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Conserved domains on  [gi|6321812|ref|NP_011888|]
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myosin 1 [Saccharomyces cerevisiae S288C]

Protein Classification

MYSc_class_II and Smc domain-containing protein( domain architecture ID 12837882)

MYSc_class_II and Smc domain-containing protein

Graphical summary

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List of domain hits

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
Smc super family cl34174
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];


The actual alignment was detected with superfamily member COG1196:

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
 
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
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
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 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
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
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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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