TIGR00606 935 SNKKAQDKVNDIKEK------VKNIHGYMKDIENKIQDGK----DDYLKQKETE-----LNTVNAQLEECEKHQEKINED 999
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1457 LDRLQKDLESTERQKELLSSTIKQQKQ-------QFENCMDDLQGNELRLREHIHALKQAEEDVKNMASIIEKLKTQNK- 1528
Cdd:TIGR00606 1000 MRLMRQDIDTQKIQERWLQDNLTLRKRenelkevEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKg 1079
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 6321812 1529 -QKEKLIWEREM---ERNDSDMQLQETLLELKRVQDVKKILS 1566
Cdd:TIGR00606 1080 yEKEIKHFKKELrepQFRDAEEKYREMMIVMRTTELVNKDLD 1121
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
864-1033 |
1.66e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 864 KKFNEQINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLRKNESLL-NRVKTSSET-----------LQK 931
Cdd:COG3883 33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgERARALYRSggsvsyldvllGSE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 932 QFDDLVSEKDEISREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQSLIKESKL 1011
Cdd:COG3883 113 SFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
170 180
....*....|....*....|..
gi 6321812 1012 KLENEIKRLKDVINSKEEEIKS 1033
Cdd:COG3883 193 AAEAQLAELEAELAAAEAAAAA 214
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1532-1745 |
1.85e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1532 KLIWEREMERNDSDMQLQETLLELKRVQDVKKILSDDLAHLKERLSAVEDR-SQYTDEINRLKEELNCSLKAETNLKKEF 1610
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1611 ATLKYKLetstndseAKISDLLKQLDHYTKVVEMLNNE--KDAISLAE------KELYQKYEALNTECESLKGKIVSLTK 1682
Cdd:COG4942 100 EAQKEEL--------AELLRALYRLGRQPPLALLLSPEdfLDAVRRLQylkylaPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321812 1683 IKQELESDLNQKTDALQISNAALSSSTQKNKEITEKIKYLEETLQLQMEQNSRNGELVKTLQA 1745
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1370-1899 |
1.95e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1370 KFEASEERVKSLEDKLKTMPLRDRtnlpvGDIIKNRDSISKYEEEIRYYKLENYKLQEILNESNGKLSQLTLDLRQSKSK 1449
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKK-----AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1450 EAllsEQLDRLQKDLESTERQKELLSSTIKQQKQQfencmDDLQGNELRLREHIHALKQAEEdvKNMASIIEKLKTQNKQ 1529
Cdd:PTZ00121 1389 EK---KKADEAKKKAEEDKKKADELKKAAAAKKKA-----DEAKKKAEEKKKADEAKKKAEE--AKKADEAKKKAEEAKK 1458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1530 KEKLIWEREMERNDSDMQlqetllelKRVQDVKKilSDDLAHLKERLSAVEDRSQYTDEINRLKEELNcslKAETNLKKE 1609
Cdd:PTZ00121 1459 AEEAKKKAEEAKKADEAK--------KKAEEAKK--ADEAKKKAEEAKKKADEAKKAAEAKKKADEAK---KAEEAKKAD 1525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1610 FATlkyKLETSTNDSEAKISDLLKQLDHYTKVVEMLN-NEKDAISLAEKELYQKYEALNTECESLKGKIVSLTKIKQELE 1688
Cdd:PTZ00121 1526 EAK---KAEEAKKADEAKKAEEKKKADELKKAEELKKaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1689 SDLNQKTDALQISNAALSSSTQKNKEitEKIKYLEETLQLQMEQNSRNGELVKTLQASCN----GYKDKFDDEKQKNIDL 1764
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKA--EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaaEEAKKAEEDKKKAEEA 1680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1765 YEENQTLQKLNTDLQLQ------LKNLHERLSDTTEKNAWLSKIHElENMVSLETDLKYEEMKKNKSLERAVEELQTKNS 1838
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEaeeakkAEELKKKEAEEKKKAEELKKAEE-ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI 1759
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321812 1839 QQtdvieLANKNRSEFEEATLKYEAQISD-LEKYISQQELEMKKSIRDNSSYRDKVQEMAQE 1899
Cdd:PTZ00121 1760 AH-----LKKEEEKKAEEIRKEKEAVIEEeLDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
867-1033 |
1.96e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 867 NEQINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQ------------------EKENLRKNESLLNRVKTSSET 928
Cdd:COG4942 68 ARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 929 LQKQFDDLVSEKDEISREKlevaQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDlncDISKEQSSQSLIKE 1008
Cdd:COG4942 148 RREQAEELRADLAELAALR----AELEAERAELEALLAELEEERAALEALKAERQKLLARLEK---ELAELAAELAELQQ 220
|
170 180
....*....|....*....|....*
gi 6321812 1009 SKLKLENEIKRLKDVINSKEEEIKS 1033
Cdd:COG4942 221 EAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
864-989 |
2.41e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 864 KKFNEQINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQFDDLVSEKdei 943
Cdd:PRK12704 64 EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQ--- 140
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 6321812 944 sREKLEVAQNL--EEAHQKIqgLQETirEREATLEKLHsknneLIKQI 989
Cdd:PRK12704 141 -LQELERISGLtaEEAKEIL--LEKV--EEEARHEAAV-----LIKEI 178
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
905-1192 |
2.79e-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: 45.97 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 905 LNQEKENLRKNESLLNRVKTSSETLQKQFDDlvsekdeiSREKLEV-AQNLEEAHQKIQGLQETIREREATLEKLHSKNN 983
Cdd:pfam10174 291 IDQLKQELSKKESELLALQTKLETLTNQNSD--------CKQHIEVlKESLTAKEQRAAILQTEVDALRLRLEEKESFLN 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 984 ELIKQISDLNCDISKEQSSQS------LIKESKLK-LENEIKRLKDVINSKEEEIKSFNDKLSSSEED---LDIKLVTLE 1053
Cdd:pfam10174 363 KKTKQLQDLTEEKSTLAGEIRdlkdmlDVKERKINvLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDssnTDTALTTLE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1054 KncniAMS-------RLQ--------SLVTENSDLRSKNENFKKEKAALNNQLKNKESELLKMKE----------KIDNH 1108
Cdd:pfam10174 443 E----ALSekeriieRLKeqreredrERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEhasslassglKKDSK 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1109 KKELATFSKQRDDAVS----EHGKI-TAELKET-------RIQLTEYKSNYQkiKEEYSNFQRET-------KEQEQKKr 1169
Cdd:pfam10174 519 LKSLEIAVEQKKEECSklenQLKKAhNAEEAVRtnpeindRIRLLEQEVARY--KEESGKAQAEVerllgilREVENEK- 595
|
330 340
....*....|....*....|...
gi 6321812 1170 nslveSLNDSKIKELEARLSQEI 1192
Cdd:pfam10174 596 -----NDKDKKIAELESLTLRQM 613
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
1631-1814 |
2.99e-04 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 45.75 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1631 LLKQLDHYTKVVEMLNNEKD---AISLAEKELYQKyEALNTECESLKGKIVSLTKIKQELESDLNQKTDALQISNA---- 1703
Cdd:PRK10361 21 LFASYQHAQQKAEQLAEREEmvaELSAAKQQITQS-EHWRAECELLNNEVRSLQSINTSLEADLREVTTRMEAAQQhadd 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1704 ---ALSSSTQKNKEITEKI--KYLEETLQLQMEQN--SRNGeLVKTLQASCNGYK----DKFDDEKQKNIDLYEENQTLQ 1772
Cdd:PRK10361 100 kirQMINSEQRLSEQFENLanRIFEHSNRRVDEQNrqSLNS-LLSPLREQLDGFRrqvqDSFGKEAQERHTLAHEIRNLQ 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6321812 1773 KLNTDLQLQLKNLHERLS-DTTEKNAW-------------LSKIHELENMVSLETD 1814
Cdd:PRK10361 179 QLNAQMAQEAINLTRALKgDNKTQGNWgevvltrvleasgLREGYEYETQVSIEND 234
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1447-1907 |
3.08e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1447 KSKEALLSEQLDrlqkdLESTERQKELLSSTIKQQKQQFENcMDDLQGNELRLREHIHALKQAEEDVKNMASIIEKlktq 1526
Cdd:PRK01156 149 AQRKKILDEILE-----INSLERNYDKLKDVIDMLRAEISN-IDYLEEKLKSSNLELENIKKQIADDEKSHSITLK---- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1527 nkQKEKLIWEREMERNDSDMqLQETLLELKRVQDVKKILSDDLAHLKERLSAVEDRSQYTDEIN-RLKEELNCSLKAETN 1605
Cdd:PRK01156 219 --EIERLSIEYNNAMDDYNN-LKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEeRHMKIINDPVYKNRN 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1606 LKKEFATLKYKLE-------------TSTNDSEAKISDLLKQLDHYTKV---VEMLNNEKDAIslaeKELYQKYEALNTE 1669
Cdd:PRK01156 296 YINDYFKYKNDIEnkkqilsnidaeiNKYHAIIKKLSVLQKDYNDYIKKksrYDDLNNQILEL----EGYEMDYNSYLKS 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1670 CESLKGKIVSLTKIKQELESDLNQKTDALQIS----NAALSSSTQKNKEITEKIKYLEE---TLQLQMEQNSRNGELVKT 1742
Cdd:PRK01156 372 IESLKKKIEEYSKNIERMSAFISEILKIQEIDpdaiKKELNEINVKLQDISSKVSSLNQrirALRENLDELSRNMEMLNG 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1743 lQASCNGYKDKFDDEKQKNI------DLYEENQTLQKLNTDLQ------LQLKNLHERLSD------TTEKNAWLSKIHE 1804
Cdd:PRK01156 452 -QSVCPVCGTTLGEEKSNHIinhyneKKSRLEEKIREIEIEVKdidekiVDLKKRKEYLESeeinksINEYNKIESARAD 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1805 LENMVSLETDLKYEEMKKNKSLER----AVEELQTKNSQ------QTDVIELANkNRSEFEEATlkyeAQISDLEKYISQ 1874
Cdd:PRK01156 531 LEDIKIKINELKDKHDKYEEIKNRykslKLEDLDSKRTSwlnalaVISLIDIET-NRSRSNEIK----KQLNDLESRLQE 605
|
490 500 510
....*....|....*....|....*....|....
gi 6321812 1875 QELEmkksIRDNSSYRDK-VQEMAQEIEFWKSRY 1907
Cdd:PRK01156 606 IEIG----FPDDKSYIDKsIREIENEANNLNNKY 635
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1657-1888 |
3.11e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1657 KELYQKYEALNTECESLKGKIVSLTKIKQELESDLNQKTDALQISNAALSSSTQKNKEITEKIKYLEETLQlqmEQNSRN 1736
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE---AQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1737 GELVKTLQASCNGYKDKFDDEKQKNIDLYEENQTLQKLNTDLQLQLKNLHERLSDTTEKNAWLSKIHElenmvSLETDLK 1816
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA-----ELEALLA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321812 1817 yeemkknkSLERAVEELQTKNSQQTDVIELANKNRSEFEEATLKYEAQISDLEKYISQQELEMKKSIRDNSS 1888
Cdd:COG4942 182 --------ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
927-1170 |
3.15e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 927 ETLQKQFDDLVSEKDEIS--REKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQIsdlncdiskeqssqs 1004
Cdd:COG4913 228 DALVEHFDDLERAHEALEdaREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--------------- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1005 likesklkLENEIKRLKDVINSKEEEIksfnDKLSSSEEDLDIKLVTLEKNCNiamsrlqslvteNSDLRSKnENFKKEK 1084
Cdd:COG4913 293 --------LEAELEELRAELARLEAEL----ERLEARLDALREELDELEAQIR------------GNGGDRL-EQLEREI 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1085 AALNNQLKNKESELLKMKEKIDN----HKKELATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQKIKEEYSNFQRE 1160
Cdd:COG4913 348 ERLERELEERERRRARLEALLAAlglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
250
....*....|
gi 6321812 1161 TKEQEQKKRN 1170
Cdd:COG4913 428 IASLERRKSN 437
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1456-1658 |
3.33e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.45 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1456 QLDRLQKDLESTERqkellssTIKQQKQQFENCMDDLQGNE-------LRLREHIHALKQAEEDVKNMASIIEKLKTQNK 1528
Cdd:PRK11637 48 QLKSIQQDIAAKEK-------SVRQQQQQRASLLAQLKKQEeaisqasRKLRETQNTLNQLNKQIDELNASIAKLEQQQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1529 QKEKLIWERemerndSDM---QLQETLLELkrvqdvkkILSDDLAHLKERLSAV-----EDRSQYTDEINRLKEELNCSL 1600
Cdd:PRK11637 121 AQERLLAAQ------LDAafrQGEHTGLQL--------ILSGEESQRGERILAYfgylnQARQETIAELKQTREELAAQK 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321812 1601 KAETNLKKEFATLKY-------KLETSTNDSEAKISDLLKQLDH-YTKVVEMLNNE---KDAISLAEKE 1658
Cdd:PRK11637 187 AELEEKQSQQKTLLYeqqaqqqKLEQARNERKKTLTGLESSLQKdQQQLSELRANEsrlRDSIARAERE 255
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1008-1547 |
3.39e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.50 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1008 ESKLKLENEIKRLKDVINSKEEEIKSFNDKLSSSEEDLDI---KLVTLEKNCNIAMSRLQSLVTENSDLRSKNENFKKEK 1084
Cdd:pfam05557 6 ESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDResdRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1085 AALNNQLKNKESELLKMKEKIDNHKKELATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQKIKEEYSNFQRETKEQ 1164
Cdd:pfam05557 86 EALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1165 eqkkrnslveSLNDSKIKELEARLSQEISlnqylnkrisgNSVETNISSTRRSTSYsddplDKEDIIKKYYDLQLAFTEI 1244
Cdd:pfam05557 166 ----------AEAEQRIKELEFEIQSQEQ-----------DSEIVKNSKSELARIP-----ELEKELERLREHNKHLNEN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1245 TRNLENEIEEKKNLISRL-RFTETR--LASSSFEDQKIKAQMKKLKKLIQDMDPSIP--------LDSILNEPLdNCPDK 1313
Cdd:pfam05557 220 IENKLLLKEEVEDLKRKLeREEKYReeAATLELEKEKLEQELQSWVKLAQDTGLNLRspedlsrrIEQLQQREI-VLKEE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1314 ESDINKLMLEVDYLKRQLDIETRAHY----DAENAISALHSKFRKIQGESSLSSSDIYKLKfeaseERVKSLEDKL---K 1386
Cdd:pfam05557 299 NSSLTSSARQLEKARRELEQELAQYLkkieDLNKKLKRHKALVRRLQRRVLLLTKERDGYR-----AILESYDKELtmsN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1387 TMPLRDRTNLPVGDII---KNRDSISKYEEEIRYYKLENYKLQ-EILNESNGKLSQLTLDLRQSKSKEAL--LSEQLDRL 1460
Cdd:pfam05557 374 YSPQLLERIEEAEDMTqkmQAHNEEMEAQLSVAEEELGGYKQQaQTLERELQALRQQESLADPSYSKEEVdsLRRKLETL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1461 QKDLESTERQKELLSSTIKQQ------------------------KQQFENCMDDLQGNELRLREHIHALKQAEEDVKNM 1516
Cdd:pfam05557 454 ELERQRLREQKNELEMELERRclqgdydpkktkvlhlsmnpaaeaYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRL 533
|
570 580 590
....*....|....*....|....*....|.
gi 6321812 1517 ASIIEKLktqnKQKEKLIWEREMERNDSDMQ 1547
Cdd:pfam05557 534 PETTSTM----NFKEVLDLRKELESAELKNQ 560
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
857-1020 |
3.45e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 857 SNDMTRTKKF-NEQINKLKNDLQEMESK-KKF--------LEEKNQKTVNELENTQDLLNQEKENLRKNESLLNRVK--- 923
Cdd:COG3206 170 REEARKALEFlEEQLPELRKELEEAEAAlEEFrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRaql 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 924 -----TSSETLQ-KQFDDLVSEKDEISREKLEVAQNLEEAHQKIQGLQETIREREATLEKlhsknnELIKQISDLNCDIS 997
Cdd:COG3206 250 gsgpdALPELLQsPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQ------EAQRILASLEAELE 323
|
170 180
....*....|....*....|...
gi 6321812 998 KEQSSQSLIKESKLKLENEIKRL 1020
Cdd:COG3206 324 ALQAREASLQAQLAQLEARLAEL 346
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1012-1153 |
3.67e-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: 44.15 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1012 KLENEIKRLKDVINSKEEEIKSFNDKLSSSEEDLDIKLVTLEKNcniamSRLQSLVTENSDLrsknENFKKEKAALNNQL 1091
Cdd:COG1579 35 ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY-----EEQLGNVRNNKEY----EALQKEIESLKRRI 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321812 1092 KNKESELLKMKEKIDNHKKELATFSKQRDDAVSEHGKITAELKEtriQLTEYKSNYQKIKEE 1153
Cdd:COG1579 106 SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE---ELAELEAELEELEAE 164
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
858-1054 |
3.96e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 858 NDMTRTKKFNEQINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLRKNESLLnrvktssETLQKQFDDLV 937
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI-------ESLAAEIEELE 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 938 SEKDEISREklevaqnLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQSLIKESKLKLENEI 1017
Cdd:TIGR02168 866 ELIEELESE-------LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6321812 1018 KRLKDVINSK----EEEIKSFNDKLSSSEEDLDIKLVTLEK 1054
Cdd:TIGR02168 939 DNLQERLSEEysltLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
846-1111 |
5.04e-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: 45.10 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 846 LFIRIKPLLTSSNDMT-RTKKFNEQINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLR----KNESLLN 920
Cdd:pfam05483 497 LLLENKELTQEASDMTlELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKckldKSEENAR 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 921 RVKTSSETLQKQFDDLVSEKDEISREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISK-E 999
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEiI 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1000 QSSQSLIKESKLKLENEIKRLKDVINSKEEEIKSFNDKLSSSEEDLDIKLVTLEKNCNIAMSRLQSLVTENSDLRSKNEN 1079
Cdd:pfam05483 657 DNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQE 736
|
250 260 270
....*....|....*....|....*....|..
gi 6321812 1080 FKKEKAALNNQLKNKESELLKMKEKIDNHKKE 1111
Cdd:pfam05483 737 QSSAKAALEIELSNIKAELLSLKKQLEIEKEE 768
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
869-1054 |
5.43e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 869 QINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQFDDLVSEKDEISRE-- 946
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 947 -------KLEV---AQNLEEAHQKIQglqetirereaTLEKLHSKNNELIKQISDLNCDISKEQSSQSLIKESKLKLENE 1016
Cdd:COG3883 97 rsggsvsYLDVllgSESFSDFLDRLS-----------ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 6321812 1017 IKRLKDVINSKEEEIKSFNDKLSSSEEDLDIKLVTLEK 1054
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1505-1792 |
5.44e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1505 ALKQAEEDVKNMASIIEKLKTQNKQKEKliwerEMERNDSDMQLQETLLELKRVQDVKKilsdDLAHLKERLS-AVEDRS 1583
Cdd:PRK11281 27 ARAASNGDLPTEADVQAQLDALNKQKLL-----EAEDKLVQQDLEQTLALLDKIDRQKE----ETEQLKQQLAqAPAKLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1584 QYTDEINRLKEELNcslkaeTNLKKEFATLKYK-LETSTNDSEAKISDLLKQLDHYtkvvemlNNEkdAISL------AE 1656
Cdd:PRK11281 98 QAQAELEALKDDND------EETRETLSTLSLRqLESRLAQTLDQLQNAQNDLAEY-------NSQ--LVSLqtqperAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1657 KELY---QKYEALNTECESLK--GKIVSLTKIKQ--------ELESDLNQKTdaLQISNAALSSSTQKNKEITEKIKYLE 1723
Cdd:PRK11281 163 AALYansQRLQQIRNLLKGGKvgGKALRPSQRVLlqaeqallNAQNDLQRKS--LEGNTQLQDLLQKQRDYLTARIQRLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1724 ETLQ-LQMEQNSRNGEL----VKTLQASCNGYKDKFD----DEKQKNIDLYEE--NQTlQKLNTDLQ--LQLKNLHERLS 1790
Cdd:PRK11281 241 HQLQlLQEAINSKRLTLsektVQEAQSQDEAARIQANplvaQELEINLQLSQRllKAT-EKLNTLTQqnLRVKNWLDRLT 319
|
..
gi 6321812 1791 DT 1792
Cdd:PRK11281 320 QS 321
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1616-1895 |
6.79e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1616 KLEtSTNDSEAKISDLL----KQLDHYTKVVEM------LNNEKDAISLA-----EKELYQKYEALNTECESLKGKIVSL 1680
Cdd:TIGR02168 180 KLE-RTRENLDRLEDILneleRQLKSLERQAEKaerykeLKAELRELELAllvlrLEELREELEELQEELKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1681 TKIKQELESDLNQKTDALQISNAALSSSTQKNKEITEKIKYLEETLQLQMEQnsrngelVKTLQASCNGYKDKFDDEKQK 1760
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER-------LANLERQLEELEAQLEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1761 NIDLYEENQTLQKLNTDLQLQLKNLHERLsdtteknawlskihelenmvsletdlkyeemkknKSLERAVEELQTKNSQQ 1840
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAEL----------------------------------EELEAELEELESRLEEL 377
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 6321812 1841 TDVIELANKNRSEFEEATLKYEAQISDLEKYISQQELEMKKSIRDNSSYRDKVQE 1895
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1372-1876 |
7.15e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.65 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1372 EASEERVKSLEDKLKtmPLRDRTNlpvgDIIKNRDSISKYEEEIRYY---KLENYKLQEILNESNGKLSQLT-------L 1441
Cdd:TIGR00606 234 ESSREIVKSYENELD--PLKNRLK----EIEHNLSKIMKLDNEIKALksrKKQMEKDNSELELKMEKVFQGTdeqlndlY 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1442 DLRQSKSKEAllSEQLDRLQKDLESTERQKELLSstikQQKQQFENCMDDLQGNELRLREHIHALK--------QAEEDV 1513
Cdd:TIGR00606 308 HNHQRTVREK--ERELVDCQRELEKLNKERRLLN----QEKTELLVEQGRLQLQADRHQEHIRARDsliqslatRLELDG 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1514 KNMASIIEKlktQNKQKEKLIWERE------MERNDSDMQLQETLLE--LKRVQDVKKILSDDLAHLKERLSAVEDRSQy 1585
Cdd:TIGR00606 382 FERGPFSER---QIKNFHTLVIERQedeaktAAQLCADLQSKERLKQeqADEIRDEKKGLGRTIELKKEILEKKQEELK- 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1586 tdeiNRLKEELNCSLKAETNLKKEFATLKYKLETSTNDSEAKISDLLKQldhytkvVEMLNNEKDAISLAEKELYQKYEA 1665
Cdd:TIGR00606 458 ----FVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKE-------VKSLQNEKADLDRKLRKLDQEMEQ 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1666 LNTECESLKgKIVSLTKIK----QELESDLNQKTDAL-----------QISNAALSSSTQKNKEITEKIKYLEETLQLQM 1730
Cdd:TIGR00606 527 LNHHTTTRT-QMEMLTKDKmdkdEQIRKIKSRHSDELtsllgyfpnkkQLEDWLHSKSKEINQTRDRLAKLNKELASLEQ 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1731 EQNSRNGELvKTLQASCNGYKDKF------DDEKQKNIDLYEENQTLQKLNTDLQLQLKNLHERLSDTTEKNAWLSK--- 1801
Cdd:TIGR00606 606 NKNHINNEL-ESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPvcq 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1802 ------------IHELENMVSLETDLKYEEMKKNKSLERAVEELQTKNSQQTDVIELANKNRSEFEEATLKYEAQISDLE 1869
Cdd:TIGR00606 685 rvfqteaelqefISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK 764
|
....*..
gi 6321812 1870 KYISQQE 1876
Cdd:TIGR00606 765 NDIEEQE 771
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
847-1047 |
7.30e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 7.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 847 FIRIKPLLTSSNDMTRTKKFNEQINKLKNDLQEMESKKKFLEEKnqktVNELENTQDLLNQEKENLRKNESLlnrvkTSS 926
Cdd:PRK05771 65 YLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEE----ISELENEIKELEQEIERLEPWGNF-----DLD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 927 ETLQKQFDDLVSEKDEISREKLEVAQNLEEahqkiQGLQETIRERE-------ATLEKLHSKNNELIKQISDLNCDISKE 999
Cdd:PRK05771 136 LSLLLGFKYVSVFVGTVPEDKLEELKLESD-----VENVEYISTDKgyvyvvvVVLKELSDEVEEELKKLGFERLELEEE 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6321812 1000 QSSQSLIKEsklkLENEIKRLKDVINSKEEEIKSFNDK----LSSSEEDLDI 1047
Cdd:PRK05771 211 GTPSELIRE----IKEELEEIEKERESLLEELKELAKKyleeLLALYEYLEI 258
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
883-1546 |
7.81e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 7.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 883 KKKFLEEKNQktVNELENTQDLLNQEKENLRKNESLLNRVKTS-------SETLQKQFDDLVSEKDEISREKLEVAQNLE 955
Cdd:PRK01156 151 RKKILDEILE--INSLERNYDKLKDVIDMLRAEISNIDYLEEKlkssnleLENIKKQIADDEKSHSITLKEIERLSIEYN 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 956 EAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISK-------EQSSQSLIKESKLKLENEIK---RLKDVIN 1025
Cdd:PRK01156 229 NAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKnnyykelEERHMKIINDPVYKNRNYINdyfKYKNDIE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1026 SKEEEIKSFNDKLSSSEEDLDiKLVTLEKNCN---IAMSRLQSLVTENSDLRSKNENFkkekaalNNQLKNKESELLKMK 1102
Cdd:PRK01156 309 NKKQILSNIDAEINKYHAIIK-KLSVLQKDYNdyiKKKSRYDDLNNQILELEGYEMDY-------NSYLKSIESLKKKIE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1103 EKIDNHKKELATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQKIKEEYSNFqRETKEQEQKKRNSLV--------- 1173
Cdd:PRK01156 381 EYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRAL-RENLDELSRNMEMLNgqsvcpvcg 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1174 ESLNDSKIKELEARLSQEISlnqYLNKRISGNSVE-TNISSTRRSTSYSDDPLDKEDIIKkyydlQLAFTEITRNLENEI 1252
Cdd:PRK01156 460 TTLGEEKSNHIINHYNEKKS---RLEEKIREIEIEvKDIDEKIVDLKKRKEYLESEEINK-----SINEYNKIESARADL 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1253 EEKKNLISRLRFTETRLasssfedQKIKAQMKKLKklIQDMDPSIPLDSILNEPLDNCpdkesDINKLMLEVDYLKRQLD 1332
Cdd:PRK01156 532 EDIKIKINELKDKHDKY-------EEIKNRYKSLK--LEDLDSKRTSWLNALAVISLI-----DIETNRSRSNEIKKQLN 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1333 ietrahyDAENAISALHSKFRKIQgesSLSSSDIYKLkfeasEERVKSLEDKLKtmplrdrtnlpvgDIIKNRDSISKYE 1412
Cdd:PRK01156 598 -------DLESRLQEIEIGFPDDK---SYIDKSIREI-----ENEANNLNNKYN-------------EIQENKILIEKLR 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1413 EEIRYYKLENYKLQEI---LNESNGKLSQLTLDLRQSKSkeallseQLDRLQKDLESTERQKELLSSTIKQQKQQFENCM 1489
Cdd:PRK01156 650 GKIDNYKKQIAEIDSIipdLKEITSRINDIEDNLKKSRK-------ALDDAKANRARLESTIEILRTRINELSDRINDIN 722
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321812 1490 DDLQGNElRLREHIHALKQAEE--DVKNMASIIEKLKTQ--NKQKEKLIWEREMERNDSDM 1546
Cdd:PRK01156 723 ETLESMK-KIKKAIGDLKRLREafDKSGVPAMIRKSASQamTSLTRKYLFEFNLDFDDIDV 782
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
907-1885 |
9.96e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 907 QEKENLRKNESLLnRVKTSSETLQKQFDDLVSEKDEISREKLEVAQNLeeahqkiQGLQETIREREATLEKLHSKNNELI 986
Cdd:pfam01576 3 QEEEMQAKEEELQ-KVKERQQKAESELKELEKKHQQLCEEKNALQEQL-------QAETELCAEAEEMRARLAARKQELE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 987 KQISDLNCDISKEQssqslikESKLKLENEIKRLKDVINSKEEEIksfnDKLSSSEEDLDIKLVTLEkncniamSRLQSL 1066
Cdd:pfam01576 75 EILHELESRLEEEE-------ERSQQLQNEKKKMQQHIQDLEEQL----DEEEAARQKLQLEKVTTE-------AKIKKL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1067 VTENSDLRSKNENFKKEKAALNNQLKNKESELLKMKEKIDNhkkelatFSKQRDDAVSEHGKITAELKETRIQLTEYKSN 1146
Cdd:pfam01576 137 EEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKS-------LSKLKNKHEAMISDLEERLKKEEKGRQELEKA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1147 YQKIKEEYSNFQRETKEQEQkkrnslveslndsKIKELEARLSQEISLNQYLNKRIsgnsvetnisstrrstsySDDPLD 1226
Cdd:pfam01576 210 KRKLEGESTDLQEQIAELQA-------------QIAELRAQLAKKEEELQAALARL------------------EEETAQ 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1227 KEDIIKKYYDLQLAFTEITRNLENEieekknlisrlrftetRLASSSFEDQKikaqmkklKKLIQDMDpsiPLDSILNEP 1306
Cdd:pfam01576 259 KNNALKKIRELEAQISELQEDLESE----------------RAARNKAEKQR--------RDLGEELE---ALKTELEDT 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1307 LDNCPDKESDINKLMLEVDYLKRQLDIETRAHydaenaisalhskfrkiqgESSLssSDIYKLKFEASEERVKSLEdKLK 1386
Cdd:pfam01576 312 LDTTAAQQELRSKREQEVTELKKALEEETRSH-------------------EAQL--QEMRQKHTQALEELTEQLE-QAK 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1387 tmplRDRTNLPvgdiiKNRDSISKyeeeiryyklENYKLQEILNesngKLSQLTLDLRQSKSKealLSEQLDRLQKDLES 1466
Cdd:pfam01576 370 ----RNKANLE-----KAKQALES----------ENAELQAELR----TLQQAKQDSEHKRKK---LEGQLQELQARLSE 423
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1467 TERQKELLSSTIKQQKQQFENC---MDDLQGNELRLREHIHALKQAEEDVKnmasiiEKLKTQNKQKEKL---IWEREME 1540
Cdd:pfam01576 424 SERQRAELAEKLSKLQSELESVsslLNEAEGKNIKLSKDVSSLESQLQDTQ------ELLQEETRQKLNLstrLRQLEDE 497
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1541 RNDSDMQLQEtllELKRVQDVKKILSDDLAHLKERLSAVEDRSQYTDEINRLKEELNCSLKAETNLKKEFATLKYKLETS 1620
Cdd:pfam01576 498 RNSLQEQLEE---EEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKT 574
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1621 TNDSEAKISDLLKQLDHYTKVV-----------EMLNNEKdAISLAEKELYQKYEALNTECESlkgKIVSLTKikqELEs 1689
Cdd:pfam01576 575 KNRLQQELDDLLVDLDHQRQLVsnlekkqkkfdQMLAEEK-AISARYAEERDRAEAEAREKET---RALSLAR---ALE- 646
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1690 dlnqktdalqisnaalssstqknkEITEKIKYLEET---LQLQMEQ--NSRN--GELVKTLQASCNGYKDKFDDEKQKNI 1762
Cdd:pfam01576 647 ------------------------EALEAKEELERTnkqLRAEMEDlvSSKDdvGKNVHELERSKRALEQQVEEMKTQLE 702
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1763 DLYEENQTLQ--KLNTDLQLQ-LKNLHER-LSDTTEKN-----AWLSKIHELENMVSLETDLKYEEMKKNKSLERAVEEL 1833
Cdd:pfam01576 703 ELEDELQATEdaKLRLEVNMQaLKAQFERdLQARDEQGeekrrQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKEL 782
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|..
gi 6321812 1834 QTKnsqqtdvIELANKNRSEFEEATLKYEAQISDLekyisQQELEMKKSIRD 1885
Cdd:pfam01576 783 EAQ-------IDAANKGREEAVKQLKKLQAQMKDL-----QRELEEARASRD 822
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1058-1293 |
1.01e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1058 IAMSRLQSLVTENSDLRSKNENFKKEKAALNNQLKNKESELLKMKEKIDNHKKELATFSKQRDDAVSEHGKITAELKETR 1137
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1138 IQLTEYKSNYQKIKEEYSNFQRETkeQEQKKRNSLVESLNDSKIKELEARLSQEISLNQYLNKRIsgnsveTNISSTRRS 1217
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRAL--YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA------EELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321812 1218 TSYSDDPLDKEDIIKKyyDLQLAFTEITRNLENEIEEKKNLISRLrftETRLASSSFEDQKIKAQMKKLKKLIQDM 1293
Cdd:COG4942 162 LAALRAELEAERAELE--ALLAELEEERAALEALKAERQKLLARL---EKELAELAAELAELQQEAEELEALIARL 232
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
860-1161 |
1.26e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 43.48 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 860 MTRTKKFNEQINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQFDDL--- 936
Cdd:pfam05701 34 VERRKLVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQDSELAKLRVEEMeqg 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 937 -VSEKDEISREKLEVAQ--------NLEEAHQKIQGLQE----TIREREATLEKLH---SKNNELIKQISDLN------- 993
Cdd:pfam05701 114 iADEASVAAKAQLEVAKarhaaavaELKSVKEELESLRKeyasLVSERDIAIKRAEeavSASKEIEKTVEELTieliatk 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 994 ---------CDISKEQS-SQSLIKES-KLKLENEIKRLkdvinskEEEIKSFNDKLSSSeEDLDIKLVTlekncniAMSR 1062
Cdd:pfam05701 194 eslesahaaHLEAEEHRiGAALAREQdKLNWEKELKQA-------EEELQRLNQQLLSA-KDLKSKLET-------ASAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1063 LQSLvteNSDLRSKNENFKKEKAALNNQLKNKESELlkmKEKIDNHKKELATFSKQRDDAvsehgkiTAELKETRIQLTE 1142
Cdd:pfam05701 259 LLDL---KAELAAYMESKLKEEADGEGNEKKTSTSI---QAALASAKKELEEVKANIEKA-------KDEVNCLRVAAAS 325
|
330 340
....*....|....*....|
gi 6321812 1143 YKSNYQKIKEEYSNF-QRET 1161
Cdd:pfam05701 326 LRSELEKEKAELASLrQREG 345
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1661-1878 |
1.39e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1661 QKYEALNTECESLKGKIVSLTKIKQELESDLNQKTDALQISNAALSSSTQKNKEITEKIKYLEETLQLQMEQNSRNGELV 1740
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1741 KTLQA--SCNGYKDKFDdekqkNIDLYeenQTLQKLNTDLQLQLKNLHERLSDTTEKNAwlSKIHELEnmvsletdlkye 1818
Cdd:COG3883 103 SYLDVllGSESFSDFLD-----RLSAL---SKIADADADLLEELKADKAELEAKKAELE--AKLAELE------------ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1819 emKKNKSLERAVEELQTKNSQQTDVIELANKNRSEFEEATLKYEAQISDLEKYISQQELE 1878
Cdd:COG3883 161 --ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
876-1065 |
1.40e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.82 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 876 DLQEMESKKKFLEEKNQKTVNELENTQDLLnQEKENLRKNE--SLLNRVKTSSETLQKQFDDLVSEKDEISREKLEVAQN 953
Cdd:pfam09787 48 ELEELRQERDLLREEIQKLRGQIQQLRTEL-QELEAQQQEEaeSSREQLQELEEQLATERSARREAEAELERLQEELRYL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 954 LEEAHQKIQGLQETIREREATLEKLhsKNNELIKQISDlncdiskeqSSQSlikesklKLENEIKRLKDVINSKEEEIKS 1033
Cdd:pfam09787 127 EEELRRSKATLQSRIKDREAEIEKL--RNQLTSKSQSS---------SSQS-------ELENRLHQLTETLIQKQTMLEA 188
|
170 180 190
....*....|....*....|....*....|..
gi 6321812 1034 fndkLSSSEEDLDIKLVTLEKncniAMSRLQS 1065
Cdd:pfam09787 189 ----LSTEKNSLVLQLERMEQ----QIKELQG 212
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1525-1746 |
1.42e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1525 TQNKQKEKLIWEREMERNDSDMQLQETLLELKRVQDVKKILSDDLAHLKERLSAVEDrsqytdEINRLKEELNcslKAET 1604
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA------EIAEAEAEIE---ERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1605 NLKKEFATLkYKLETSTNDSEA-----KISDLLKQLDHYTKVVEMLNNEKDAISLAEKELYQKYEALNTECESLKGKIVS 1679
Cdd:COG3883 87 ELGERARAL-YRSGGSVSYLDVllgseSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321812 1680 LTKIKQELESDLNQKTDALQISNAALSSSTQKNKEITEKIKYLEETLQLQMEQNSRNGELVKTLQAS 1746
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1388-1728 |
1.54e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 43.69 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1388 MPLRDRTNLPVGDIiknRDSISKYEEEIRYYKLENYKLQE-ILNESNGKLSQlTLDLRQSKSKEAL-LSEQLDRLQKDLE 1465
Cdd:PLN03229 421 MKKREAVKTPVREL---EGEVEKLKEQILKAKESSSKPSElALNEMIEKLKK-EIDLEYTEAVIAMgLQERLENLREEFS 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1466 STERQKELLSSTIKQQkqqFENCMDDLQ------GNELRLREHIHALKQAEEDVKNM--ASIIEKLKTQNKQKEKLIWER 1537
Cdd:PLN03229 497 KANSQDQLMHPVLMEK---IEKLKDEFNkrlsraPNYLSLKYKLDMLNEFSRAKALSekKSKAEKLKAEINKKFKEVMDR 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1538 EmerndsdmQLQETLLELK-RVQDVKKILSDDL-AHLKERLSAVEDRSQYtdEINRLKEELNCSLKAETNLKKEFAT--- 1612
Cdd:PLN03229 574 P--------EIKEKMEALKaEVASSGASSGDELdDDLKEKVEKMKKEIEL--ELAGVLKSMGLEVIGVTKKNKDTAEqtp 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1613 ---LKYKLETSTNDSEAKISDLLKQLDHYTKVVEMLNNEKDAISLAEKELYQKYEALNTECESLKGKIVSLTKIKQELEs 1689
Cdd:PLN03229 644 ppnLQEKIESLNEEINKKIERVIRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALNSSELKEKFE- 722
|
330 340 350
....*....|....*....|....*....|....*....
gi 6321812 1690 DLNQKTDALQISNAALSSSTQKNKEITEKIKYLEETLQL 1728
Cdd:PLN03229 723 ELEAELAAARETAAESNGSLKNDDDKEEDSKEDGSRVEV 761
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1661-1901 |
1.60e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1661 QKYEALNTECESLKGKIVSLTKIKQELESDLNQKTDALQISNAALSSSTQKNKEITEKIKYLEETL-QLQMEQNSRNGEL 1739
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1740 vktlqascngykdkfddEKQKNiDLYEENQTLQKLNTDLQLQLKNLHERLSDTTEKNAWLSKIheLENMVSLETDLKyee 1819
Cdd:COG4942 100 -----------------EAQKE-ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL--APARREQAEELR--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1820 mKKNKSLERAVEELQTKNSQQTDVIELANKNRSEFEEATLKYEAQISDLEKYISQQELEMKKSIRDNSSYRDKVQEMAQE 1899
Cdd:COG4942 157 -ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
..
gi 6321812 1900 IE 1901
Cdd:COG4942 236 AA 237
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
871-1090 |
1.67e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.50 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 871 NKLKNDLQEMESKKKfleeKNQ-KTVNELENTQDLLNQEKENL---RKNESLLNRVKTSSETLQKQFDDLVSEK------ 940
Cdd:PRK10929 26 KQITQELEQAKAAKT----PAQaEIVEALQSALNWLEERKGSLeraKQYQQVIDNFPKLSAELRQQLNNERDEPrsvppn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 941 ---DEISREKLEV-AQNLEEAHQkIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQSLIKESKLK-LEN 1015
Cdd:PRK10929 102 mstDALEQEILQVsSQLLEKSRQ-AQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTaLQA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1016 EIKRLKDVINSKEEEIKSFNDK----------LSSSEEDLDIKLVTLEKNCNI--------AMSRLQSLVTENSDL-RSK 1076
Cdd:PRK10929 181 ESAALKALVDELELAQLSANNRqelarlrselAKKRSQQLDAYLQALRNQLNSqrqreaerALESTELLAEQSGDLpKSI 260
|
250
....*....|....*..
gi 6321812 1077 NENFKKEK---AALNNQ 1090
Cdd:PRK10929 261 VAQFKINRelsQALNQQ 277
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1447-1643 |
1.76e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1447 KSKEALLSEQLDRLQKDLESTERQKELLSSTIKQQKQQFENC---------MDDLQG--NEL-RLREHIHALKQAEEDVK 1514
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdEIDVASaeREIaELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1515 NMASIIEKLKTQNKQKEKLIWEREMERNDSDMQLQETLLELKRVQDV-----KKILSDDLAHLKERLSAVED-------R 1582
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleaaeDLARLELRALLEERFAAALGdaverelR 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321812 1583 SQYTDEINRLKEELNcslKAETNLKKEFATLKYKLETSTNDSEAKISDLLKQLDHYTKVVE 1643
Cdd:COG4913 769 ENLEERIDALRARLN---RAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEE 826
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
863-1171 |
1.83e-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: 43.29 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 863 TKKFNEQINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQFDD-LVSEKD 941
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKaLAERKD 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 942 --EISREKLEVAQNLEEAHQK--IQGLQETIRE-REATLEKLHSKNNELIKQISDLNCDISKEQSS-QSLIKESKLKLEN 1015
Cdd:pfam12128 679 saNERLNSLEAQLKQLDKKHQawLEEQKEQKREaRTEKQAYWQVVEGALDAQLALLKAAIAARRSGaKAELKALETWYKR 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1016 EIKRL---KDVINSKEEEIKSFNDKLSSSEED-----------------LDIKLVTLEKNCNIAMSRL-QSLVTENSDLR 1074
Cdd:pfam12128 759 DLASLgvdPDVIAKLKREIRTLERKIERIAVRrqevlryfdwyqetwlqRRPRLATQLSNIERAISELqQQLARLIADTK 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1075 SKNENFKKEKAALNNQLKNKESELLKMKEKIdnhkKELATFSKQRDDAVSEHgkitaELKETRIQLTEYKSNYQKIKEEY 1154
Cdd:pfam12128 839 LRRAKLEMERKASEKQQVRLSENLRGLRCEM----SKLATLKEDANSEQAQG-----SIGERLAQLEDLKLKRDYLSESV 909
|
330
....*....|....*..
gi 6321812 1155 SNFQRETKEQEQKKRNS 1171
Cdd:pfam12128 910 KKYVEHFKNVIADHSGS 926
|
|
| COG5644 |
COG5644 |
U3 small nucleolar RNA-associated protein 14 [Function unknown]; |
860-1186 |
1.93e-03 |
|
U3 small nucleolar RNA-associated protein 14 [Function unknown];
Pssm-ID: 227931 [Multi-domain] Cd Length: 869 Bit Score: 43.15 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 860 MTRTKKFNEQINKLKNDLQEMESKKKFLEEKNQKTVNElentqDLLNQEKENLRKNESLLNRVKTSSETlqkqfddlvse 939
Cdd:COG5644 385 MFREERKAKRVAKIKSKTYRKIRKNRKEKEMALIPKSE-----DLENEKSEEARALERMTQRHKNTSSW----------- 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 940 kdeiSREKLEVAQNLEEAHQKIQglqETIREREATLEKLHSKN---NELIKQISDLNCDISKEQSSQSLIKESKLKLEN- 1015
Cdd:COG5644 449 ----TRKMLERASHGEGTREAVN---EQIRKGDELMQRIHGKEimdGEDVSEFSDSDYDTNEQVSTAFEKIRNEEELKGv 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1016 -EIKRLKDVINSKEEEIKSFNDKLSSSEEDLDIKLVTLEK--NCNIAMSRLQSLVTENSD------LRSKNENFKKEKAA 1086
Cdd:COG5644 522 lGMKFMRDASNRQMAASKISVADLVKVENGDDIDVGELDEvgGDAIYANAGRREVFPVVEqrrklaPRKRKEDFVTPSTS 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1087 LNNQL------KNKESELLKMKEKIDNHKKELATFSKQRDDAVSEHGKITAelKETRIQlteyKSNYQKIKEEYSNFQRE 1160
Cdd:COG5644 602 LEKSMdrilhgQKKRAEGAVVFEKPLEATENFNPWLDRKMRRIKRIKKKAY--RRIRRD----KRLKKKMPEEENTQENH 675
|
330 340
....*....|....*....|....*.
gi 6321812 1161 TKEQEQKKRNSlveslNDSKIKELEA 1186
Cdd:COG5644 676 LGSEKKRHGGV-----PDILLKEIEV 696
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1243-1901 |
1.98e-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: 43.50 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1243 EITRNLENEIEEKKNLISRLRFTETRLASSSFEDQKIKAQMKKLKKLIQDMDPSIPLDSilnepLDNCPDKESDI-NKLM 1321
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDG-----FERGPFSERQIkNFHT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1322 LEVDYLKRQLDIETRAHYDAENAISALHSKFRKIQGESSLSSSDIyKLKFEASEERVKSLEDKLKTMplrDRTNLPVGDI 1401
Cdd:TIGR00606 398 LVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTI-ELKKEILEKKQEELKFVIKEL---QQLEGSSDRI 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1402 IKNRDSISKYEEEIRyyKLENYKLQEILNESNGKLSQLTLDLRQSKSKEALLSEQLDR---LQKDLESTERQKELLSSTI 1478
Cdd:TIGR00606 474 LELDQELRKAERELS--KAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHhttTRTQMEMLTKDKMDKDEQI 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1479 KQQKQQFENCMDDLQG---NELRLREHIHAL----KQAEEDVKNMASIIEKLKTQNKQKEKliweREMERNDSDMQLQET 1551
Cdd:TIGR00606 552 RKIKSRHSDELTSLLGyfpNKKQLEDWLHSKskeiNQTRDRLAKLNKELASLEQNKNHINN----ELESKEEQLSSYEDK 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1552 LLELKRVQDvkkiLSDDLAHLKERLS-AVEDR----------SQYTDEINRLKEELNCSLKAETNLKKEFATLKYKLETS 1620
Cdd:TIGR00606 628 LFDVCGSQD----EESDLERLKEEIEkSSKQRamlagatavySQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSK 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1621 T-------NDSEAKISDLLKQLDHYTKVVEMLNNEKDAISLAEKELYQKYEALNTECeslkgkivsltkikQELESDLNQ 1693
Cdd:TIGR00606 704 LrlapdklKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDI--------------QRLKNDIEE 769
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1694 KTDALQISNAALSSSTQKNKEITekikyLEETLQLQMEQNSRN-GELVKTLQA-----SCNGYKDKFDDEKQKNIDLYEE 1767
Cdd:TIGR00606 770 QETLLGTIMPEEESAKVCLTDVT-----IMERFQMELKDVERKiAQQAAKLQGsdldrTVQQVNQEKQEKQHELDTVVSK 844
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1768 NQTLQKLNTDLQLQLKNLHERLSDTteknawlsKIHELENMVSLETDLKYEEMKKNKSLEraVEELQTKNSQQtdviela 1847
Cdd:TIGR00606 845 IELNRKLIQDQQEQIQHLKSKTNEL--------KSEKLQIGTNLQRRQQFEEQLVELSTE--VQSLIREIKDA------- 907
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 6321812 1848 nKNRSEFEEATLKYEAQisDLEKYISQQELEMKKSirdnssyRDKVQEMAQEIE 1901
Cdd:TIGR00606 908 -KEQDSPLETFLEKDQQ--EKEELISSKETSNKKA-------QDKVNDIKEKVK 951
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
927-1119 |
2.12e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 927 ETLQKQFDDLVSEKDEISREKLEVAQNLEEAHQKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDI---SKEQSSQ 1003
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELeklEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1004 SLIKESKlKLENEIKRLKDVINSKEEEIKSFNDkLSSSEEDLDIKLVTLEKNCNIAMSRLqSLVTEN--SDLRSKNENFK 1081
Cdd:COG4717 129 PLYQELE-ALEAELAELPERLEELEERLEELRE-LEEELEELEAELAELQEELEELLEQL-SLATEEelQDLAEELEELQ 205
|
170 180 190
....*....|....*....|....*....|....*...
gi 6321812 1082 KEKAALNNQLKNKESELLKMKEKIDNHKKELATFSKQR 1119
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1412-1631 |
2.14e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1412 EEEIRYYKLENYKLQEILNESNGKLSQLTLDLRQSKSKEALLSEQLDRLQKDLESTERQKELLSstikqqKQQFEncmdd 1491
Cdd:pfam07888 58 EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALL------AQRAA----- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1492 lqgNELRLREHIHALKQAEEDVKNMASIIEKLKTQNKQKEKLIWEREMERNDSDMQLQETLLELKRvqdvkkiLSDDLAH 1571
Cdd:pfam07888 127 ---HEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRS-------LSKEFQE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321812 1572 LKERLSAVEDRS-QYTDEINRLKEELNCSLKAETN---LKKEFATLKYKLETSTNDSEAKISDL 1631
Cdd:pfam07888 197 LRNSLAQRDTQVlQLQDTITTLTQKLTTAHRKEAEneaLLEELRSLQERLNASERKVEGLGEEL 260
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
890-1186 |
2.52e-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: 42.80 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 890 KNQKTVNELENT-------QDLLNQEKENLRKNESLLNRVKTSSETLQKQFDDLVSEKDEISREKLEVAQNLEEAHQKIQ 962
Cdd:pfam17380 279 QHQKAVSERQQQekfekmeQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 963 GLQ-ETIREREAT--------LEKLH---SKNNELIKQisDLncdisKEQSSQSLIKESKLKLENEIKRLKDVINSKEEE 1030
Cdd:pfam17380 359 KRElERIRQEEIAmeisrmreLERLQmerQQKNERVRQ--EL-----EAARKVKILEEERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1031 IKSFNDKLSSSEEDLDIKLVTLEKncniaMSRLQSLvtenSDLRSKNENFKKEKAALNNQLKNK-----------ESELL 1099
Cdd:pfam17380 432 ARQREVRRLEEERAREMERVRLEE-----QERQQQV----ERLRQQEEERKRKKLELEKEKRDRkraeeqrrkilEKELE 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1100 KMKEKI---DNHKKELATFSKQRDDAVSEHG--KITAELKETRIQLTEYKSNYQKIK---EEYSNFqrETKEQEQKKRNS 1171
Cdd:pfam17380 503 ERKQAMieeERKRKLLEKEMEERQKAIYEEErrREAEEERRKQQEMEERRRIQEQMRkatEERSRL--EAMEREREMMRQ 580
|
330
....*....|....*
gi 6321812 1172 LVESlnDSKIKELEA 1186
Cdd:pfam17380 581 IVES--EKARAEYEA 593
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1232-1744 |
2.64e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1232 KKYYDLQLAFTEITRNLENEIEEKKNLISRLRFTETRLASSSFEDQKIKAQMKKLKKLIQDMDPSIPLDSILNEPLDNCP 1311
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1312 DKESDINKLMLEVDYLKRQLDietrahydaenAISALHSKFRKIQGESSLSSSDIYKLKFEASE-ERVKSLEDKLKTMPL 1390
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIK-----------ELEEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEELERLKK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1391 RdRTNLPVGDIIKNRDSISKYEEEIRyykLENYKLQEILNESNGKLSQLTL---DLRQSKSKEALLSEQLDRlqkdlest 1467
Cdd:PRK03918 380 R-LTGLTPEKLEKELEELEKAKEEIE---EEISKITARIGELKKEIKELKKaieELKKAKGKCPVCGRELTE-------- 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1468 ERQKELLSSTIKqqkqqfencmdDLQGNELRLREHIHALKQAEEDVKNMASIIEKLKTQNKQKEKLIWEREMERNDSDMQ 1547
Cdd:PRK03918 448 EHRKELLEEYTA-----------ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYN 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1548 LQEtlleLKRVQDVKKILSDDLAHLKERLSAVEDRSQYTDEINRLKEELNCSLKaetNLKKEFATLKYKLETSTNDSEAK 1627
Cdd:PRK03918 517 LEE----LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD---ELEEELAELLKELEELGFESVEE 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1628 ISDLLKQLD-HYTKVVEMLNNEKD------AISLAEKELYQKYEALN---TECESLKGKIVSLTKIKQELE-SDLNQKTD 1696
Cdd:PRK03918 590 LEERLKELEpFYNEYLELKDAEKElereekELKKLEEELDKAFEELAeteKRLEELRKELEELEKKYSEEEyEELREEYL 669
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 6321812 1697 ALQISNAALSSSTQKNKEITEKIKYLEETLQLQMEQNSRNGELVKTLQ 1744
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
897-1204 |
3.35e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.53 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 897 ELEN-TQDLLNQEKENLRKNESLLNRVktsSETLQKQFDDLVSEKDEisreklevAQNLEEahqKIQGLQETIREREATL 975
Cdd:PLN03229 437 EVEKlKEQILKAKESSSKPSELALNEM---IEKLKKEIDLEYTEAVI--------AMGLQE---RLENLREEFSKANSQD 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 976 EKLHSKNNELIKQISD-LNCDISKEQSSQSLikESKLKLENEIKRLKDVI--NSKEEEIKS-FNDKLSSSEEDLDIKLVT 1051
Cdd:PLN03229 503 QLMHPVLMEKIEKLKDeFNKRLSRAPNYLSL--KYKLDMLNEFSRAKALSekKSKAEKLKAeINKKFKEVMDRPEIKEKM 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1052 LEKNCNIAMSRLQSLVTENSDLRSKNENFKKE-KAALNNQLKNKESELLKMKekidnhKKELATFSKQRDDAVSE----- 1125
Cdd:PLN03229 581 EALKAEVASSGASSGDELDDDLKEKVEKMKKEiELELAGVLKSMGLEVIGVT------KKNKDTAEQTPPPNLQEkiesl 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1126 HGKITAELkETRIQLTEYKSNYQKIKEEY----SNFQRETKEQ----EQKKRNSLVESLNDSKIKELEARLSQEISLNQY 1197
Cdd:PLN03229 655 NEEINKKI-ERVIRSSDLKSKIELLKLEVakasKTPDVTEKEKiealEQQIKQKIAEALNSSELKEKFEELEAELAAARE 733
|
....*..
gi 6321812 1198 LNKRISG 1204
Cdd:PLN03229 734 TAAESNG 740
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1419-1789 |
3.46e-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: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1419 KLENykLQEILNESNGKLSQL-----TLDLRQSKSKEAL------LSEQ---LDRLQKDLESTERQKELLSSTIKQQKQQ 1484
Cdd:pfam10174 402 KIEN--LQEQLRDKDKQLAGLkervkSLQTDSSNTDTALttleeaLSEKeriIERLKEQREREDRERLEELESLKKENKD 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1485 FENCMDDLQGNelrLREHIHALKQAEEDVKNMASIIEKLKTQNKQKEKLIWEREMERNDSDMQLQETLlELKRVQDVKKI 1564
Cdd:pfam10174 480 LKEKVSALQPE---LTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH-NAEEAVRTNPE 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1565 LSDDLAHLKErlsavedrsqytdEINRLKEElncSLKAETNLKKEFATLKyKLETSTNDSEAKISDL----LKQLDHYTK 1640
Cdd:pfam10174 556 INDRIRLLEQ-------------EVARYKEE---SGKAQAEVERLLGILR-EVENEKNDKDKKIAELesltLRQMKEQNK 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1641 VV---EMLNNEKDAISLAEKELYQKYEALNTECES---LKGKIVSLTKIKQELESdLNQKTDALQISNAalSSSTQKNKE 1714
Cdd:pfam10174 619 KVaniKHGQQEMKKKGAQLLEEARRREDNLADNSQqlqLEELMGALEKTRQELDA-TKARLSSTQQSLA--EKDGHLTNL 695
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321812 1715 ITEKIKYLEETLQLQMEqnsrngelvkTLQASCNgykdkfddEKQKNIDLYEENQTLQKLNTDLQLQLKNLHERL 1789
Cdd:pfam10174 696 RAERRKQLEEILEMKQE----------ALLAAIS--------EKDANIALLELSSSKKKKTQEEVMALKREKDRL 752
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
866-1055 |
3.56e-03 |
|
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: 41.54 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 866 FNEQInKLKNDLQEMESKKKFLEEKNQKTVN---ELENTQDLLNQEKENLRKNESLLNRVKtssETLQKQFDDLVSEKDE 942
Cdd:smart00787 115 MDKQF-QLVKTFARLEAKKMWYEWRMKLLEGlkeGLDENLEGLKEDYKLLMKELELLNSIK---PKLRDRKDALEEELRQ 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 943 ISREKLEVAQNLEEAHQKiqgLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQSLIKESKLKLENEIKRLKD 1022
Cdd:smart00787 191 LKQLEDELEDCDPTELDR---AKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
170 180 190
....*....|....*....|....*....|...
gi 6321812 1023 VINSKEEEIKsfnDKLSSSEEDLDIKLVTLEKN 1055
Cdd:smart00787 268 FTFKEIEKLK---EQLKLLQSLTGWKITKLSGN 297
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
863-1044 |
3.70e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.13 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 863 TKKFNEQINKLKNDLQEMESKKKFLEEKN-QKTVNELENTQDLLNQEKENLR------KNESLLNRVKTSSETLQKQFD- 934
Cdd:PRK04778 225 QTELPDQLQELKAGYRELVEEGYHLDHLDiEKEIQDLKEQIDENLALLEELDldeaeeKNEEIQERIDQLYDILEREVKa 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 935 --DLVSEKDEISREKLEVAQNLEEAHQKIQGLQE--TIRERE-ATLEKLHSKNNELIKQISDLNCDISKEQSSQSLIKEs 1009
Cdd:PRK04778 305 rkYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQsyTLNESElESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQE- 383
|
170 180 190
....*....|....*....|....*....|....*
gi 6321812 1010 klKLENEIKRLKDVinskEEEIKSFNDKLSSSEED 1044
Cdd:PRK04778 384 --ELEEILKQLEEI----EKEQEKLSEMLQGLRKD 412
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1438-1695 |
3.89e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 42.35 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1438 QLTLDLRQSKS-KEALLSEQLDRLQKDLESTERQKELLsstikQQKQQFENCMDDLQGNELRLREHIHALKQaeedvkNM 1516
Cdd:PRK10929 27 QITQELEQAKAaKTPAQAEIVEALQSALNWLEERKGSL-----ERAKQYQQVIDNFPKLSAELRQQLNNERD------EP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1517 ASIIEKLKTQNKQKEKLiweremerndsdmQLQETLLELKRV----QDVKKILSDDLAHLKERLSavEDRSQYTDEINRL 1592
Cdd:PRK10929 96 RSVPPNMSTDALEQEIL-------------QVSSQLLEKSRQaqqeQDRAREISDSLSQLPQQQT--EARRQLNEIERRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1593 K----------EELNCSLKAETNLKK------EFATLkykleTSTNDSE-AKI-SDLLK----QLDHYTKVVE-MLNNEK 1649
Cdd:PRK10929 161 QtlgtpntplaQAQLTALQAESAALKalvdelELAQL-----SANNRQElARLrSELAKkrsqQLDAYLQALRnQLNSQR 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 6321812 1650 DaiSLAEKELYqKYEALNTECESLKGKIVSLTKIKQELESDLNQKT 1695
Cdd:PRK10929 236 Q--REAERALE-STELLAEQSGDLPKSIVAQFKINRELSQALNQQA 278
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
656-683 |
3.92e-03 |
|
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: 40.02 E-value: 3.92e-03
10 20
....*....|....*....|....*...
gi 6321812 656 SSRHREQQITLLNQLASTHPHFVRCIIP 683
Cdd:cd01363 143 FEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1372-1904 |
3.93e-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: 42.12 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1372 EASEERVKSLEDKLKTMPLRDRTNLPVGDIIKNRDSISKYEEEIRYYKLENYKLQEILNESNGKLSQLTLDLRQSKSKEA 1451
Cdd:pfam10174 40 ELKKERALRKEEAARISVLKEQYRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1452 LLSEQLDRLQKDLESTERQKELLSSTIKQQKQ----QFENC-----MDDLQGNELRLREHIHALKQ----AEEDVKNMAS 1518
Cdd:pfam10174 120 RLQSEHERQAKELFLLRKTLEEMELRIETQKQtlgaRDESIkklleMLQSKGLPKKSGEEDWERTRriaeAEMQLGHLEV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1519 IIEKLKTQNKQ-KEKLIWEREMERNDSDMQLQETLLELK-----RVQDVKKILSDDLAHLK-----------ERLSAVED 1581
Cdd:pfam10174 200 LLDQKEKENIHlREELHRRNQLQPDPAKTKALQTVIEMKdtkisSLERNIRDLEDEVQMLKtngllhtedreEEIKQMEV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1582 RSQYTD----EINRLKEELNcslKAETnlkkEFATLKYKLETSTN---DSEAKIsDLLKQldhytkvvemlnnekdaiSL 1654
Cdd:pfam10174 280 YKSHSKfmknKIDQLKQELS---KKES----ELLALQTKLETLTNqnsDCKQHI-EVLKE------------------SL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1655 AEKElyQKYEALNTECESLKGKIvsltkikQELESDLNQKTDALQisnaalsSSTQKNKEITEKIKYLEETLQLQMEQns 1734
Cdd:pfam10174 334 TAKE--QRAAILQTEVDALRLRL-------EEKESFLNKKTKQLQ-------DLTEEKSTLAGEIRDLKDMLDVKERK-- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1735 rngelVKTLQASCNGYKDKFDDEKQKNIDLYEENQTLQKLNTDLQLQLKNLHERLSDTTEKNAWLSKIHELENMVSLEtd 1814
Cdd:pfam10174 396 -----INVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLE-- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1815 lKYEEMKK-NKSLERAVEELQT-KNSQQTDVIELANKNRSeFEEATLKYEAQISDLEKYISQ---------------QEL 1877
Cdd:pfam10174 469 -ELESLKKeNKDLKEKVSALQPeLTEKESSLIDLKEHASS-LASSGLKKDSKLKSLEIAVEQkkeecsklenqlkkaHNA 546
|
570 580
....*....|....*....|....*..
gi 6321812 1878 EMkkSIRDNSSYRDKVQEMAQEIEFWK 1904
Cdd:pfam10174 547 EE--AVRTNPEINDRIRLLEQEVARYK 571
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
865-1161 |
4.64e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 41.09 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 865 KFNEQINKLKNDLQEMESKKKFLEEK----------NQKTVNELENTQDLLNQEKENLRkneSLLNRVKTSSETLQKQFD 934
Cdd:pfam09728 1 KAARELMQLLNKLDSPEEKLAALCKKyaelleemkrLQKDLKKLKKKQDQLQKEKDQLQ---SELSKAILAKSKLEKLCR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 935 DLVSEKDEISREKLEVAQNLEEAHQKI-QGLQETIREREATLEKLHSKNNELIKQISDLncdiskEQSSQSLIKESKLKl 1013
Cdd:pfam09728 78 ELQKQNKKLKEESKKLAKEEEEKRKELsEKFQSTLKDIQDKMEEKSEKNNKLREENEEL------REKLKSLIEQYELR- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1014 ENEIKRLkdvINSKEEEIKSFNDKLSSSEEDLDIKLVTLE-KNCNIAMSRLQSLVTENSDLRSK----NENFKKEKAALN 1088
Cdd:pfam09728 151 ELHFEKL---LKTKELEVQLAEAKLQQATEEEEKKAQEKEvAKARELKAQVQTLSETEKELREQlnlyVEKFEEFQDTLN 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321812 1089 nqlknkesellKMKEKIDNHKKELATFSKQRDDAVSEHGKITAELKETRIQLTEYKSNYQKIKEEYSNFQRET 1161
Cdd:pfam09728 228 -----------KSNEVFTTFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKL 289
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1074-1179 |
4.68e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1074 RSKNENFKKEK--AALNNQLKNKESELLKMKEKIDNHKKELATFSKQRDDAVSEHGKITAE-LKETRIQLTEYKSNYQKI 1150
Cdd:PRK12705 81 REEERLVQKEEqlDARAEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEqARKLLLKLLDAELEEEKA 160
|
90 100
....*....|....*....|....*....
gi 6321812 1151 KEEYSNFQRETKEQEQKKRNSLVESLNDS 1179
Cdd:PRK12705 161 QRVKKIEEEADLEAERKAQNILAQAMQRI 189
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1544-1719 |
4.70e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1544 SDMQLQETLLELKRVQDVKKILSDDLAHLKERLSAVEDR-SQYTDEINRLKEELNcslkaetNLKKEFATLKYKLETStN 1622
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDElAALEARLEAAKTELE-------DLEKEIKRLELEIEEV-E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1623 DSEAKISDLL------KQLDHYTKVVEMLNNEKDAISLAEKELYQKYEALNTECESLKGKivsLTKIKQELESDLNQKTD 1696
Cdd:COG1579 73 ARIKKYEEQLgnvrnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE---LAELEAELEEKKAELDE 149
|
170 180
....*....|....*....|...
gi 6321812 1697 ALQISNAALSSSTQKNKEITEKI 1719
Cdd:COG1579 150 ELAELEAELEELEAEREELAAKI 172
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1086-1795 |
5.00e-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: 41.93 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1086 ALNNQLKNKESELLKMKEKIDNHKKELATfskqrddavsehgkitaelKETRIQLTEYKSNYQKIKEEYSNFQRETKEQE 1165
Cdd:TIGR04523 23 GYKNIANKQDTEEKQLEKKLKTIKNELKN-------------------KEKELKNLDKNLNKDEEKINNSNNKIKILEQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1166 QKKRNSlVESLNDSKIKELEARLSQEISLNQYLNKRISGNSVETNISSTRRSTSYSDDPLDKEDIIKKYYDLqlafTEIT 1245
Cdd:TIGR04523 84 IKDLND-KLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEL----EKLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1246 RNLENEIEEKKNLISRLRFTETRLASSSFEDQKIKAQMKKLKKLIQDMDPSIPLDSILNEPLDNCPDKESDINKlmlEVD 1325
Cdd:TIGR04523 159 NKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKD---NIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1326 YLKRQLDIETRAHYDAENAISALHSKFRKIQGESSLSSSDIyklkfEASEERVKSLEDKLKT--MPLRDRTNLPVGDIIK 1403
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL-----EQNNKKIKELEKQLNQlkSEISDLNNQKEQDWNK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1404 N-RDSISKYEEEIRYYKLENYKLQEILNESNGKLSQLTLDLRQSKSKEALLSEQLDRLQKDLESTERQKELLSSTIKQQK 1482
Cdd:TIGR04523 311 ElKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1483 QQFencmddlqgNELRLRehihaLKQAEEDVKNMASIIEKLKTQNKQKEKLIWEREMERNDsdmqLQETLLELKRVQDVK 1562
Cdd:TIGR04523 391 SQI---------NDLESK-----IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK----NNSEIKDLTNQDSVK 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1563 KILSDDLAHLKERLSavEDRSQYTDEINRLKEELNCSLKAETNLKKEFATLKYKletsTNDSEAKISDLLKQLDHYTKVV 1642
Cdd:TIGR04523 453 ELIIKNLDNTRESLE--TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE----KKELEEKVKDLTKKISSLKEKI 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1643 EMLNNEKDAISLAEKELYQKYEALNTECESLKGKIVSLTKIKQELESDLNQKtdalqisnaalsSSTQKNKEITEKIKYL 1722
Cdd:TIGR04523 527 EKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQK------------SLKKKQEEKQELIDQK 594
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321812 1723 EETLQLQMEQNSRNGELVKTLqascngyKDKFDDEKQKNIDLYEENQTLQKLNTDLQLQLKNLHERLSDTTEK 1795
Cdd:TIGR04523 595 EKEKKDLIKEIEEKEKKISSL-------EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
864-1163 |
5.04e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 864 KKFNEQINKLKNDLQEMESKKKFLEEKNQKTVNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQFDDLVSEKDEI 943
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 944 SREKlevaQNLEEahqKIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQSLIKESKLKLENEIKRLKDV 1023
Cdd:pfam01576 881 QDEK----RRLEA---RIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAK 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1024 INSKEEEIKSfndKLSSSEEDLDIKLVTLEKNCniamsrlqslvtensdlrsknENFKKEKAALNNQLKNKESELLKMKE 1103
Cdd:pfam01576 954 LQEMEGTVKS---KFKSSIAALEAKIAQLEEQL---------------------EQESRERQAANKLVRRTEKKLKEVLL 1009
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1104 KIDNHKKELATFSKQRDdavsehgKITAELKETRIQLTEYKSNYQKIKEEYSNFQRETKE 1163
Cdd:pfam01576 1010 QVEDERRHADQYKDQAE-------KGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDD 1062
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1438-1704 |
5.45e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1438 QLTLDLRQSKSKEAL--LSEQLDRLQKDLESTERQkellsstIKQQKQQfencmddlqgnelrlrehiHALKQAEEDVKn 1515
Cdd:COG3206 163 EQNLELRREEARKALefLEEQLPELRKELEEAEAA-------LEEFRQK-------------------NGLVDLSEEAK- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1516 maSIIEKLKTQNKQKEKLiwerEMERNDSDMQLQETLLELKRVQDVKKILSDD--LAHLKERLSAVED-----RSQYTDE 1588
Cdd:COG3206 216 --LLLQQLSELESQLAEA----RAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAelaelSARYTPN 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1589 ---INRLKEELNcslKAETNLKKEFATLKYKLETSTNDSEAKISDLLKQLDHYtkvvemlnnEKDAISLAEKElyQKYEA 1665
Cdd:COG3206 290 hpdVIALRAQIA---ALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQL---------EARLAELPELE--AELRR 355
|
250 260 270
....*....|....*....|....*....|....*....
gi 6321812 1666 LNTECESLKGKIVSLTKIKQELESDLNQKTDALQISNAA 1704
Cdd:COG3206 356 LEREVEVARELYESLLQRLEEARLAEALTVGNVRVIDPA 394
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
860-1038 |
5.75e-03 |
|
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: 41.55 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 860 MTRTKKFNEQINKLKNDLQEMESKKKFLEEKNQKTVNELEN---TQDLLNQEKENLRKNESLLNRVKTSSETLQKQF--- 933
Cdd:pfam05667 348 ESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVkkkTLDLLPDAEENIAKLQALVDASAQRLVELAGQWekh 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 934 -----DDLVSEKDEISREKLEVAQNLEEahqkIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISKEQSSQSL--I 1006
Cdd:pfam05667 428 rvpliEEYRALKEAKSNKEDESQRKLEE----IKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVSRSAYTRRIleI 503
|
170 180 190
....*....|....*....|....*....|..
gi 6321812 1007 KESKLKLENEIKRLKDVINSKEEEIKSFNDKL 1038
Cdd:pfam05667 504 VKNIKKQKEEITKILSDTKSLQKEINSLTGKL 535
|
|
| MUTSd |
smart00533 |
DNA-binding domain of DNA mismatch repair MUTS family; |
889-1112 |
5.85e-03 |
|
DNA-binding domain of DNA mismatch repair MUTS family;
Pssm-ID: 214710 [Multi-domain] Cd Length: 308 Bit Score: 41.13 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 889 EKNQKTVNELENTQDLLNQEKENLRKN---ESLLNRVKTSSETLQkqfdDLVSEKDEISREKlEVAQNLEEAHQKIQGLQ 965
Cdd:smart00533 35 NERLDAVEELVENPELRQKLRQLLKRIpdlERLLSRIERGRASPR----DLLRLYDSLEGLK-EIRQLLESLDGPLLGLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 966 etireREATLEKLHSKNNELIK-QISDLNCDISKEqssqSLIKESklkLENEIKRLKDVINSKEEEIKSFNDKLsssEED 1044
Cdd:smart00533 110 -----LKVILEPLLELLELLLElLNDDDPLEVNDG----GLIKDG---FDPELDELREKLEELEEELEELLKKE---REE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321812 1045 LDIKLVTLEKNCN----IAMSRLQ-SLVTENSDLRSKNENFKKEKaalNNQLKNKESELLKMKEKIDNHKKEL 1112
Cdd:smart00533 175 LGIDSLKLGYNKVhgyyIEVTKSEaKKVPKDFIRRSSLKNTERFT---TPELKELENELLEAKEEIERLEKEI 244
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1378-1730 |
6.45e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1378 VKSLEDKLKTMPLRDRTNLpvgDIIKNRDSISKYEEEIRYYK--LENYK--LQEILNESNGKLSqltldLRQSKSKEALL 1453
Cdd:PRK11281 62 QQDLEQTLALLDKIDRQKE---ETEQLKQQLAQAPAKLRQAQaeLEALKddNDEETRETLSTLS-----LRQLESRLAQT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1454 SEQLDRLQKDLEST-----------ER-QKELlsSTIKQQKQQFENCMDDLQGNELRLREHIHALKQAEEDVKNMASIIE 1521
Cdd:PRK11281 134 LDQLQNAQNDLAEYnsqlvslqtqpERaQAAL--YANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1522 KLKTQN---------KQKEKLI-WEREMERNDSDMQ----------LQETLLELKRVQDVKKILSDDLahLKERLSAVED 1581
Cdd:PRK11281 212 RKSLEGntqlqdllqKQRDYLTaRIQRLEHQLQLLQeainskrltlSEKTVQEAQSQDEAARIQANPL--VAQELEINLQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1582 RSQY----TDEINRL-------KEELNCSLKAETNLKKEFATLK---------YK----LETSTNDSE--AKISDL-LKQ 1634
Cdd:PRK11281 290 LSQRllkaTEKLNTLtqqnlrvKNWLDRLTQSERNIKEQISVLKgslllsrilYQqqqaLPSADLIEGlaDRIADLrLEQ 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1635 LDhytkvvemLNNEKDAIS-----LAEKELYQKYEALNTECESLKgkivSLTKIKQELESDLNQktdalQISNA-ALSSS 1708
Cdd:PRK11281 370 FE--------INQQRDALFqpdayIDKLEAGHKSEVTDEVRDALL----QLLDERRELLDQLNK-----QLNNQlNLAIN 432
|
410 420
....*....|....*....|...
gi 6321812 1709 TQKN-KEITEKIKYLEETLQLQM 1730
Cdd:PRK11281 433 LQLNqQQLLSVSDSLQSTLTQQI 455
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
864-1125 |
6.50e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 864 KKFNEQINKLKNDLQEMESKKKFL----EEKNQKT---VNELENTQDLLNQEKENLRKNESLLNRVKTSSETLQKQFDDL 936
Cdd:COG1340 18 EELREEIEELKEKRDELNEELKELaekrDELNAQVkelREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 937 VSEKDEISREKLEvaqnLEEAHQKIQGLQETIREREATLEklhsKNNELIKQISDLNCDISKeqssqsliKESKLKLENE 1016
Cdd:COG1340 98 RKELAELNKAGGS----IDKLRKEIERLEWRQQTEVLSPE----EEKELVEKIKELEKELEK--------AKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1017 IKRLKDVINSKEEEIKSFNDKLSSSEEDLDIKLVTLEKncniAMSRLQSLVTENSDLRSKNENFKKEKAALNNQLKNKES 1096
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIE----LYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK 237
|
250 260
....*....|....*....|....*....
gi 6321812 1097 ELLKMKEKIDNHKKELATFSKQRDDAVSE 1125
Cdd:COG1340 238 ELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
868-1098 |
6.69e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 868 EQINKLKNDLQE-MESKKKFLEEKNQ-KTVNELENTQDLLNQEKENLRKNESLLNRVK-----TSSETLQKQFDDLVSEK 940
Cdd:COG4913 225 EAADALVEHFDDlERAHEALEDAREQiELLEPIRELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 941 DEISREKLEVAQNLEEAHQKIQGLQETIRE----REATLEKLHSKNNELIKQISDlncdisKEQSSQSLIKESKLKLENE 1016
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERER------RRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1017 IKRLKDVInskeEEIKSFNDKLSSSEEDLDIKLVTLEKNCNIAMSRLQSLVTENSDLRSKNENFKKE----KAALNNQLK 1092
Cdd:COG4913 379 AEEFAALR----AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARllalRDALAEALG 454
|
....*.
gi 6321812 1093 NKESEL 1098
Cdd:COG4913 455 LDEAEL 460
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
867-1104 |
8.06e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.56 E-value: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 867 NEQINKLKNDLQEMESKkkfLEEKNQKTVNELENTQDLLNQEKENLRKNESLlnRVKTSSETLQKQFDDLVSEKDEIsRE 946
Cdd:pfam15905 93 DKRLQALEEELEKVEAK---LNAAVREKTSLSASVASLEKQLLELTRVNELL--KAKFSEDGTQKKMSSLSMELMKL-RN 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 947 KLEVAQNLEEAHQ-----KIQGLQETIREREATLEKLHSKNNELIKQISDLNCDISK---EQSSQSLIKESKLKLENEIK 1018
Cdd:pfam15905 167 KLEAKMKEVMAKQegmegKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKlleYITELSCVSEQVEKYKLDIA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1019 RLKDVINSKEEEIKSFNDKLSSSE-------EDLDIKLVTLEkncniamSRLQSLVTENsdlRSKNENFKKEKAALNNQL 1091
Cdd:pfam15905 247 QLEELLKEKNDEIESLKQSLEEKEqelskqiKDLNEKCKLLE-------SEKEELLREY---EEKEQTLNAELEELKEKL 316
|
250
....*....|...
gi 6321812 1092 KNKESELLKMKEK 1104
Cdd:pfam15905 317 TLEEQEHQKLQQK 329
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1408-1901 |
9.12e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1408 ISKYEEEIRYYKLENYKLQEILNESNGKLSQLTLDLRQSKSKEALLSEQLDRLQ----------------KDLESTERQK 1471
Cdd:TIGR00606 202 VQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKeiehnlskimkldneiKALKSRKKQM 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1472 ELLSSTIKQQKQQFENCMDDlqgnELRLREHIHAlKQAEEDVKNMASIIEKLKTQNKQKEKLIWER-EMERNDSDMQLQ- 1549
Cdd:TIGR00606 282 EKDNSELELKMEKVFQGTDE----QLNDLYHNHQ-RTVREKERELVDCQRELEKLNKERRLLNQEKtELLVEQGRLQLQa 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1550 -----------------ETLLEL---KRVQDVKKILSDDLAHLKERLSavEDRSQYTDEINRLKEELNCSLKAETNLKKE 1609
Cdd:TIGR00606 357 drhqehirardsliqslATRLELdgfERGPFSERQIKNFHTLVIERQE--DEAKTAAQLCADLQSKERLKQEQADEIRDE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1610 FATLKYKLETSTNDSEAKISDL---LKQLDHYTKVVEMLNNEKDAISLAEKELYQKYEALNTECesLKGKIVSLtkikQE 1686
Cdd:TIGR00606 435 KKGLGRTIELKKEILEKKQEELkfvIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTET--LKKEVKSL----QN 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1687 LESDLNQKTDALQISNAALSSSTQKNKEiTEKIKYLEETLQLQMEQNSRNGELVKTLQASCNGYKDKFDD---EKQKNID 1763
Cdd:TIGR00606 509 EKADLDRKLRKLDQEMEQLNHHTTTRTQ-MEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDwlhSKSKEIN 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1764 LYEENqtLQKLNTDLQLQLKNLHERLSDTTEKNAWLS----KIHELENMVSLETDLK--YEEMKKNKS-----------L 1826
Cdd:TIGR00606 588 QTRDR--LAKLNKELASLEQNKNHINNELESKEEQLSsyedKLFDVCGSQDEESDLErlKEEIEKSSKqramlagatavY 665
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321812 1827 ERAVEELQTKNSQQTDVIELANKNRSEFEEATLKYEAQISDLEKYISQQELEMKKSIRDNSSYRDKVQEMAQEIE 1901
Cdd:TIGR00606 666 SQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIID 740
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1096-1699 |
9.23e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1096 SELLKMKEKIDNHKKELATFSKQRDDAVSEHGKITAELKETRIQlteyksnYQKIKEEYSNFQRETKEQeqkkrNSLVES 1175
Cdd:PRK01156 183 SNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIE-------YNNAMDDYNNLKSALNEL-----SSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1176 LN--DSKIKELEARLSQEISLNQYLNKrisgnsvetniSSTRRSTSYSDDPLDKEDIIKKYYdlqlafteitrNLENEIE 1253
Cdd:PRK01156 251 KNryESEIKTAESDLSMELEKNNYYKE-----------LEERHMKIINDPVYKNRNYINDYF-----------KYKNDIE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1254 EKKNLISRLRFtetrlasssfEDQKIKAQMKKLKKLIQDMDPSIPLDSI---LNEPLDNCPDKESDINKLMLEVDYLKRQ 1330
Cdd:PRK01156 309 NKKQILSNIDA----------EINKYHAIIKKLSVLQKDYNDYIKKKSRyddLNNQILELEGYEMDYNSYLKSIESLKKK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1331 LDietrahydaenaisalhsKFRKIQGESSLSSSDIYKLKFEASEERVKSLEDKLKTMplrDRTNLPVGDIIKNRDSISK 1410
Cdd:PRK01156 379 IE------------------EYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKL---QDISSKVSSLNQRIRALRE 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1411 YEEEIRyyklenyKLQEILNeSNGKLSQLTLDLRQSKSKEAL--LSEQLDRLQKDLESTERQKELLSSTIKQQKQQfenc 1488
Cdd:PRK01156 438 NLDELS-------RNMEMLN-GQSVCPVCGTTLGEEKSNHIInhYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKR---- 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1489 MDDLQGNEL-RLREHIHALKQAEEDVKNMASIIEKLKTQNKQKEKLIWE-REMERNDSDMQLQETLLEL----------- 1555
Cdd:PRK01156 506 KEYLESEEInKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRyKSLKLEDLDSKRTSWLNALavislidietn 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 1556 -KRVQDVKKILSDDLAHLKERLSAVEDRSQYTDE-INRLKEELNcSLKAETNLKKEFATLKYKLETSTNDSEAKISDLLK 1633
Cdd:PRK01156 586 rSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKsIREIENEAN-NLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDS 664
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321812 1634 QLDHYTKVVEMLNNEKDAISLAEKELyqkyEALNTECESLKGKIVSLTKIKQELESDLNQKTDALQ 1699
Cdd:PRK01156 665 IIPDLKEITSRINDIEDNLKKSRKAL----DDAKANRARLESTIEILRTRINELSDRINDINETLE 726
|
|
| PRK12595 |
PRK12595 |
bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed |
928-1024 |
9.99e-03 |
|
bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed
Pssm-ID: 183614 [Multi-domain] Cd Length: 360 Bit Score: 40.34 E-value: 9.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321812 928 TLQKQFDDLVSEKDEISREKLE-------VAQNLEEAHQKiQGLQ--ETIREREaTLEKLHSKNN---------ELIKQI 989
Cdd:PRK12595 1 MMNEELEQLRKEIDEINLQLLEllskrgeLVQEIGEEKTK-QGTKryDPVRERE-MLDMIAENNEgpfedstiqHLFKEI 78
|
90 100 110
....*....|....*....|....*....|....*
gi 6321812 990 SDLNCDISKEQSSQSLIKESKLKLENEIKRLKDVI 1024
Cdd:PRK12595 79 FKASLELQEDDNRKALLVSRKKKPEDTIVDVKGEV 113
|
|
|