NCBI Conserved Domain Search

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

820-1042

1.58e-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: 1.58e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  820 AARKELQYRQQTKAAVIIQSYCRSYLAHSQYMGLKKA-AITTQCAWRGRLARRELRKLK--------MAAKETGALQAAK 890
Cdd:TIGR02168  702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLeAEVEQLEERIAQLSKELTELEaeieeleeRLEEAEEELAEAE 781

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  891 ---NKLEKQVEELTWRLQLEKRMRVDMEEAKSQENKKLQQKLQELELQSNETKDLLKR----EQETAKAAWEKAALVPEV 963
Cdd:TIGR02168  782 aeiEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRledlEEQIEELSEDIESLAAEI 861

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  964 QVDTTLVNELTAENEKLKTLVASLE--------------TKIDETEQRFDEVKKAREELLKKATDAESKINGLTNTMLSL 1029
Cdd:TIGR02168  862 EELEELIEELESELEALLNERASLEealallrseleelsEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941

                          250
                   ....*....|....*.
gi 1002244077 1030 QEKLTN---MELENQV 1042
Cdd:TIGR02168  942 QERLSEeysLTLEEAE 957

PTZ00121

MAEBL; Provisional

872-1018

2.45e-05

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 2.45e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  872 ELRKLKMAAKETGALQAAKNKLE--KQVEELTwrlQLEKRMRVDmEEAKSQENKKLQQ---------KLQELELQSNETK 940
Cdd:PTZ00121  1253 EIRKFEEARMAHFARRQAAIKAEeaRKADELK---KAEEKKKAD-EAKKAEEKKKADEakkkaeeakKADEAKKKAEEAK 1328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  941 ---DLLKREQETAKAAWEKAALVPEVQVDTTLVNELTAENEKLKTlvASLETKIDETEQRFDEVKKArEELLKKATDAES 1017
Cdd:PTZ00121  1329 kkaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK--EEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKK 1405


                   .
gi 1002244077 1018 K 1018
Cdd:PTZ00121  1406 K 1406

Spc7

smart00787

Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...

902-1059

3.64e-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: 41.16 E-value: 3.64e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   902 WRLQLEKRMRVDMEEaksqENKKLQQKLQELELQSNETKDLLKREQEtakaawEKAALVPEVQVDTTLVNELtaeNEKLK 981
Cdd:smart00787  137 WRMKLLEGLKEGLDE----NLEGLKEDYKLLMKELELLNSIKPKLRD------RKDALEEELRQLKQLEDEL---EDCDP 203

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002244077   982 TLVASLETKIDETEQRFDEVKKAREELLKKATDAESKINGLTNTMLSLQEKLtnMELENQVLRQQALFRSPVRTIPEN 1059
Cdd:smart00787  204 TELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEI--AEAEKKLEQCRGFTFKEIEKLKEQ 279

Name

Accession

Description

Interval

E-value

MYSc_Myo11

cd01384

class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...

76-719

0e+00

Pssm-ID: 276835 Cd Length: 647 Bit Score: 1355.42 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPHLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVS 155
Cdd:cd01384      1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPHLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  156 GESGAGKTESTKMLMQYLAFMGGKVQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGAAIR 235
Cdd:cd01384     81 GESGAGKTETTKMLMQYLAYMGGRAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  236 TYLLERSRVCQISDPERNYHCFYMLCS-APAEERERYKLGDPASFHYLNQSNCIKLDGMDDSSEYIATRRAMDIVGISSD 314
Cdd:cd01384    161 TYLLERSRVVQVSDPERNYHCFYQLCAgAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISEE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  315 EQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSKFHLRTASELFMCDEEALEESLCKRVIATRGESIVKNLDARAAA 394
Cdd:cd01384    241 EQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAAT 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  395 LSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEY 474
Cdd:cd01384    321 LSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEEY 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  475 TKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPKFSRSDFTIHHYAGHV 554
Cdd:cd01384    401 TKEEIDWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPKLSRTDFTIDHYAGDV 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  555 TYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFPPS--EESTKSTKFTSIGSSFKQQLQALLETLSSVEPHYIRCIKP 632
Cdd:cd01384    481 TYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLprEGTSSSSKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKP 560

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  633 NNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVLDESYDEVTATEMLLEKVNLTGYQIG 712
Cdd:cd01384    561 NNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLKGSDDEKAACKKILEKAGLKGYQIG 640


                   ....*..
gi 1002244077  713 KTKVFLR 719
Cdd:cd01384    641 KTKVFLR 647

MYSc

smart00242

Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...

58-730

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: 1032.88 E-value: 0e+00

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077    58 EAKRCGVEDMTRLAYLHEPGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIAD 137
Cdd:smart00242    2 PPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLP-IYTDEVIKKYRGKSRGELPPHVFAIAD 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   138 RAYRYMMNYGVSQAILVSGESGAGKTESTKMLMQYLAFMGGKVQSGGRsVQQQVLESNPVLEAFGNAKTVRNNNSSRFGK 217
Cdd:smart00242   81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGS-VEDQILESNPILEAFGNAKTLRNNNSSRFGK 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   218 FVEIQFDQSGKISGAAIRTYLLERSRVCQISDPERNYHCFYMLCS-APAEERERYKLGDPASFHYLNQSNCIKLDGMDDS 296
Cdd:smart00242  160 FIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAgASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDA 239

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   297 SEYIATRRAMDIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSkfHLRTASELFMCDEEALEESLCKRV 376
Cdd:smart00242  240 EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKE--ELSNAAELLGVDPEELEKALTKRK 317

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   377 IATRGESIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNE 456
Cdd:smart00242  318 IKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANE 397

                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   457 KLQQHFNQHVFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFS 536
Cdd:smart00242  398 KLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFS 477

                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   537 RP-KFSRSDFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFPPSEES-TKSTKFTSIGSSFKQQLQA 614
Cdd:smart00242  478 KPkKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNaGSKKRFQTVGSQFKEQLNE 557

                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   615 LLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVL-DESYDE 693
Cdd:smart00242  558 LMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWpPWGGDA 637

                           650       660       670
                    ....*....|....*....|....*....|....*....
gi 1002244077   694 VTATEMLLEKVNL--TGYQIGKTKVFLRAGQMAELDARR 730
Cdd:smart00242  638 KKACEALLQSLGLdeDEYQLGKTKVFLRPGQLAELEELR 676

COG5022

Myosin heavy chain [General function prediction only];

3-1484

0e+00

Myosin heavy chain [General function prediction only];

Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 911.00 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077    3 SKVRFTVGSNVWVEDADVAWIDGlveqvtgdELIIRCTSGKKVTANVS-------SVYPKDAEAKR------CGVEDMTR 69
Cdd:COG5022      2 STTNAEVGSGCWIPDEEKGWIWA--------EIIKEAFNKGKVTEEGKkedgesvSVKKKVLGNDRiklpkfDGVDDLTE 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   70 LAYLHEPGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVS 149
Cdd:COG5022     74 LSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLG-IYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKEN 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  150 QAILVSGESGAGKTESTKMLMQYLAFMGGKVQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKI 229
Cdd:COG5022    153 QTIIISGESGAGKTENAKRIMQYLASVTSSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEI 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  230 SGAAIRTYLLERSRVCQISDPERNYHCFYMLC-SAPAEERERYKLGDPASFHYLNQSNCIKLDGMDDSSEYIATRRAMDI 308
Cdd:COG5022    233 CGAKIETYLLEKSRVVHQNKNERNYHIFYQLLaGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKT 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  309 VGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSKFhlrtASELFMCDEEALEESLCKRVIATRGESIVKNL 388
Cdd:COG5022    313 IGIDEEEQDQIFKILAAILHIGNIEFKEDRNGAAIFSDNSVLDK----ACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPL 388

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  389 DARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFK 468
Cdd:COG5022    389 NLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFK 468

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  469 MEQEEYTKEEIDWSYIQFVDNQEILDLIEKK-PGGIIALLDETCMLRNSTHETFAEKLYQQFKG--NQHFSRPKFSRSDF 545
Cdd:COG5022    469 LEQEEYVKEGIEWSFIDYFDNQPCIDLIEKKnPLGILSLLDEECVMPHATDESFTSKLAQRLNKnsNPKFKKSRFRDNKF 548

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  546 TIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFPPSEESTKSTKFTSIGSSFKQQLQALLETLSSVEPH 625
Cdd:COG5022    549 VVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIESKGRFPTLGSRFKESLNSLMSTLNSTQPH 628

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  626 YIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPE---VLDESYDEVT--ATEML 700
Cdd:COG5022    629 YIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSkswTGEYTWKEDTknAVKSI 708

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  701 LEKVNL--TGYQIGKTKVFLRAGQMAELDARRTEVLSSSASKIQRKVRSYLAHKHFIQLRLSATQLQAVCRG-QIARHYY 777
Cdd:COG5022    709 LEELVIdsSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGfRLRRLVD 788

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  778 EDLRRKAATLtIQTYYRMHFARKNYRDLCSASTTVQSGLrgmaaRKELQYRQQT------KAAVIIQSYCRSYLAHSQYM 851
Cdd:COG5022    789 YELKWRLFIK-LQPLLSLLGSRKEYRSYLACIIKLQKTI-----KREKKLRETEevefslKAEVLIQKFGRSLKAKKRFS 862

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  852 GLKKAAITTQCAWRGRLARRELRKLKMAAKETGALQAAKNKLEKQVEELTWRLQLEKRMRVDMeeaKSQENKKLQQKLQE 931
Cdd:COG5022    863 LLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEF---KTELIARLKKLLNN 939

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  932 LELQSNETKDLLKREQetakaawekaalvpevqvdttlVNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKK 1011
Cdd:COG5022    940 IDLEEGPSIEYVKLPE----------------------LNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNF 997

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1012 atdaESKINGLTNTMLSLQEKLTNM-ELENQVLRQQALFrSPVRTIPENTSPKANSTNSSPHGDEQMTPHgtppaSKEYG 1090
Cdd:COG5022    998 ----KKELAELSKQYGALQESTKQLkELPVEVAELQSAS-KIISSESTELSILKPLQKLKGLLLLENNQL-----QARYK 1067

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1091 KFAQPRPSFF-----ERQHESVDALINCVTENigfsegkpiaaitiykclvhwKIFETEKTSVFDR-LIQIFGSAMQKHD 1164
Cdd:COG5022   1068 ALKLRRENSLlddkqLYQLESTENLLKTINVK---------------------DLEVTNRNLVKPAnVLQFIVAQMIKLN 1126

                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1165 SNEDlaywlstSSTLLIMLQKSLKaaGSSGGTPRKKPQTQSSFLGRMVFRSSNITVDMDLVRQIEAKYPAFLFKQQLT-A 1243
Cdd:COG5022   1127 LLQE-------ISKFLSQLVNTLE--PVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKSKLSsS 1197

                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1244 FVEGLYGMIRDNVKKE-----LSSLLSHAIQVPRIMKASMVRGRSFGTSSLprgrSFSNQGSY-WQAIVDNLDELLKILQ 1317
Cdd:COG5022   1198 EVNDLKNELIALFSKIfsgwpRGDKLKKLISEGWVPTEYSTSLKGFNNLNK----KFDTPASMsNEKLLSLLNSIDNLLS 1273

                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1318 ENCVPAIFMRKIFTQIFSFINAQLFNSLLVRHECCSFSNGEYVKQGLAQMEVWCGEVKPEYVGSALDELKHIRQavgfLV 1397
Cdd:COG5022   1274 SYKLEEEVLPATINSLLQYINVGLFNALRTKASSLRWKSATEVNYNSEELDDWCREFEISDVDEELEELIQAVK----VL 1349

                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1398 IFKKFRISYDEIVNDLCPVLSVQQLYKICTQYwdDKYNTES-VSEEVLDEMRTLITKESGQDSSENTFLLDDEISMPISL 1476
Cdd:COG5022   1350 QLLKDDLNKLDELLDACYSLNPAEIQNLKSRY--DPADKENnLPKEILKKIEALLIKQELQLSLEGKDETEVHLSEIFSE 1427


                   ....*...
gi 1002244077 1477 EEIGDSMD 1484
Cdd:COG5022   1428 EKSLISLD 1435

MYSc

cd00124

Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...

76-719

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: 897.72 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFG-ELSPHPFAIADRAYRYMMNYGVSQAILV 154
Cdd:cd00124      1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLP-LYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  155 SGESGAGKTESTKMLMQYLAFMGGKVQSGGR----SVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKIS 230
Cdd:cd00124     80 SGESGAGKTETTKLVLKYLAALSGSGSSKSSssasSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  231 GAAIRTYLLERSRVCQISDPERNYHCFYMLCS-----APAEERERYKLGDPASFHYLNQSNCIKLDGMDDSSEYIATRRA 305
Cdd:cd00124    160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAglsdgAREELKLELLLSYYYLNDYLNSSGCDRIDGVDDAEEFQELLDA 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  306 MDIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVpKDDKSKFHLRTASELFMCDEEALEESLCKRVIATRGESIV 385
Cdd:cd00124    240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEDSS-AEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETIT 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  386 KNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQD--PSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFN 463
Cdd:cd00124    319 KPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTdaAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFN 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  464 QHVFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHF-SRPKFSR 542
Cdd:cd00124    399 QHVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFfSKKRKAK 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  543 SDFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHAsrcsfvsslfppseestkstkftsiGSSFKQQLQALLETLSSV 622
Cdd:cd00124    479 LEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS-------------------------GSQFRSQLDALMDTLNST 533

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  623 EPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLP---EVLDESYDEVTATEM 699
Cdd:cd00124    534 QPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPgatEKASDSKKAAVLALL 613

                          650       660
                   ....*....|....*....|
gi 1002244077  700 LLEKVNLTGYQIGKTKVFLR 719
Cdd:cd00124    614 LLLKLDSSGYQLGKTKVFLR 633

Myosin_head

pfam00063

Myosin head (motor domain);

64-719

0e+00

Myosin head (motor domain);

Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 873.91 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   64 VEDMTRLAYLHEPGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYM 143
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLP-IYSEDMIKAYRGKRRGELPPHIFAIADEAYRSM 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  144 MNYGVSQAILVSGESGAGKTESTKMLMQYLAFMGGKVQSG-GRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQ 222
Cdd:pfam00063   80 LQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGnVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQ 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  223 FDQSGKISGAAIRTYLLERSRVCQISDPERNYHCFYMLCS-APAEERERYKLGDPASFHYLNQSNCIKLDGMDDSSEYIA 301
Cdd:pfam00063  160 FDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAgASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKI 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  302 TRRAMDIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSkfhLRTASELFMCDEEALEESLCKRVIATRG 381
Cdd:pfam00063  240 TDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTEN---LQKAASLLGIDSTELEKALCKRRIKTGR 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  382 ESIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLL-IGVLDIYGFESFKTNSFEQFCINLTNEKLQQ 460
Cdd:pfam00063  317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASfIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  461 HFNQHVFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPK- 539
Cdd:pfam00063  397 FFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQKPRl 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  540 FSRSDFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFPPSEE---------------STKSTKFTSI 604
Cdd:pfam00063  477 QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETaesaaanesgkstpkRTKKKRFITV 556

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  605 GSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLP 684
Cdd:pfam00063  557 GSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAP 636

                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 1002244077  685 EVLDE-SYDEVTATEMLLEKVNLTG--YQIGKTKVFLR 719
Cdd:pfam00063  637 KTWPKwKGDAKKGCEAILQSLNLDKeeYQFGKTKIFFR 674

MYSc_Myo5

cd01380

class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...

76-719

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: 833.34 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYG-MNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILV 154
Cdd:cd01380      1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLP-IYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  155 SGESGAGKTESTKMLMQYLAFMGGkVQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGAAI 234
Cdd:cd01380     80 SGESGAGKTVSAKYAMRYFATVGG-SSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANM 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  235 RTYLLERSRVCQISDPERNYHCFYMLC-SAPAEERERYKLGDPASFHYLNQSNCIKLDGMDDSSEYIATRRAMDIVGISS 313
Cdd:cd01380    159 RTYLLEKSRVVFQAEEERNYHIFYQLCaAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISE 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  314 DEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKskfHLRTASELFMCDEEALEESLCKRVIATRGESIVKNLDARAA 393
Cdd:cd01380    239 EEQMEIFRILAAILHLGNVEIKATRNDSASISPDDE---HLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQA 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  394 ALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKL--LIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQ 471
Cdd:cd01380    316 IVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhsFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQ 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  472 EEYTKEEIDWSYIQFVDNQEILDLIEKKPgGIIALLDETCMLRNSTHETFAEKLYQQFKG--NQHFSRPKFSRSDFTIHH 549
Cdd:cd01380    396 EEYVKEEIEWSFIDFYDNQPCIDLIEGKL-GILDLLDEECRLPKGSDENWAQKLYNQHLKkpNKHFKKPRFSNTAFIVKH 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  550 YAGHVTYQTDLFLDKNIDyAVNEHQV-LLHASRcsfvsslfppseeSTKSTkftsIGSSFKQQLQALLETLSSVEPHYIR 628
Cdd:cd01380    475 FADDVEYQVEGFLEKNRD-TVSEEHLnVLKASK-------------NRKKT----VGSQFRDSLILLMETLNSTTPHYVR 536

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  629 CIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVLDESYDEVTATEMLLEKV--NL 706
Cdd:cd01380    537 CIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRDDKKKTCENILENLilDP 616

                          650
                   ....*....|...
gi 1002244077  707 TGYQIGKTKVFLR 719
Cdd:cd01380    617 DKYQFGKTKIFFR 629

MYSc_Myo8

cd01383

class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...

76-719

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: 783.43 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGfgELSPHPFAIADRAYRYMMNYGVSQAILVS 155
Cdd:cd01383      1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVP-LYGNEFITAYRQKL--LDSPHVYAVADTAYREMMRDEINQSIIIS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  156 GESGAGKTESTKMLMQYLAFMGGkvqsGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGAAIR 235
Cdd:cd01383     78 GESGAGKTETAKIAMQYLAALGG----GSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQ 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  236 TYLLERSRVCQISDPERNYHCFYMLCS-APAEERERYKLGDPASFHYLNQSNCIKLDGMDDSSEYIATRRAMDIVGISSD 314
Cdd:cd01383    154 TYLLEKSRVVQLANGERSYHIFYQLCAgASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKE 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  315 EQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSkfhLRTASELFMCDEEALEESLCKRVIATRGESIVKNLDARAAA 394
Cdd:cd01383    234 DQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEA---VSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAI 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  395 LSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLL-IGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEE 473
Cdd:cd01383    311 DARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRsISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEE 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  474 YTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPKfsRSDFTIHHYAGH 553
Cdd:cd01383    391 YELDGIDWTKVDFEDNQECLDLIEKKPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGER--GGAFTIRHYAGE 468

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  554 VTYQTDLFLDKNIDYAVNEHQVLLHASRCS----FVSSLFPPSEESTKSTKFT-------SIGSSFKQQLQALLETLSSV 622
Cdd:cd01383    469 VTYDTSGFLEKNRDLLHSDLIQLLSSCSCQlpqlFASKMLDASRKALPLTKASgsdsqkqSVATKFKGQLFKLMQRLENT 548

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  623 EPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVLDESYDEVTATEMLLE 702
Cdd:cd01383    549 TPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDPLSTSVAILQ 628

                          650
                   ....*....|....*....
gi 1002244077  703 KVNLTG--YQIGKTKVFLR 719
Cdd:cd01383    629 QFNILPemYQVGYTKLFFR 647

MYSc_class_II

cd01377

class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...

76-719

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: 773.94 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVS 155
Cdd:cd01377      1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLP-IYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  156 GESGAGKTESTKMLMQYLAFMGGKVQSGGR------SVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKI 229
Cdd:cd01377     80 GESGAGKTENTKKVIQYLASVAASSKKKKEsgkkkgTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  230 SGAAIRTYLLERSRVCQISDPERNYHCFYMLCS-APAEERERYKLGDPASFHYLNQSNCIKLDGMDDSSEYIATRRAMDI 308
Cdd:cd01377    160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSgADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  309 VGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSkfhLRTASELFMCDEEALEESLCK-RVIATRgESIVKN 387
Cdd:cd01377    240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEE---ADKAAHLLGVNSSDLLKALLKpRIKVGR-EWVTKG 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  388 LDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVF 467
Cdd:cd01377    316 QNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMF 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  468 KMEQEEYTKEEIDWSYIQF-VDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFKG---NQHFSRPKFSRS 543
Cdd:cd01377    396 VLEQEEYKKEGIEWTFIDFgLDLQPTIDLIEKPNMGILSILDEECVFPKATDKTFVEKLYSNHLGkskNFKKPKPKKSEA 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  544 DFTIHHYAGHVTYQTDLFLDKNIDyAVNEHQV-LLHASRCSFVSSLFPPSEES--------TKSTKFTSIGSSFKQQLQA 614
Cdd:cd01377    476 HFILKHYAGDVEYNIDGWLEKNKD-PLNENVVaLLKKSSDPLVASLFKDYEESgggggkkkKKGGSFRTVSQLHKEQLNK 554

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  615 LLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVLDESY-DE 693
Cdd:cd01377    555 LMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFdDG 634

                          650       660
                   ....*....|....*....|....*...
gi 1002244077  694 VTATEMLLEKVNL--TGYQIGKTKVFLR 719
Cdd:cd01377    635 KAACEKILKALQLdpELYRIGNTKVFFK 662

MYSc_Myo22

cd14883

class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...

77-719

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: 746.46 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   77 GVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVSG 156
Cdd:cd14883      2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELP-IYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  157 ESGAGKTESTKMLMQYLAfmggKVQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGAAIRT 236
Cdd:cd14883     81 ESGAGKTETTKLILQYLC----AVTNNHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  237 YLLERSRVCQISDPERNYHCFYML---CSAPAEERERYKLGDPASFHYLNQSNCIKLDGMDDSSEYIATRRAMDIVGISS 313
Cdd:cd14883    157 YLLEQSRITFQAPGERNYHVFYQLlagAKHSKELKEKLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPE 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  314 DEQDAIFRVVAAILHLGNVEF--VEGSEADSSVpkDDKSKfhLRTASELFMCDEEALEESLCKRVIATRGESIVKNLDAR 391
Cdd:cd14883    237 EMQEGIFSVLSAILHLGNLTFedIDGETGALTV--EDKEI--LKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQ 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  392 AAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQ 471
Cdd:cd14883    313 EARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQ 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  472 EEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPKFSRSD--FTIHH 549
Cdd:cd14883    393 EEYEKEGINWSHIVFTDNQECLDLIEKPPLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKteFGVKH 472

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  550 YAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFPPSEEST----------------KSTKFTSIGSSFKQQLQ 613
Cdd:cd14883    473 YAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDLLAltglsislggdttsrgTSKGKPTVGDTFKHQLQ 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  614 ALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVLDESYD- 692
Cdd:cd14883    553 SLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSADHKe 632

                          650       660
                   ....*....|....*....|....*....
gi 1002244077  693 EVTATEMLLEKVNL--TGYQIGKTKVFLR 719
Cdd:cd14883    633 TCGAVRALMGLGGLpeDEWQVGKTKVFLR 661

MYSc_Myo1

cd01378

class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...

81-719

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: 739.36 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   81 NLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVSGESGA 160
Cdd:cd01378      6 NLKKRFENDEIYTYIGHVLISVNPFKDLG-IYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGESGA 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  161 GKTESTKMLMQYLAFMGGKVQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGAAIRTYLLE 240
Cdd:cd01378     85 GKTEASKRIMQYIAAVSGGSESEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYLLE 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  241 RSRVCQISDPERNYHCFY-MLCSAPAEERERYKLGDPASFHYLNQSNCIKLDGMDDSSEYIATRRAMDIVGISSDEQDAI 319
Cdd:cd01378    165 KSRVVGQIKGERNFHIFYqLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEEQDSI 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  320 FRVVAAILHLGNVEFVEGSEADSSVPkdDKSkfHLRTASELFMCDEEALEESLCKRVIATRGE---SIVKNLDARAAALS 396
Cdd:cd01378    245 FRILAAILHLGNIQFAEDEEGNAAIS--DTS--VLDFVAYLLGVDPDQLEKALTHRTIETGGGgrsVYEVPLNVEQAAYA 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  397 RDALARIVYSRLFDWLVNKINTSI-GQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYT 475
Cdd:cd01378    321 RDALAKAIYSRLFDWIVERINKSLaAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEEYV 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  476 KEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCM-LRNSTHETFAEKLYQQFKGNQHFSRPK----FSRSDFTIHHY 550
Cdd:cd01378    401 REGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLtAGDATDQTFLQKLNQLFSNHPHFECPSghfeLRRGEFRIKHY 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  551 AGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFPPSEESTKSTKFTSIGSSFKQQLQALLETLSSVEPHYIRCI 630
Cdd:cd01378    481 AGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCI 560

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  631 KPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPE---VLDESYDEVTATEMLLEKVNLT 707
Cdd:cd01378    561 KPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKtwpAWDGTWQGGVESILKDLNIPPE 640

                          650
                   ....*....|..
gi 1002244077  708 GYQIGKTKVFLR 719
Cdd:cd01378    641 EYQMGKTKIFIR 652

MYSc_Myo7

cd01381

class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...

77-719

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: 734.83 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   77 GVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVSG 156
Cdd:cd01381      2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILP-IYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  157 ESGAGKTESTKMLMQYLAFMGGKvqsgGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGAAIRT 236
Cdd:cd01381     81 ESGAGKTESTKLILQYLAAISGQ----HSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQ 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  237 YLLERSRVCQISDPERNYHCFY-MLCSAPAEERERYKLGDPASFHYLNQSNCIKLDGMDDSSEYIATRRAMDIVGISSDE 315
Cdd:cd01381    157 YLLEKSRIVSQAPDERNYHIFYcMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEE 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  316 QDAIFRVVAAILHLGNVEFvEGSEADSSVPKDDKSKFHLRTASELFMCDEEALEESLCKRVIATRGESIVKNLDARAAAL 395
Cdd:cd01381    237 IWDIFKLLAAILHLGNIKF-EATVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALD 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  396 SRDALARIVYSRLFDWLVNKINTSIGQDP---SSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQE 472
Cdd:cd01381    316 VRDAFVKGIYGRLFIWIVNKINSAIYKPRgtdSSRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQE 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  473 EYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPKfSRSD--FTIHHY 550
Cdd:cd01381    396 EYDKEGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPK-SDLNtsFGINHF 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  551 AGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFPP--SEESTKSTKFTSIGSSFKQQLQALLETLSSVEPHYIR 628
Cdd:cd01381    475 AGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEdiSMGSETRKKSPTLSSQFRKSLDQLMKTLSACQPFFVR 554

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  629 CIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVL-DESYDEVTATEMLLEKVNLT 707
Cdd:cd01381    555 CIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPpAHKTDCRAATRKICCAVLGG 634

                          650
                   ....*....|....
gi 1002244077  708 G--YQIGKTKVFLR 719
Cdd:cd01381    635 DadYQLGKTKIFLK 648

MYSc_Myo6

cd01382

class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...

79-719

0e+00

class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276833 Cd Length: 649 Bit Score: 678.20 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   79 LHNLKSRYGMNEIYTYTGNILIAVNPFQRLPHLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVSGES 158
Cdd:cd01382      4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  159 GAGKTESTKMLMQYLAFMGGkvqSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGAAIRTYL 238
Cdd:cd01382     84 GAGKTESTKYILRYLTESWG---SGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  239 LERSRVCQISDPERNYHCFYMLC-SAPAEERERYkLGDPAsfhylnqsncikldgMDDSSEYIATRRAMDIVGISSDEQD 317
Cdd:cd01382    161 LEKSRICVQSKEERNYHIFYRLCaGAPEDLREKL-LKDPL---------------LDDVGDFIRMDKAMKKIGLSDEEKL 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  318 AIFRVVAAILHLGNVEFVEGSEADSSVPK-DDKSKFHLRTASELFMCDEEALEESLCKRVI-----ATRGESIVKNLDAR 391
Cdd:cd01382    225 DIFRVVAAVLHLGNIEFEENGSDSGGGCNvKPKSEQSLEYAAELLGLDQDELRVSLTTRVMqttrgGAKGTVIKVPLKVE 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  392 AAALSRDALARIVYSRLFDWLVNKINTSIGQDpSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQ 471
Cdd:cd01382    305 EANNARDALAKAIYSKLFDHIVNRINQCIPFE-TSSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKEEQ 383

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  472 EEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPKFSRSD------- 544
Cdd:cd01382    384 ELYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSIPRKSKLKihrnlrd 463

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  545 ---FTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFPPSEESTKSTK-------FTSIGSSFKQQLQA 614
Cdd:cd01382    464 degFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKDSKqkagklsFISVGNKFKTQLNL 543

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  615 LLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVLdESYDEV 694
Cdd:cd01382    544 LMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKL-ARLDPR 622

                          650       660
                   ....*....|....*....|....*..
gi 1002244077  695 TATEMLLEKVNLTG--YQIGKTKVFLR 719
Cdd:cd01382    623 LFCKALFKALGLNEndFKFGLTKVFFR 649

MYSc_Myo4

cd14872

class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...

76-719

0e+00

class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276839 Cd Length: 644 Bit Score: 661.09 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVS 155
Cdd:cd14872      1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLP-LYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILIS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  156 GESGAGKTESTKMLMQYLAFMGGKVQSggrsVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGAAIR 235
Cdd:cd14872     80 GESGAGKTEATKQCLSFFAEVAGSTNG----VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  236 TYLLERSRVCQISDPERNYHCFYMLCSAPAEEReRYKLGDPASFHYLNQSNCIKLDGMDDSSEYIATRRAMDIVGISSDE 315
Cdd:cd14872    156 NYLLEKSRVVYQIKGERNFHIFYQLLASPDPAS-RGGWGSSAAYGYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFDDAD 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  316 QDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSKFHLRTASELFMCDEEALEESLCKRVIATRG-ESIVKNLDARAAA 394
Cdd:cd14872    235 INNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIKGcDPTRIPLTPAQAT 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  395 LSRDALARIVYSRLFDWLVNKINTSIGQDPSSK-LLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEE 473
Cdd:cd14872    315 DACDALAKAAYSRLFDWLVKKINESMRPQKGAKtTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEAL 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  474 YTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSR--PKFSRSDFTIHHYA 551
Cdd:cd14872    395 YQSEGVKFEHIDFIDNQPVLDLIEKKQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYaeVRTSRTEFIVKHYA 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  552 GHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFPPSEESTKSTKFTsIGSSFKQQLQALLETLSSVEPHYIRCIK 631
Cdd:cd14872    475 GDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEGDQKTSKVT-LGGQFRKQLSALMTALNATEPHYIRCVK 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  632 PNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEV-LDESYDEVTATEMLLEKVN--LTG 708
Cdd:cd14872    554 PNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVKTIaKRVGPDDRQRCDLLLKSLKqdFSK 633

                          650
                   ....*....|.
gi 1002244077  709 YQIGKTKVFLR 719
Cdd:cd14872    634 VQVGKTRVLYR 644

MYSc_Myo40

cd14901

class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...

76-718

0e+00

class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 654.16 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIY------KGAGFGELSPHPFAIADRAYRYMM----N 145
Cdd:cd14901      1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLP-LYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLfasrG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  146 YGVSQAILVSGESGAGKTESTKMLMQYLAFMGGKVQSGGRS-----VQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVE 220
Cdd:cd14901     80 QKCDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNAterenVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  221 IQFDQSGKISGAAIRTYLLERSRVCQISDPERNYHCFYMLCS-APAEERERYKLGDPASFHYLNQSNC-IKLDGMDDSSE 298
Cdd:cd14901    160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRgASSDELHALGLTHVEEYKYLNSSQCyDRRDGVDDSVQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  299 YIATRRAMDIVGISSDEQDAIFRVVAAILHLGNVEFVE-GSEADSSvpkDDKSKFHLRTASELFMCDEEALEESLCKRVI 377
Cdd:cd14901    240 YAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKkDGEGGTF---SMSSLANVRAACDLLGLDMDVLEKTLCTREI 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  378 ATRGESIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSS--KLLIGVLDIYGFESFKTNSFEQFCINLTN 455
Cdd:cd14901    317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTgaSRFIGIVDIFGFEIFATNSLEQLCINFAN 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  456 EKLQQHFNQHVFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHF 535
Cdd:cd14901    397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHASF 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  536 SRPKFSR--SDFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSlfppseestkstkftSIGSSFKQQLQ 613
Cdd:cd14901    477 SVSKLQQgkRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS---------------TVVAKFKVQLS 541

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  614 ALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEV-----LD 688
Cdd:cd14901    542 SLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPDGasdtwKV 621

                          650       660       670
                   ....*....|....*....|....*....|...
gi 1002244077  689 ESYDEVTATEMLLEKVNLTG---YQIGKTKVFL 718
Cdd:cd14901    622 NELAERLMSQLQHSELNIEHlppFQVGKTKVFL 654

MYSc_Myo27

cd14888

class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...

76-719

0e+00

class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 650.22 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPHLYNNHMMEIYKgAGFGELSPHPFAIADRAYRYMMNYGVSQAILVS 155
Cdd:cd14888      1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPGLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  156 GESGAGKTESTKMLMQYLAFMGGKVQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQ---------S 226
Cdd:cd14888     80 GESGAGKTESTKYVMKFLACAGSEDIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskrmsgdR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  227 GKISGAAIRTYLLERSRVCQISDPERNYHCFYMLCSA---------PAEERERYKLGDPAS---------------FHYL 282
Cdd:cd14888    160 GRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAareakntglSYEENDEKLAKGADAkpisidmssfephlkFRYL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  283 NQSNCIKLDGMDDSSEYIATRRAMDIVGISSDEQDAIFRVVAAILHLGNVEFVEgSEADSSVPKDDKSKF-HLRTASELF 361
Cdd:cd14888    240 TKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFEN-NEACSEGAVVSASCTdDLEKVASLL 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  362 MCDEEALEESLCKRVIATRGESIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLI-GVLDIYGFES 440
Cdd:cd14888    319 GVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFcGVLDIFGFEC 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  441 FKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHET 520
Cdd:cd14888    399 FQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKPLGIFCMLDEECFVPGGKDQG 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  521 FAEKLYQQFKGNQHFSRPKFSRSDFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFPP-----SEES 595
Cdd:cd14888    479 LCNKLCQKHKGHKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSAylrrgTDGN 558

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  596 TKSTKFTSIGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEF 675
Cdd:cd14888    559 TKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEF 638

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....
gi 1002244077  676 VDRFGVLLPEVldesydevtatemllEKVNLTGYQIGKTKVFLR 719
Cdd:cd14888    639 YNDYRILLNGE---------------GKKQLSIWAVGKTLCFFK 667

MYSc_Myo29

cd14890

class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...

78-719

0e+00

class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 645.29 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPHLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVS----QAIL 153
Cdd:cd14890      3 LLHTLRLRYERDEIYTYVGPILISINPYKSIPDLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSGVLdpsnQSII 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  154 VSGESGAGKTESTKMLMQYLAFMGGKVQSGGR---------------SVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKF 218
Cdd:cd14890     83 ISGESGAGKTEATKIIMQYLARITSGFAQGASgegeaaseaieqtlgSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGKF 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  219 VEIQFDQSGKISGAAIRTYLLERSRVCQISDPERNYHCFYMLCS-APAEERERYKLGDPASFHYLnQSNCIKLDGMDDSS 297
Cdd:cd14890    163 IEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAgADEALRERLKLQTPVEYFYL-RGECSSIPSCDDAK 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  298 EYIATRRAMDIVGISSDEQDAIFRVVAAILHLGNVEFveGSEADSSVPKDDKSKFHLRTASELFMCDEEALEESLCKRVI 377
Cdd:cd14890    242 AFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDF--ESENDTTVLEDATTLQSLKLAAELLGVNEDALEKALLTRQL 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  378 ATRGESIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQdPSSKL-LIGVLDIYGFESFKTNSFEQFCINLTNE 456
Cdd:cd14890    320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISS-PDDKWgFIGVLDIYGFEKFEWNTFEQLCINYANE 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  457 KLQQHFNQHVFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIAL---LDETCMLRNSTHET-FAEKLYQQF--- 529
Cdd:cd14890    399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVNGKPGIfitLDDCWRFKGEEANKkFVSQLHASFgrk 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  530 ----------KGNQHFSRPKFSRS-DFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLhasrcsfvsslfppsEESTKS 598
Cdd:cd14890    479 sgsggtrrgsSQHPHFVHPKFDADkQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELI---------------KQSRRS 543

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  599 TKFTSIGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDR 678
Cdd:cd14890    544 IREVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYD 623

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|...
gi 1002244077  679 FGVLLPEvlDESYDEVTA--TEMLleKVNLTGYQIGKTKVFLR 719
Cdd:cd14890    624 FQVLLPT--AENIEQLVAvlSKML--GLGKADWQIGSSKIFLK 662

MYSc_Myo9

cd01385

class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...

79-719

0e+00

class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 624.40 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   79 LHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVSGES 158
Cdd:cd01385      4 LENLRARFKHGKIYTYVGSILIAVNPFKFLP-IYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGES 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  159 GAGKTESTKMLMQYLAFMGGKvqSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGAAIRTYL 238
Cdd:cd01385     83 GSGKTESTNFLLHHLTALSQK--GYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  239 LERSRVCQISDPERNYH-CFYMLCSAPAEERERYKLGDPASFHYLNQSNCIKLDGMDDSSEYIATRRAMDIVGISSDEQD 317
Cdd:cd01385    161 LEKSRIVSQEKNERNYHvFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQR 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  318 AIFRVVAAILHLGNVEFV-EGSEADSSVPKddKSKFHLRTASELFMCDEEALEESLCKRVIATRGESIVKNLDARAAALS 396
Cdd:cd01385    241 QIFSVLSAVLHLGNIEYKkKAYHRDESVTV--GNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIAT 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  397 RDALARIVYSRLFDWLVNKIN--------TSIGQDPSskllIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFK 468
Cdd:cd01385    319 RDAMAKCLYSALFDWIVLRINhallnkkdLEEAKGLS----IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFK 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  469 MEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPKFSRSDFTIH 548
Cdd:cd01385    395 LEQEEYKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIA 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  549 HYAGHVTYQTDLFLDKNIDY--------------------------AVNEHQVLLHASRCSFV----------------S 586
Cdd:cd01385    475 HYAGKVKYQIKDFREKNLDLmrpdivavlrssssafvreligidpvAVFRWAVLRAFFRAMAAfreagrrraqrtaghsL 554

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  587 SLFPPSEEST----KSTKFTSIGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRIS 662
Cdd:cd01385    555 TLHDRTTKSLlhlhKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIR 634

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002244077  663 CLGYPTRRTFDEFVDRFGVLLPEVLDESYDEVTATEMLLeKVNLTGYQIGKTKVFLR 719
Cdd:cd01385    635 RSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEKL-NLDRDNYQIGKTKVFLK 690

MYSc_Myo31

cd14892

class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...

82-719

0e+00

class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 615.62 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   82 LKSRYGMNEIYTYTGNILIAVNPFQRLPHLYN--NHMMEIYKGAGFGELSPHPFAIADRAYRYMM----NYGVSQAILVS 155
Cdd:cd14892      7 LRRRYERDAIYTFTADILISINPYKSIPLLYDvpGFDSQRKEEATASSPPPHVFSIAERAYRAMKgvgkGQGTPQSIVVS 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  156 GESGAGKTESTKMLMQYLA---------FMGGKVQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQS 226
Cdd:cd14892     87 GESGAGKTEASKYIMKYLAtasklakgaSTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNSD 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  227 GKISGAAIRTYLLERSRVCQISDPERNYHCFYMLCSA-PAEERERYKLGDPASFHYLNQSNCIKLDGMDDSSEYIATRRA 305
Cdd:cd14892    167 GRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGlDANENAALELTPAESFLFLNQGNCVEVDGVDDATEFKQLRDA 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  306 MDIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSKfHLRTASELFMCDEEALEESLCKRVIAT-RGESI 384
Cdd:cd14892    247 MEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGV-NVAKAAGLLGVDAAELMFKLVTQTTSTaRGSVL 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  385 VKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQ----------DPSSKLLIGVLDIYGFESFKTNSFEQFCINLT 454
Cdd:cd14892    326 EIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQqtsgvtggaaSPTFSPFIGILDIFGFEIMPTNSFEQLCINFT 405

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  455 NEKLQQHFNQHVFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCML-RNSTHETFAEKLYQ-QFKGN 532
Cdd:cd14892    406 NEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKPLGLLPLLEEQMLLkRKTTDKQLLTIYHQtHLDKH 485

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  533 QHFSRPKFSRSDFTIHHYAGHVTYQTDLFLDKNIDyavNEHQVLLHASRCSfvsslfppseestkstkftsigSSFKQQL 612
Cdd:cd14892    486 PHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNND---NLHDDLRDLLRSS----------------------SKFRTQL 540

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  613 QALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLL--------- 683
Cdd:cd14892    541 AELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLArnkagvaas 620

                          650       660       670
                   ....*....|....*....|....*....|....*.
gi 1002244077  684 PEVLDESYDEVTATEMLLEKVNLTGYQIGKTKVFLR 719
Cdd:cd14892    621 PDACDATTARKKCEEIVARALERENFQLGRTKVFLR 656

MYSc_Myo42

cd14903

class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...

76-719

0e+00

class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 612.94 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPHLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVS 155
Cdd:cd14903      1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  156 GESGAGKTESTKMLMQYLAFMGGKVQSggrSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGAAIR 235
Cdd:cd14903     81 GESGAGKTETTKILMNHLATIAGGLND---STIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  236 TYLLERSRVCQISDPERNYHCFYMLCSAPAEErERYKLGDPASFHYLNQSNCIKLDGMDDSSEYIATRRAMDIVGISSDE 315
Cdd:cd14903    158 TYLLEKTRVISHERPERNYHIFYQLLASPDVE-ERLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEEK 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  316 QDAIFRVVAAILHLGNVEFVEGS---EADSSVPKDDkskfHLRTASELFMCDEEALEESLCKRVIATRGESIVKNLDARA 392
Cdd:cd14903    237 QEVLFEVLAGILHLGQLQIQSKPnddEKSAIAPGDQ----GAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQ 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  393 AALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQE 472
Cdd:cd14903    313 AEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQI 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  473 EYTKEEIDWSYIQFVDNQEILDLIEKKPgGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSR-PKFSRSDFTIHHYA 551
Cdd:cd14903    393 EYEEEGIRWAHIDFADNQDVLAVIEDRL-GIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEfPRTSRTQFTIKHYA 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  552 GHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFPPSEESTKSTKF----------------TSIGSSFKQQLQAL 615
Cdd:cd14903    472 GPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTslargarrrrggalttTTVGTQFKDSLNEL 551

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  616 LETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVLDESYDEVT 695
Cdd:cd14903    552 MTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGRNTDVPVAE 631

                          650       660
                   ....*....|....*....|....*..
gi 1002244077  696 ATEMLLEKVNLTG---YQIGKTKVFLR 719
Cdd:cd14903    632 RCEALMKKLKLESpeqYQMGLTRIYFQ 658

MYSc_Myo10

cd14873

class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...

78-719

0e+00

class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 610.64 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPHLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVSGE 157
Cdd:cd14873      3 IMYNLFQRYKRNQIYTYIGSILASVNPYQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISGE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  158 SGAGKTESTKMLMQYLAFM-----GGKVQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGA 232
Cdd:cd14873     83 SGAGKTESTKLILKFLSVIsqqslELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQGG 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  233 AIRTYLLERSRVCQISDPERNYHCFY-MLCSAPAEERERYKLGDPASFHYLNQSNCIKLDGMDDSSEYIATRRAMDIVGI 311
Cdd:cd14873    163 RIVDYLLEKNRVVRQNPGERNYHIFYaLLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVMQF 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  312 SSDEQDAIFRVVAAILHLGNVEFVEGSEADSSvpkddkSKFHLRTASELFMCDEEALEESLCKRVIATRGESIVKNLDAR 391
Cdd:cd14873    243 SKEEVREVSRLLAGILHLGNIEFITAGGAQVS------FKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQ 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  392 AAALSRDALARIVYSRLFDWLVNKINTSI-GQDPSSKllIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKME 470
Cdd:cd14873    317 QAVDSRDSLAMALYARCFEWVIKKINSRIkGKEDFKS--IGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLE 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  471 QEEYTKEEIDWSYIQFVDNQEILDLIEKKPgGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPKFSRSDFTIHHY 550
Cdd:cd14873    395 QLEYSREGLVWEDIDWIDNGECLDLIEKKL-GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNNFGVKHY 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  551 AGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFP--PSEESTKSTKFTS------IGSSFKQQLQALLETLSSV 622
Cdd:cd14873    474 AGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEhvSSRNNQDTLKCGSkhrrptVSSQFKDSLHSLMATLSSS 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  623 EPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEV-LDESYDEVTATemLL 701
Cdd:cd14873    554 NPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLaLPEDVRGKCTS--LL 631

                          650       660
                   ....*....|....*....|
gi 1002244077  702 EKVNLTG--YQIGKTKVFLR 719
Cdd:cd14873    632 QLYDASNseWQLGKTKVFLR 651

MYSc_Myo3

cd01379

class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...

78-719

0e+00

class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 606.58 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVSGE 157
Cdd:cd01379      3 IVSQLQKRYSRDQIYTYIGDILIAVNPFQNLG-IYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  158 SGAGKTESTKMLMQYLAFMGgkvQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGAAIRTY 237
Cdd:cd01379     82 SGAGKTESANLLVQQLTVLG---KANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEY 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  238 LLERSRVCQISDPERNYHCFYMLCSAPAEER--ERYKLGDPASFHYLNQSNCIKLDGMDDSS---EYIATRRAMDIVGIS 312
Cdd:cd01379    159 LLEKSRVVHQAIGERNFHIFYYIYAGLAEDKklAKYKLPENKPPRYLQNDGLTVQDIVNNSGnreKFEEIEQCFKVIGFT 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  313 SDEQDAIFRVVAAILHLGNVEFVEgseaDSSVPKDDKSKF-----HLRTASELFMCDEEALEESLCKRVIATRGESIVKN 387
Cdd:cd01379    239 KEEVDSVYSILAAILHIGDIEFTE----VESNHQTDKSSRisnpeALNNVAKLLGIEADELQEALTSHSVVTRGETIIRN 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  388 LDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSS---KLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQ 464
Cdd:cd01379    315 NTVEEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSAsdePLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQ 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  465 HVFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFKgNQHFSRPKFSRSD 544
Cdd:cd01379    395 HIFAWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNIK-SKYYWRPKSNALS 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  545 FTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASrcsfvsslfppSEESTKSTkftsIGSSFKQQLQALLETLSSVEP 624
Cdd:cd01379    474 FGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSS-----------ENPLVRQT----VATYFRYSLMDLLSKMVVGQP 538

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  625 HYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLlpevldeSY---DEVTAT---- 697
Cdd:cd01379    539 HFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFL-------AFkwnEEVVANrenc 611

                          650       660
                   ....*....|....*....|..
gi 1002244077  698 EMLLEKVNLTGYQIGKTKVFLR 719
Cdd:cd01379    612 RLILERLKLDNWALGKTKVFLK 633

MYSc_Myo15

cd01387

class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...

78-719

0e+00

class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 602.51 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFqRLPHLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVSGE 157
Cdd:cd01387      3 VLWNLKTRYERNLIYTYIGSILVSVNPY-KMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  158 SGAGKTESTKMLMQYLAFMggkVQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFdQSGKISGAAIRTY 237
Cdd:cd01387     82 SGSGKTEATKLIMQYLAAV---NQRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAITSQY 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  238 LLERSRVCQISDPERNYHCFY-MLCSAPAEERERYKLGDPASFHYLNQSNCIKLDGMDDSSEYIATRRAMDIVGISSDEQ 316
Cdd:cd01387    158 LLEKSRIVTQAKNERNYHVFYeLLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQ 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  317 DAIFRVVAAILHLGNVEF--------VEGSEADSSVpkddkskfHLRTASELFMCDEEALEESLCKRVIATRGESIVKNL 388
Cdd:cd01387    238 DSIFRILASVLHLGNVYFhkrqlrhgQEGVSVGSDA--------EIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPL 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  389 DARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFK 468
Cdd:cd01387    310 TIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFK 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  469 MEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPKFSRSDFTIH 548
Cdd:cd01387    390 LEQEEYIREQIDWTEIAFADNQPVINLISKKPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRMPLPEFTIK 469

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  549 HYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFPPSEESTKST--------------KFTSIGSSFKQQLQA 614
Cdd:cd01387    470 HYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKApprlgkgrfvtmkpRTPTVAARFQDSLLQ 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  615 LLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVLDESYDEV 694
Cdd:cd01387    550 LLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRPAPGD 629

                          650       660
                   ....*....|....*....|....*...
gi 1002244077  695 TATEMLLEKVNLTG---YQIGKTKVFLR 719
Cdd:cd01387    630 MCVSLLSRLCTVTPkdmYRLGATKVFLR 657

MyosinXI_CBD

cd15475

cargo binding domain of myosin XI; Class XI myosins are a plant specific group, homologous to ...

1101-1477

0e+00

Pssm-ID: 271259 Cd Length: 326 Bit Score: 602.26 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1101 ERQHESVDALINCVTENIGFSEGKPIAAITIYKCLVHWKIFETEKTSVFDRLIQIFGSAMQKHDSNEDLAYWLSTSSTLL 1180
Cdd:cd15475      1 ERQQENVDALIKCVSENLGFSEGKPVAAFTIYKCLLHWKSFEAEKTSVFDRIIQTIGSAIEDQDNNDHLAYWLSNTSTLL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1181 IMLQKSLkaagssggtprkkpqtqssflgrmvfrssnitvdmdlvrqieakyPAFLFKQQLTAFVEGLYGMIRDNVKKEL 1260
Cdd:cd15475     81 FLLQRSL---------------------------------------------PALLFKQQLTAYVEKIYGIIRDNLKKEL 115

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1261 SSLLSHAIQVPRImkasmVRGRSFGTSSLPRGRSFSNQGSYWQAIVDNLDELLKILQENCVPAIFMRKIFTQIFSFINAQ 1340
Cdd:cd15475    116 SPLLSLCIQAPRT-----SRGSSSKSSSSANSLGQQSPSSHWQSIIKSLNSLLSTLKENHVPPFLVQKIFTQVFSFINVQ 190

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1341 LFNSLLVRHECCSFSNGEYVKQGLAQMEVWCGEVKPEYVGSALDELKHIRQAVGFLVIFKKFRISYDEIVNDLCPVLSVQ 1420
Cdd:cd15475    191 LFNSLLLRRECCSFSNGEYVKAGLAELELWCSQATEEYAGSSWDELKHIRQAVGFLVIHQKSRKSYDEITNDLCPVLSVQ 270

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002244077 1421 QLYKICTQYWDDKYNTESVSEEVLDEMRTLITKESgQDSSENTFLLDDEISMPISLE 1477
Cdd:cd15475    271 QLYRICTMYWDDKYGTQSVSPEVISSMRVLMTEDS-NNAVSNSFLLDDDSSIPFSVE 326

MYSc_Myo30

cd14891

class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...

76-719

0e+00

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: 594.71 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEI--YTYTGNILIAVNPFQRLPhlyNNHMMEiYKGAGFGELSPHPFAIADRAYRYM-MNYGV--SQ 150
Cdd:cd14891      1 AGILHNLEERSKLDNQrpYTFMANVLIAVNPLRRLP---EPDKSD-YINTPLDPCPPHPYAIAEMAYQQMcLGSGRmqNQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  151 AILVSGESGAGKTESTKMLMQYL---------------AFMGGKVQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRF 215
Cdd:cd14891     77 SIVISGESGAGKTETSKIILRFLttravggkkasgqdiEQSSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRF 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  216 GKFVEIQF-DQSGKISGAAIRTYLLERSRVCQISDPERNYHCFY-MLCSAPAEERERYKLGDPASFHYLNQSNCIKLDGM 293
Cdd:cd14891    157 GKFMKLQFtKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYqLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNI 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  294 DDSSEYIATRRAMDIVGISSDEQDAIFRVVAAILHLGNVEF--VEGSEADSSVPKDDkSKFHLRTASELFMCDEEALEES 371
Cdd:cd14891    237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFdeEDTSEGEAEIASES-DKEALATAAELLGVDEEALEKV 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  372 LCKRVIATRGESIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKT-NSFEQFC 450
Cdd:cd14891    316 ITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFETkNDFEQLL 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  451 INLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFK 530
Cdd:cd14891    396 INYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPNGILPLLDNEARNPNPSDAKLNETLHKTHK 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  531 GNQHFSRP--KFSRSDFTIHHYAGHVTYQTDLFLDKNIDyavnehqvllhasrcsfvssLFPPSEESTKSTkftsiGSSF 608
Cdd:cd14891    476 RHPCFPRPhpKDMREMFIVKHYAGTVSYTIGSFIDKNND--------------------IIPEDFEDLLAS-----SAKF 530

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  609 KQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPE--- 685
Cdd:cd14891    531 SDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPsvt 610

                          650       660       670
                   ....*....|....*....|....*....|....*
gi 1002244077  686 VLDESYDEVTATEMLLE-KVNLTGYQIGKTKVFLR 719
Cdd:cd14891    611 RLFAENDRTLTQAILWAfRVPSDAYRLGRTRVFFR 645

MYSc_Myo36

cd14897

class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...

78-719

0e+00

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: 567.40 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGF-GELSPHPFAIADRAYRYMMNYGVSQAILVSG 156
Cdd:cd14897      3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLP-IFDKKHHEEYSNLSVrSQRPPHLFWIADQAYRRLLETGRNQCILVSG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  157 ESGAGKTESTKMLMQYLAFMGGKVQSggrSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGAAIRT 236
Cdd:cd14897     82 ESGAGKTESTKYMIKHLMKLSPSDDS---DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDD 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  237 YLLERSRVCQISDPERNYHCFYMLCSAPAEERER-YKLGDPASFHYLNQSNcIKLDGMDDSSEYIATR-------RAMDI 308
Cdd:cd14897    159 YLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLyYFLEDPDCHRILRDDN-RNRPVFNDSEELEYYRqmfhdltNIMKL 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  309 VGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDkskFHLRTASELFMCDEEALEESLCKRVIATRGESIVKNL 388
Cdd:cd14897    238 IGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADE---YPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWK 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  389 DARAAALSRDALARIVYSRLFDWLVNKINTSI-----GQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFN 463
Cdd:cd14897    315 SLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkdFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFN 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  464 QHVFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPKFSRS 543
Cdd:cd14897    395 DYVFPRERSEYEIEGIEWRDIEYHDNDDVLELFFKKPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVASPGNRV 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  544 DFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFPpseestkstkftsigSSFKQQLQALLETLSSVE 623
Cdd:cd14897    475 AFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT---------------SYFKRSLSDLMTKLNSAD 539

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  624 PHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVLDESYDEVTATEMLLEK 703
Cdd:cd14897    540 PLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFSNKVRSDDLGKCQKILKT 619

                          650
                   ....*....|....*.
gi 1002244077  704 VNLTGYQIGKTKVFLR 719
Cdd:cd14897    620 AGIKGYQFGKTKVFLK 635

MYSc_Myo43

cd14904

class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...

76-719

0e+00

class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276869 Cd Length: 653 Bit Score: 560.72 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPHLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVS 155
Cdd:cd14904      1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  156 GESGAGKTESTKMLMQYLAFMggkvqSGGR--SVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGAA 233
Cdd:cd14904     81 GESGAGKTETTKIVMNHLASV-----AGGRkdKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAK 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  234 IRTYLLERSRVCQISDPERNYHCFY-MLCSAPAEERERYKLGDPASFHYLNQS-NCIKLDGMDDSSEYIATRRAMDIVGI 311
Cdd:cd14904    156 CETYLLEKSRVVSIAEGERNYHIFYqLLAGLSSEERKEFGLDPNCQYQYLGDSlAQMQIPGLDDAKLFASTQKSLSLIGL 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  312 SSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKskfhLRTASELFMCDEEALEESLCKRVIATRGESIVKNLDAR 391
Cdd:cd14904    236 DNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQ----LSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPV 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  392 AAALSRDALARIVYSRLFDWLVNKINTSIGQDPSS-KLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKME 470
Cdd:cd14904    312 EAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRiKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTV 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  471 QEEYTKEEIDWSYIQFVDNQEILDLIEKKPgGIIALLDETCMLRNSTHETFAEKL---YQQFKGNQHFSRPKFSRSDFTI 547
Cdd:cd14904    392 EEEYIREGLQWDHIEYQDNQGIVEVIDGKM-GIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDFPKVKRTQFII 470

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  548 HHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLF-----------PPSEESTKSTKftSIGSSFKQQLQALL 616
Cdd:cd14904    471 NHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFgsseapsetkeGKSGKGTKAPK--SLGSQFKTSLSQLM 548

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  617 ETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVLDESYDEVTA 696
Cdd:cd14904    549 DNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSKDVRRTC 628

                          650       660
                   ....*....|....*....|....*
gi 1002244077  697 TEML--LEKVNLTGYQIGKTKVFLR 719
Cdd:cd14904    629 SVFMtaIGRKSPLEYQIGKSLIYFK 653

MYSc_Myo46

cd14907

class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...

78-719

1.35e-180

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: 553.87 E-value: 1.35e-180

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPHLYNNHMMEIYK------GAGF--GELSPHPFAIADRAYRYMMNYGVS 149
Cdd:cd14907      3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDNLFSEEVMQMYKeqiiqnGEYFdiKKEPPHIYAIAALAFKQLFENNKK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  150 QAILVSGESGAGKTESTKMLMQYLAFMGGKVQS----------------GGRSVQQQVLESNPVLEAFGNAKTVRNNNSS 213
Cdd:cd14907     83 QAIVISGESGAGKTENAKYAMKFLTQLSQQEQNseevltltssiratskSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  214 RFGKFVEIQFD-QSGKISGAAIRTYLLERSRVCQISDPERNYHCFY-MLCSAPAEERERYKLGDPAS---FHYLNQSNCI 288
Cdd:cd14907    163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYhLLYGADQQLLQQLGLKNQLSgdrYDYLKKSNCY 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  289 KLDGMDDSSEYIATRRAMDIVGISSDEQDAIFRVVAAILHLGNVEFvEGSEADSSVPKDDKSKFHLRTASELFMCDEEAL 368
Cdd:cd14907    243 EVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQF-DDSTLDDNSPCCVKNKETLQIIAKLLGIDEEEL 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  369 EESLCKRVIATRGESIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSK--------LLIGVLDIYGFES 440
Cdd:cd14907    322 KEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMPKDEKDqqlfqnkyLSIGLLDIFGFEV 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  441 FKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKE--EIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTH 518
Cdd:cd14907    402 FQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEglEDYLNQLSYTDNQDVIDLLDKPPIGIFNLLDDSCKLATGTD 481

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  519 ETFAEKLYQQFKGNQHFSRP-KFSRSDFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLF-------- 589
Cdd:cd14907    482 EKLLNKIKKQHKNNSKLIFPnKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFsgedgsqq 561

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  590 ---PPSEESTKSTKFtsIGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGY 666
Cdd:cd14907    562 qnqSKQKKSQKKDKF--LGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGY 639

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1002244077  667 PTRRTFDEFVDRFGVLLPEVLdesydevtatemllekvnltgyqIGKTKVFLR 719
Cdd:cd14907    640 PYRKSYEDFYKQYSLLKKNVL-----------------------FGKTKIFMK 669

MYSc_Myo47

cd14908

class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...

76-719

2.82e-176

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: 543.35 E-value: 2.82e-176

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGF---------GELSPHPFAIADRAYRYMMN- 145
Cdd:cd14908      1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLP-LYGKEILESYRQEGLlrsqgiespQALGPHVFAIADRSYRQMMSe 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  146 YGVSQAILVSGESGAGKTESTKMLMQYLAFMG----GKVQSGGR----SVQQQVLESNPVLEAFGNAKTVRNNNSSRFGK 217
Cdd:cd14908     80 IRASQSILISGESGAGKTESTKIVMLYLTTLGngeeGAPNEGEElgklSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  218 FVEIQFDQSGKISGAAIRTYLLERSRVCQISDPERNYHCFYMLC-SAPAEERERYKLGD--------PASFHYLNQSNCI 288
Cdd:cd14908    160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrGGDEEEHEKYEFHDgitgglqlPNEFHYTGQGGAP 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  289 KLDGMDDSSEYIATRRAMDIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSKFHLRTASELFMCDEEAL 368
Cdd:cd14908    240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARVAKLLGVDVDKL 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  369 EESLCKRVIATRGESIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIG--QDPSSKLLIGVLDIYGFESFKTNSF 446
Cdd:cd14908    320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINweNDKDIRSSVGVLDIFGFECFAHNSF 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  447 EQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCML-RNSTHETFAEKL 525
Cdd:cd14908    400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAKKKGILTMLDDECRLgIRGSDANYASRL 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  526 YQQF---KGNQHFSRPKFS-------RSDFTIHHYAGHVTYQTDL-FLDKNIDYAVNEHQVLLHAsrcsfvsslfppsee 594
Cdd:cd14908    480 YETYlpeKNQTHSENTRFEatsiqktKLIFAVRHFAGQVQYTVETtFCEKNKDEIPLTADSLFES--------------- 544

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  595 stkstkftsiGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDE 674
Cdd:cd14908    545 ----------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKD 614

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002244077  675 FVDRFGVLLP----EVLDESYDEVTATEMLLEKVNL-------------------TGYQIGKTKVFLR 719
Cdd:cd14908    615 FFKRYRMLLPlipeVVLSWSMERLDPQKLCVKKMCKdlvkgvlspamvsmknipeDTMQLGKSKVFMR 682

MYSc_Myo28

cd14889

class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...

78-719

2.84e-173

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: 534.49 E-value: 2.84e-173

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLpHLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVS----QAIL 153
Cdd:cd14889      3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYL-HIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLGRLARgpknQCIV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  154 VSGESGAGKTESTKMLMQYLAfmggKVQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFdQSGKISGAA 233
Cdd:cd14889     82 ISGESGAGKTESTKLLLRQIM----ELCRGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAK 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  234 IRTYLLERSRVCQISDPERNYHCFY-MLCSAPAEERERYKLGDPASFHYLNQSNCIKLDGMDDSSEYIATRRAMDIVGIS 312
Cdd:cd14889    157 INEYLLEKSRVVHQDGGEENFHIFYyMFAGISAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYDEVCNAMDMVGFT 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  313 SDEQDAIFRVVAAILHLGNVEFvEGSEADSSVPKDDkSKFHLRTASELFMCDEEALEESLCKRVIATRGESIVKNLDARA 392
Cdd:cd14889    237 EQEEVDMFTILAGILSLGNITF-EMDDDEALKVEND-SNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQ 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  393 AALSRDALARIVYSRLFDWLVNKINTSIG-QDPSSKLL--IGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKM 469
Cdd:cd14889    315 AEDARDSIAKVAYGRVFGWIVSKINQLLApKDDSSVELreIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLM 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  470 EQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPKFSRSDFTIHH 549
Cdd:cd14889    395 EQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSRSKSPKFTVNH 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  550 YAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLF-----------------PPSEESTKSTKFTSIGSSFKQQL 612
Cdd:cd14889    475 YAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFtatrsrtgtlmpraklpQAGSDNFNSTRKQSVGAQFKHSL 554

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  613 QALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVlDESYD 692
Cdd:cd14889    555 GVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILLCEP-ALPGT 633

                          650       660
                   ....*....|....*....|....*..
gi 1002244077  693 EVTATEmLLEKVNLTGYQIGKTKVFLR 719
Cdd:cd14889    634 KQSCLR-ILKATKLVGWKCGKTRLFFK 659

MYSc_Myh2_insects_mollusks

cd14911

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...

78-719

1.33e-172

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: 533.02 E-value: 1.33e-172

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVSGE 157
Cdd:cd14911      3 VLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  158 SGAGKTESTKMLMQYLAFMGGKVQSGGRSV--------------QQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQF 223
Cdd:cd14911     82 SGAGKTENTKKVIQFLAYVAASKPKGSGAVphpavnpavligelEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  224 DQSGKISGAAIRTYLLERSRVCQISDPERNYHCFY-MLCSAPAEERERYKLGDPASFHYLNQSNcIKLDGMDDSSEYIAT 302
Cdd:cd14911    162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYqLLAGATPEQREKFILDDVKSYAFLSNGS-LPVPGVDDYAEFQAT 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  303 RRAMDIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSKfhLRTASELFMCDEEALEESLCKRVIATRgE 382
Cdd:cd14911    241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVA--QKIAHLLGLSVTDMTRAFLTPRIKVGR-D 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  383 SIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDP-SSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQH 461
Cdd:cd14911    318 FVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKrQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQL 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  462 FNQHVFKMEQEEYTKEEIDWSYIQF-VDNQEILDLIEkKPGGIIALLDETCMLRNSTHETFAEKLYqqfkgNQHFSRPKF 540
Cdd:cd14911    398 FNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPGGIMALLDEECWFPKATDKTFVDKLV-----SAHSMHPKF 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  541 SRS------DFTIHHYAGHVTYQTDLFLDKNIDyAVNEHQV-LLHASRCSFVSSLFPPSE---------------ESTKS 598
Cdd:cd14911    472 MKTdfrgvaDFAIVHYAGRVDYSAAKWLMKNMD-PLNENIVsLLQGSQDPFVVNIWKDAEivgmaqqaltdtqfgARTRK 550

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  599 TKFTSIGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDR 678
Cdd:cd14911    551 GMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQR 630

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....
gi 1002244077  679 FGVLLPEVLDESY-DEVTATEMLLEKVNLTG--YQIGKTKVFLR 719
Cdd:cd14911    631 YELLTPNVIPKGFmDGKKACEKMIQALELDSnlYRVGQSKIFFR 674

MYSc_Myo34

cd14895

class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...

76-719

3.32e-168

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: 522.59 E-value: 3.32e-168

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPHLYNNHMmeiYKGA--GFGELSPHPFAIADRAYRYMM-------NY 146
Cdd:cd14895      1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPGLYDLHK---YREEmpGWTALPPHVFSIAEGAYRSLRrrlhepgAS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  147 GVSQAILVSGESGAGKTESTKMLMQYLAFMGGKVQSGGRSVQQ------QVLESNPVLEAFGNAKTVRNNNSSRFGKFVE 220
Cdd:cd14895     78 KKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRraisgsELLSANPILESFGNARTLRNDNSSRFGKFVR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  221 IQF-----DQSGKISGAAIRTYLLERSRVCQISDPERNYHCFY-MLCSAPAEERERYKLGD--PASFHYLNQSNC-IKLD 291
Cdd:cd14895    158 MFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYeLLAGAADDMKLELQLELlsAQEFQYISGGQCyQRND 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  292 GMDDSSEYIATRRAMDIVGISSDEQDAIFRVVAAILHLGNVEFV----EGSEAD-----------SSVPKDDKSKFHLRT 356
Cdd:cd14895    238 GVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVasseDEGEEDngaasapcrlaSASPSSLTVQQHLDI 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  357 ASELFMCDEEALEESLCKRVIATRGESIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQ----DPSSKLL--- 429
Cdd:cd14895    318 VSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQrqfaLNPNKAAnkd 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  430 ----IGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIA 505
Cdd:cd14895    398 ttpcIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRPSGIFS 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  506 LLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPKFSRSD--FTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCS 583
Cdd:cd14895    478 LLDEECVVPKGSDAGFARKLYQRLQEHSNFSASRTDQADvaFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKTSDA 557

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  584 FVSSLF---------------PPSEESTKSTKFTSIGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQ 648
Cdd:cd14895    558 HLRELFeffkasesaelslgqPKLRRRSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSS 637

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002244077  649 QLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLlpeVLDESYDEVTATEmLLEKVNLTGYQIGKTKVFLR 719
Cdd:cd14895    638 QLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLL---VAAKNASDATASA-LIETLKVDHAELGKTRVFLR 704

MYSc_Myh15_mammals

cd14929

class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...

76-719

5.10e-165

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: 512.60 E-value: 5.10e-165

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVS 155
Cdd:cd14929      1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  156 GESGAGKTESTKMLMQYLAFMGGKVQSGGR--SVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGAA 233
Cdd:cd14929     80 GESGAGKTVNTKHIIQYFATIAAMIESKKKlgALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSAD 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  234 IRTYLLERSRVCQISDPERNYHCFYMLCSAPAEERERYKLG-DPASFHYLNqSNCIKLDGMDDSSEYIATRRAMDIVGIS 312
Cdd:cd14929    160 IDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSaNPSDFHFCS-CGAVAVESLDDAEELLATEQAMDILGFL 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  313 SDEQDAIFRVVAAILHLGNVEFV-----EGSEADSSVPKDDKSKFHLRTASELFMCdeealeesLCKRVIATRGESIVKN 387
Cdd:cd14929    239 PDEKYGCYKLTGAIMHFGNMKFKqkpreEQLEADGTENADKAAFLMGINSSELVKG--------LIHPRIKVGNEYVTRS 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  388 LDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVF 467
Cdd:cd14929    311 QNIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMF 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  468 KMEQEEYTKEEIDWSYIQF-VDNQEILDLIEkKPGGIIALLDETCMLRNSTHETFAEKLY-QQFKGNQHFSRPKFSRSDF 545
Cdd:cd14929    391 VLEQEEYRKEGIDWVSIDFgLDLQACIDLIE-KPMGIFSILEEECMFPKATDLTFKTKLFdNHFGKSVHFQKPKPDKKKF 469

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  546 TIH----HYAGHVTYQTDLFLDKNIDYaVNEHQV-LLHASRCSFVSSLFP---------PSEEST--KSTKFTSIGSSFK 609
Cdd:cd14929    470 EAHfelvHYAGVVPYNISGWLEKNKDL-LNETVVaVFQKSSNRLLASLFEnyistdsaiQFGEKKrkKGASFQTVASLHK 548

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  610 QQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVLDE 689
Cdd:cd14929    549 ENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPK 628

                          650       660       670
                   ....*....|....*....|....*....|....
gi 1002244077  690 S--YDEVTATEMLLE--KVNLTGYQIGKTKVFLR 719
Cdd:cd14929    629 SkfVSSRKAAEELLGslEIDHTQYRFGITKVFFK 662

PTZ00014

myosin-A; Provisional

66-779

1.08e-164

myosin-A; Provisional

Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 517.28 E-value: 1.08e-164

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   66 DMTRLAYLHEPGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPHLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMN 145
Cdd:PTZ00014   100 DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDKLPPHVFTTARRALENLHG 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  146 YGVSQAILVSGESGAGKTESTKMLMQYlaFMGGKVQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQ 225
Cdd:PTZ00014   180 VKKSQTIIVSGESGAGKTEATKQIMRY--FASSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGE 257

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  226 SGKISGAAIRTYLLERSRVCQISDPERNYHCFYMLCS-APAEERERYKLGDPASFHYLNqSNCIKLDGMDDSSEYIATRR 304
Cdd:PTZ00014   258 EGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKgANDEMKEKYKLKSLEEYKYIN-PKCLDVPGIDDVKDFEEVME 336

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  305 AMDIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEA---DSSVpKDDKSKFHLRTASELFMCDEEALEESLCKRVIATRG 381
Cdd:PTZ00014   337 SFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGgltDAAA-ISDESLEVFNEACELLFLDYESLKKELTVKVTYAGN 415

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  382 ESIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQH 461
Cdd:PTZ00014   416 QKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKN 495

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  462 FNQHVFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPKFS 541
Cdd:PTZ00014   496 FVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVD 575

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  542 -RSDFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFPPSE-ESTKSTKFTSIGSSFKQQLQALLETL 619
Cdd:PTZ00014   576 sNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEvEKGKLAKGQLIGSQFLNQLDSLMSLI 655

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  620 SSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVL-LPEVLDESYDEVTATE 698
Cdd:PTZ00014   656 NSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLdLAVSNDSSLDPKEKAE 735

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  699 MLLEKVNL--TGYQIGKTKVFLRAGQMAELDARRTEVLSSSASKIQRKVRSYLAHKHFIQLRLSATQLQAVCrGQIARHY 776
Cdd:PTZ00014   736 KLLERSGLpkDSYAIGKTMVFLKKDAAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKVRKNIKSLVRIQ-AHLRRHL 814


                   ...
gi 1002244077  777 YED 779
Cdd:PTZ00014   815 VIA 817

MYSc_Myo39

cd14900

class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...

78-682

5.77e-164

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: 508.69 E-value: 5.77e-164

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPHLYNNHMMEIY-----------KGAGFGELSPHPFAIADRAYRYMMNY 146
Cdd:cd14900      3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPGLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMMLG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  147 GVS----QAILVSGESGAGKTESTKMLMQYLAFMGG-------KVQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRF 215
Cdd:cd14900     83 LNGvmsdQSILVSGESGSGKTESTKFLMEYLAQAGDnnlaasvSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSRF 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  216 GKFVEIQFDQSGKISGAAIRTYLLERSRVCQISDPERNYHCFY-MLCSAPAEERERyklgdpasfHYLNQsncikldgmd 294
Cdd:cd14900    163 GKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYeMAIGASEAARKR---------DMYRR---------- 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  295 dsseyiaTRRAMDIVGISSDEQDAIFRVVAAILHLGNVEFV--EGSEADSSVPKD--DKSKFHLRTASELFMCDEEALEE 370
Cdd:cd14900    224 -------VMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEhdENSDRLGQLKSDlaPSSIWSRDAAATLLSVDATKLEK 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  371 SLCKRVIATRGESIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKL-----LIGVLDIYGFESFKTNS 445
Cdd:cd14900    297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKShgglhFIGILDIFGFEVFPKNS 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  446 FEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKL 525
Cdd:cd14900    377 FEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRPTGILSLIDEECVMPKGSDTTLASKL 456

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  526 YQQFKGNQHF--SRPKFSRSDFTIHHYAGHVTYQTDLFLDKNIDyavnehqvLLHASrcsfVSSLFppseestkstkftS 603
Cdd:cd14900    457 YRACGSHPRFsaSRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQE----AVDLF-------------V 511

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002244077  604 IGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVL 682
Cdd:cd14900    512 YGLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSL 590

MYSc_Myh10

cd14920

class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...

78-719

1.75e-163

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: 509.17 E-value: 1.75e-163

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVSGE 157
Cdd:cd14920      3 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  158 SGAGKTESTKMLMQYLAFM-----GGKVQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGA 232
Cdd:cd14920     82 SGAGKTENTKKVIQYLAHVasshkGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  233 AIRTYLLERSRVCQISDPERNYHCFY-MLCSAPAEERERYKLGDPASFHYLNQSNcIKLDGMDDSSEYIATRRAMDIVGI 311
Cdd:cd14920    162 NIETYLLEKSRAVRQAKDERTFHIFYqLLSGAGEHLKSDLLLEGFNNYRFLSNGY-IPIPGQQDKDNFQETMEAMHIMGF 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  312 SSDEQDAIFRVVAAILHLGNVEFVEGSEAD-SSVPKDDKSK--FHLrtaseLFMCDEEALEESLCKRVIATRgESIVKNL 388
Cdd:cd14920    241 SHEEILSMLKVVSSVLQFGNISFKKERNTDqASMPENTVAQklCHL-----LGMNVMEFTRAILTPRIKVGR-DYVQKAQ 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  389 DARAAALSRDALARIVYSRLFDWLVNKINTSIGQDP-SSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVF 467
Cdd:cd14920    315 TKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  468 KMEQEEYTKEEIDWSYIQF-VDNQEILDLIEK--KPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPKFSR-- 542
Cdd:cd14920    395 ILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKdk 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  543 SDFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLF-------PPSEES------------TKSTKFTS 603
Cdd:cd14920    475 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdvdrivGLDQVTgmtetafgsaykTKKGMFRT 554

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  604 IGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLL 683
Cdd:cd14920    555 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 634

                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1002244077  684 PEVLDESY-DEVTATEMLLEKVNLTG--YQIGKTKVFLR 719
Cdd:cd14920    635 PNAIPKGFmDGKQACERMIRALELDPnlYRIGQSKIFFR 673

MYSc_Myo41

cd14902

class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...

76-684

2.71e-163

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: 510.20 E-value: 2.71e-163

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPHLYNNHMMEIYK--------GAGFGELSPHPFAIADRAYRYMM-NY 146
Cdd:cd14902      1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPDLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLkPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  147 GVSQAILVSGESGAGKTESTKMLMQYLAFMGGKVQSGGRS------VQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVE 220
Cdd:cd14902     81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEgsdaveIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  221 IQFDQSGKISGAAIRTYLLERSRVCQISDPERNYHCFYMLCSAPAEERERYkLGDPASFHY--LNQSNC----IKLDGMD 294
Cdd:cd14902    161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDL-LGLQKGGKYelLNSYGPsfarKRAVADK 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  295 DSSEYIATRRAMDIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSKFHLRTASELFMCDEEALEESLCK 374
Cdd:cd14902    240 YAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSS 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  375 RVIATRGESIVKNLDARAAALSRDALARIVYSRLFDWLVNKIN---------TSIGQDPSSKLLIGVLDIYGFESFKTNS 445
Cdd:cd14902    320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSdeinyfdsaVSISDEDEELATIGILDIFGFESLNRNG 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  446 FEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKL 525
Cdd:cd14902    400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSNGLFSLLDQECLMPKGSNQALSTKF 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  526 YQQFKGnqhfsrpkfsRSDFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLF-------PPSEESTK- 597
Cdd:cd14902    480 YRYHGG----------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGadenrdsPGADNGAAg 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  598 -----STKFTSIGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTF 672
Cdd:cd14902    550 rrrysMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAH 629

                          650
                   ....*....|..
gi 1002244077  673 DEFVDRFGVLLP 684
Cdd:cd14902    630 ASFIELFSGFKC 641

MYSc_Myo14

cd14876

class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...

76-719

2.08e-162

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: 505.29 E-value: 2.08e-162

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPHLYNNhMMEIYKGAG-FGELSPHPFAIADRAYRYMMNYGVSQAILV 154
Cdd:cd14876      1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDE-WIRKYRDAPdLTKLPPHVFYTARRALENLHGVNKSQTIIV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  155 SGESGAGKTESTKMLMQYLAFMGGKVQSGgrSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGAAI 234
Cdd:cd14876     80 SGESGAGKTEATKQIMRYFASAKSGNMDL--RIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSV 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  235 RTYLLERSRVCQISDPERNYHCFYMLCS-APAEERERYKLGDPASFHYLNqSNCIKLDGMDDSSEYIATRRAMDIVGISS 313
Cdd:cd14876    158 VAFLLEKSRIVTQDDNERSYHIFYQLLKgADSEMKSKYHLLGLKEYKFLN-PKCLDVPGIDDVADFEEVLESLKSMGLTE 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  314 DEQDAIFRVVAAILHLGNVEFVEGSEA--DSSVPKDDKSKFHLRTASELFMCDEEALEESLCKRVIATRGESIVKNLDAR 391
Cdd:cd14876    237 EQIDTVFSIVSGVLLLGNVKITGKTEQgvDDAAAISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKD 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  392 AAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQ 471
Cdd:cd14876    317 DAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERES 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  472 EEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPKF-SRSDFTIHHY 550
Cdd:cd14876    397 KLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVdSNINFIVVHT 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  551 AGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFPPSE-ESTKSTKFTSIGSSFKQQLQALLETLSSVEPHYIRC 629
Cdd:cd14876    477 IGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVvEKGKIAKGSLIGSQFLKQLESLMGLINSTEPHFIRC 556

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  630 IKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVL-LPEVLDESYDEVTATEMLLEKVNLT- 707
Cdd:cd14876    557 IKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLdLGIANDKSLDPKVAALKLLESSGLSe 636

                          650
                   ....*....|...
gi 1002244077  708 -GYQIGKTKVFLR 719
Cdd:cd14876    637 dEYAIGKTMVFLK 649

MYSc_Myh1_insects_crustaceans

cd14909

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...

76-719

4.00e-160

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: 499.75 E-value: 4.00e-160

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVS 155
Cdd:cd14909      1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  156 GESGAGKTESTKMLMQYLAFMGG-----KVQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKIS 230
Cdd:cd14909     80 GESGAGKTENTKKVIAYFATVGAskktdEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  231 GAAIRTYLLERSRVCQISDPERNYHCFYMLCSAPAEERERYKL--GDPASFHYLNQSNcIKLDGMDDSSEYIATRRAMDI 308
Cdd:cd14909    160 GADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLlsDNIYDYYIVSQGK-VTVPNVDDGEEFSLTDQAFDI 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  309 VGISSDEQDAIFRVVAAILHLGNVEFV-----EGSEADSSVPKDDKSKfhlrtaseLFMCDEEALEESLCKRVIATRGES 383
Cdd:cd14909    239 LGFTKQEKEDVYRITAAVMHMGGMKFKqrgreEQAEQDGEEEGGRVSK--------LFGCDTAELYKNLLKPRIKVGNEF 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  384 IVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFN 463
Cdd:cd14909    311 VTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFN 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  464 QHVFKMEQEEYTKEEIDWSYIQF-VDNQEILDLIEkKPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQ-HFSRPKFS 541
Cdd:cd14909    391 HHMFVLEQEEYKREGIDWAFIDFgMDLLACIDLIE-KPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSaPFQKPKPP 469

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  542 R-----SDFTIHHYAGHVTYQTDLFLDKNIDyAVNEHQV-LLHASRCSFVSSLF---------PPSEESTKSTK---FTS 603
Cdd:cd14909    470 KpgqqaAHFAIAHYAGCVSYNITGWLEKNKD-PLNDTVVdQFKKSQNKLLIEIFadhagqsggGEQAKGGRGKKgggFAT 548

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  604 IGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLL 683
Cdd:cd14909    549 VSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILN 628

                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 1002244077  684 PEVLDESYDEVTATEMLLEKVNLTG--YQIGKTKVFLR 719
Cdd:cd14909    629 PAGIQGEEDPKKAAEIILESIALDPdqYRLGHTKVFFR 666

MYSc_Myo45

cd14906

class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...

78-683

9.63e-160

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: 500.66 E-value: 9.63e-160

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPHLYNNHMMEIYKGAGF-GELSPHPFAIADRAYRYMMNYGVSQAILVSG 156
Cdd:cd14906      3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISSIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  157 ESGAGKTESTKMLMQYLAFMGGKVQSGGR-------SVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQS-GK 228
Cdd:cd14906     83 ESGSGKTEASKTILQYLINTSSSNQQQNNnnnnnnnSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdGK 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  229 ISGAAIRTYLLERSRVCQISDPER-NYHCFY-MLCSAPAEERERYKL-GDPASFHYLNQSNCI-------------KLDG 292
Cdd:cd14906    163 IDGASIETYLLEKSRISHRPDNINlSYHIFYyLVYGASKDERSKWGLnNDPSKYRYLDARDDVissfksqssnknsNHNN 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  293 MDDSSE-YIATRRAMDIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSKFHLRTASELFMCDEEALEES 371
Cdd:cd14906    243 KTESIEsFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLESVSKLLGYIESVFKQA 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  372 LCKRVIAT--RGESIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSK-----------LLIGVLDIYGF 438
Cdd:cd14906    323 LLNRNLKAggRGSVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNdlaggsnkknnLFIGVLDIFGF 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  439 ESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTH 518
Cdd:cd14906    403 ENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKSDGILSLLDDECIMPKGSE 482

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  519 ETFAEKLYQQFKG-NQHFSRpKFSRSDFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFPPSEEST- 596
Cdd:cd14906    483 QSLLEKYNKQYHNtNQYYQR-TLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQITSTt 561

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  597 ----KSTKFTSIGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTF 672
Cdd:cd14906    562 nttkKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDF 641

                          650
                   ....*....|.
gi 1002244077  673 DEFVDRFGVLL 683
Cdd:cd14906    642 NQFFSRYKCIV 652

MYSc_Myh7b

cd14927

class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...

78-719

1.68e-159

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: 498.71 E-value: 1.68e-159

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVSGE 157
Cdd:cd14927      3 VLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  158 SGAGKTESTKMLMQYLAF-------MGGKVQSG----GRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQS 226
Cdd:cd14927     82 SGAGKTVNTKRVIQYFAIvaalgdgPGKKAQFLatktGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  227 GKISGAAIRTYLLERSRVCQISDPERNYHCFYMLCSAPAEERERYKL--GDPASFHYLNQSnCIKLDGMDDSSEYIATRR 304
Cdd:cd14927    162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLvsMNPYDYHFCSQG-VTTVDNMDDGEELMATDH 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  305 AMDIVGISSDEQDAIFRVVAAILHLGNVEFV-----EGSEADSSVPKDdkskfhlrTASELFMCDEEALEESLCKRVIAT 379
Cdd:cd14927    241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKqkqreEQAEADGTESAD--------KAAYLMGVSSADLLKGLLHPRVKV 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  380 RGESIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQ 459
Cdd:cd14927    313 GNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQ 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  460 QHFNQHVFKMEQEEYTKEEIDWSYIQF-VDNQEILDLIEkKPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQ-HFSR 537
Cdd:cd14927    393 QFFNHHMFILEQEEYKREGIEWVFIDFgLDLQACIDLIE-KPLGILSILEEECMFPKASDASFKAKLYDNHLGKSpNFQK 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  538 PKFSR-----SDFTIHHYAGHVTYQTDLFLDKNIDyAVNEHQV-LLHASRCSFVSSLF----------PP----SEESTK 597
Cdd:cd14927    472 PRPDKkrkyeAHFEVVHYAGVVPYNIVGWLDKNKD-PLNETVVaIFQKSQNKLLATLYenyvgsdsteDPksgvKEKRKK 550

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  598 STKFTSIGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVD 677
Cdd:cd14927    551 AASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQ 630

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*.
gi 1002244077  678 RFGVLLPEVL-DESY-DEVTATEMLLEKVNL--TGYQIGKTKVFLR 719
Cdd:cd14927    631 RYRILNPSAIpDDKFvDSRKATEKLLGSLDIdhTQYQFGHTKVFFK 676

MYSc_Myo19

cd14880

class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...

78-684

3.36e-158

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: 494.37 E-value: 3.36e-158

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPHLYNNHMMEIYKGAGFGE-LSPHPFAIADRAYRYMMNY--GVSQAILV 154
Cdd:cd14880      3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPQLYSPELMREYHAAPQPQkLKPHIFTVGEQTYRNVKSLiePVNQSIVV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  155 SGESGAGKTESTKMLMQYLAFMGGKVQSG-----GRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKI 229
Cdd:cd14880     83 SGESGAGKTWTSRCLMKFYAVVAASPTSWeshkiAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQM 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  230 SGAAIRTYLLERSRV-CQISDpERNYHCFYMLCS-APAEERERYKLGDPASFHYL-NQSNCIKLDGMDdsseyiATRRAM 306
Cdd:cd14880    163 TGAAVQTYLLEKTRVaCQAPS-ERNFHIFYQICKgASADERLQWHLPEGAAFSWLpNPERNLEEDCFE------VTREAM 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  307 DIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSKFHLRTASELFMCDEEALEESLCKRVI-ATRGESIV 385
Cdd:cd14880    236 LHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVRTSALLLKLPEDHLLETLQIRTIrAGKQQQVF 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  386 KNLDARAAA-LSRDALARIVYSRLFDWLVNKINTSIGQDPSS-KLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFN 463
Cdd:cd14880    316 KKPCSRAECdTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFV 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  464 QHVFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCML-RNSTHETFAEKLYQQFKGNQHFSRPKFSR 542
Cdd:cd14880    396 AHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSPISICSLINEECRLnRPSSAAQLQTRIESALAGNPCLGHNKLSR 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  543 S-DFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFPPSEE-------STKS-TKFTSIGSSFKQQLQ 613
Cdd:cd14880    476 EpSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEektqeepSGQSrAPVLTVVSKFKASLE 555

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002244077  614 ALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLP 684
Cdd:cd14880    556 QLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLRR 626

MYSc_Myh16

cd14934

class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...

78-719

3.22e-156

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: 489.15 E-value: 3.22e-156

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVSGE 157
Cdd:cd14934      3 VLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLP-IYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  158 SGAGKTESTKMLMQYLAFMG--GKVQSGGR-SVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGAAI 234
Cdd:cd14934     82 SGAGKTENTKKVIQYFANIGgtGKQSSDGKgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGADI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  235 RTYLLERSRVCQISDPERNYHCFYMLCS--APAEERERYKLGDPASFHYLNQSnCIKLDGMDDSSEYIATRRAMDIVGIS 312
Cdd:cd14934    162 ESYLLEKSRVISQQAAERGYHIFYQILSnkKPELIESLLLVPNPKEYHWVSQG-VTVVDNMDDGEELQITDVAFDVLGFS 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  313 SDEQDAIFRVVAAILHLGNVEFV-----EGSEADSSVPKDdkskfhlrTASELFMCDEEALEESLCKRVIATRGESIVKN 387
Cdd:cd14934    241 AEEKIGVYKLTGGIMHFGNMKFKqkpreEQAEVDTTEVAD--------KVAHLMGLNSGELQKGITRPRVKVGNEFVQKG 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  388 LDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVF 467
Cdd:cd14934    313 QNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  468 KMEQEEYTKEEIDWSYIQF-VDNQEILDLIEkKPGGIIALLDETCMLRNSTHETFAEKLYQQFKG-NQHFSRPKFSR--- 542
Cdd:cd14934    393 VLEQEEYKREGIEWVFIDFgLDLQACIDLLE-KPMGIFSILEEQCVFPKATDATFKAALYDNHLGkSSNFLKPKGGKgkg 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  543 --SDFTIHHYAGHVTYQTDLFLDKNIDyAVNEHQVLLHASRCSFVSSLFPPSEESTKSTKFTSIGSSF-------KQQLQ 613
Cdd:cd14934    472 peAHFELVHYAGTVGYNITGWLEKNKD-PLNETVVGLFQKSSLGLLALLFKEEEAPAGSKKQKRGSSFmtvsnfyREQLN 550

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  614 ALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVLDESY-D 692
Cdd:cd14934    551 KLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQGFvD 630

                          650       660
                   ....*....|....*....|....*....
gi 1002244077  693 EVTATEMLLEKVNL--TGYQIGKTKVFLR 719
Cdd:cd14934    631 NKKASELLLGSIDLdvNEYKIGHTKVFFR 659

MYSc_Myh3

cd14913

class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...

76-719

9.82e-155

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: 485.71 E-value: 9.82e-155

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVS 155
Cdd:cd14913      1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  156 GESGAGKTESTKMLMQYLAFMGGKVQSGGR-------SVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGK 228
Cdd:cd14913     80 GESGAGKTVNTKRVIQYFATIAATGDLAKKkdskmkgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  229 ISGAAIRTYLLERSRVCQISDPERNYHCFYMLCSAPAEERERYKL--GDPASFHYLNQSNcIKLDGMDDSSEYIATRRAM 306
Cdd:cd14913    160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLitTNPYDYPFISQGE-ILVASIDDAEELLATDSAI 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  307 DIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPkdDKSKFHLRTASeLFMCDEEALEESLCKRVIATRGESIVK 386
Cdd:cd14913    239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEP--DGTEVADKTAY-LMGLNSSDLLKALCFPRVKVGNEYVTK 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  387 NLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHV 466
Cdd:cd14913    316 GQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHM 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  467 FKMEQEEYTKEEIDWSYIQF-VDNQEILDLIEkKPGGIIALLDETCMLRNSTHETFAEKLYQQFKG-NQHFSRPKFSR-- 542
Cdd:cd14913    396 FVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLGkSNNFQKPKVVKgr 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  543 --SDFTIHHYAGHVTYQTDLFLDKNIDyAVNEHQV-LLHASRCSFVSSLFP-------PSEE----STKSTKFTSIGSSF 608
Cdd:cd14913    475 aeAHFSLIHYAGTVDYSVSGWLEKNKD-PLNETVVgLYQKSSNRLLAHLYAtfatadaDSGKkkvaKKKGSSFQTVSALF 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  609 KQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVLD 688
Cdd:cd14913    554 RENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIP 633

                          650       660       670
                   ....*....|....*....|....*....|....*
gi 1002244077  689 ES--YDEVTATEMLLEKVNL--TGYQIGKTKVFLR 719
Cdd:cd14913    634 EGqfIDSKKACEKLLASIDIdhTQYKFGHTKVFFK 668

MYSc_Myh18

cd14932

class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...

78-719

1.05e-152

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: 480.29 E-value: 1.05e-152

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVSGE 157
Cdd:cd14932      3 VLHNLKERYYSGLIYTYSGLFCVVINPYKYLP-IYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  158 SGAGKTESTKMLMQYLAFM----------GGKVQSGGRsVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSG 227
Cdd:cd14932     82 SGAGKTENTKKVIQYLAYVassfktkkdqSSIALSHGE-LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  228 KISGAAIRTYLLERSRVCQISDPERNYHCF-YMLCSAPAEERERYKLGDPASFHYLNQSNcIKLDGMDDSSEYIATRRAM 306
Cdd:cd14932    161 YIVGANIETYLLEKSRAIRQAKDERAFHIFyYLLTGAGDKLRSELCLEDYSKYRFLSNGN-VTIPGQQDKELFAETMEAF 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  307 DIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSKfhlRTASELFMCDEEALEESLCKRVIATRGESIVK 386
Cdd:cd14932    240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAA---QKVCHLLGMNVTDFTRAILSPRIKVGRDYVQK 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  387 NLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDP-SSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQH 465
Cdd:cd14932    317 AQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  466 VFKMEQEEYTKEEIDWSYIQF-VDNQEILDLIEKK--PGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPKFSR 542
Cdd:cd14932    397 MFILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLK 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  543 --SDFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFPPSEE------------------STKSTKFT 602
Cdd:cd14932    477 ddADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRivgldkvagmgeslhgafKTRKGMFR 556

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  603 SIGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVL 682
Cdd:cd14932    557 TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 636

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|
gi 1002244077  683 LPEVLDESY-DEVTATEMLLEKVNLTG--YQIGKTKVFLR 719
Cdd:cd14932    637 TPNAIPKGFmDGKQACVLMVKALELDPnlYRIGQSKVFFR 676

MYSc_Myo35

cd14896

class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...

76-719

2.13e-152

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: 478.51 E-value: 2.13e-152

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVS 155
Cdd:cd14896      1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLP-LFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  156 GESGAGKTESTKMLMQYLAFMGgkvQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFdQSGKISGAAIR 235
Cdd:cd14896     80 GHSGSGKTEAAKKIVQFLSSLY---QDQTEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVS 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  236 TYLLERSRVCQISDPERNYHCFY-MLCSAPAEERERYKLGDPASFHYLNQSNCIKLDGMDDSSEYIATRRAMDIVGISSD 314
Cdd:cd14896    156 HYLLETSRVVFQAQAERSFHVFYeLLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAE 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  315 EQDAIFRVVAAILHLGNVEFvEGSEADSSVPKDDKSKFHLRTASELFMCDEEALEESLCKRVIATRGESIVKNLDARAAA 394
Cdd:cd14896    236 ELTAIWAVLAAILQLGNICF-SSSERESQEVAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAI 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  395 LSRDALARIVYSRLFDWLVNKINTSIG--QDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQE 472
Cdd:cd14896    315 DARDALAKTLYSRLFTWLLKRINAWLAppGEAESDATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEE 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  473 EYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPKFSRSDFTIHHYAG 552
Cdd:cd14896    395 ECQRELLPWVPIPQPPRESCLDLLVDQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQLPLPVFTVRHYAG 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  553 HVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFPPSEEST--KSTKFTsIGSSFKQQLQALLETLSSVEPHYIRCI 630
Cdd:cd14896    475 TVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYglGQGKPT-LASRFQQSLGDLTARLGRSHVYFIHCL 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  631 KPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVLDESYDEVTATEMLLEKVNLTG-- 708
Cdd:cd14896    554 NPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEALSDRERCGAILSQVLGAESpl 633

                          650
                   ....*....|.
gi 1002244077  709 YQIGKTKVFLR 719
Cdd:cd14896    634 YHLGATKVLLK 644

MYSc_Myh7

cd14917

class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...

76-719

4.09e-148

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: 468.04 E-value: 4.09e-148

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVS 155
Cdd:cd14917      1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  156 GESGAGKTESTKMLMQYLAFMGG------KVQSGGR-SVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGK 228
Cdd:cd14917     80 GESGAGKTVNTKRVIQYFAVIAAigdrskKDQTPGKgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  229 ISGAAIRTYLLERSRVCQISDPERNYHCFYMLCSAPAEERERYKL--GDPASFHYLNQSNcIKLDGMDDSSEYIATRRAM 306
Cdd:cd14917    160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLitNNPYDYAFISQGE-TTVASIDDAEELMATDNAF 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  307 DIVGISSDEQDAIFRVVAAILHLGNVEFV-----EGSEADSSvPKDDKSKFhlrtaseLFMCDEEALEESLCKRVIATRG 381
Cdd:cd14917    239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKqkqreEQAEPDGT-EEADKSAY-------LMGLNSADLLKGLCHPRVKVGN 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  382 ESIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQH 461
Cdd:cd14917    311 EYVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  462 FNQHVFKMEQEEYTKEEIDWSYIQF-VDNQEILDLIEkKPGGIIALLDETCMLRNSTHETFAEKLYQQFKG-NQHFSRPK 539
Cdd:cd14917    391 FNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNHLGkSNNFQKPR 469

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  540 FSR----SDFTIHHYAGHVTYQTDLFLDKNIDyAVNEHQV-LLHASRCSFVSSLF-------PPSE----ESTKSTKFTS 603
Cdd:cd14917    470 NIKgkpeAHFSLIHYAGTVDYNIIGWLQKNKD-PLNETVVgLYQKSSLKLLSNLFanyagadAPIEkgkgKAKKGSSFQT 548

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  604 IGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLL 683
Cdd:cd14917    549 VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 628

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|
gi 1002244077  684 PEVLDES--YDEVTATEMLLEKVNL--TGYQIGKTKVFLR 719
Cdd:cd14917    629 PAAIPEGqfIDSRKGAEKLLSSLDIdhNQYKFGHTKVFFK 668

MYSc_Myh9

cd14919

class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...

78-719

7.20e-148

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: 467.26 E-value: 7.20e-148

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVSGE 157
Cdd:cd14919      3 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  158 SGAGKTESTKMLMQYLAFMGG--KVQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGAAIR 235
Cdd:cd14919     82 SGAGKTENTKKVIQYLAHVASshKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  236 TYLLERSRVCQISDPERNYHCFYMLCSAPAEERERYKLGDPASFHYLNQSNCIKLDGMDDSSEYIATRRAMDIVGISSDE 315
Cdd:cd14919    162 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEE 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  316 QDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSKfhlRTASELFMCDEEALEESLCKRVIATRGESIVKNLDARAAAL 395
Cdd:cd14919    242 QMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAA---QKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  396 SRDALARIVYSRLFDWLVNKINTSIGQDP-SSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEY 474
Cdd:cd14919    319 AIEALAKATYERMFRWLVLRINKALDKTKrQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  475 TKEEIDWSYIQF-VDNQEILDLIEKK--PGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPK--FSRSDFTIHH 549
Cdd:cd14919    399 QREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKqlKDKADFCIIH 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  550 YAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFP-------------------PSEESTKSTKFTSIGSSFKQ 610
Cdd:cd14919    479 YAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKdvdriigldqvagmsetalPGAFKTRKGMFRTVGQLYKE 558

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  611 QLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVLDES 690
Cdd:cd14919    559 QLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKG 638

                          650       660       670
                   ....*....|....*....|....*....|..
gi 1002244077  691 Y-DEVTATEMLLEKVNLTG--YQIGKTKVFLR 719
Cdd:cd14919    639 FmDGKQACVLMIKALELDSnlYRIGQSKVFFR 670

MYSc_Myh4

cd14915

class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...

76-719

4.58e-145

class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 459.97 E-value: 4.58e-145

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVS 155
Cdd:cd14915      1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  156 GESGAGKTESTKMLMQYLAFMG------------GKVQSggrSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQF 223
Cdd:cd14915     80 GESGAGKTVNTKRVIQYFATIAvtgekkkeeaasGKMQG---TLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  224 DQSGKISGAAIRTYLLERSRVCQISDPERNYHCFYMLCSAPAEERERYKL--GDPASFHYLNQSNcIKLDGMDDSSEYIA 301
Cdd:cd14915    157 GATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLitTNPYDFAFVSQGE-ITVPSIDDQEELMA 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  302 TRRAMDIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSKfhlRTASELFMCDEEALEESLCKRVIATRG 381
Cdd:cd14915    236 TDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA---DKAAYLTSLNSADLLKALCYPRVKVGN 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  382 ESIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQH 461
Cdd:cd14915    313 EYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQF 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  462 FNQHVFKMEQEEYTKEEIDWSYIQF-VDNQEILDLIEkKPGGIIALLDETCMLRNSTHETFAEKLYQQFKG-NQHFSRPK 539
Cdd:cd14915    393 FNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHLGkSNNFQKPK 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  540 FSR----SDFTIHHYAGHVTYQTDLFLDKNIDyAVNEHQV-LLHASRCSFVSSLFPPSEES------------TKSTKFT 602
Cdd:cd14915    472 PAKgkaeAHFSLVHYAGTVDYNIAGWLDKNKD-PLNETVVgLYQKSGMKTLAFLFSGGQTAeaeggggkkggkKKGSSFQ 550

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  603 SIGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVL 682
Cdd:cd14915    551 TVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 630

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 1002244077  683 LPEVLDES--YDEVTATEMLLEKVNL--TGYQIGKTKVFLR 719
Cdd:cd14915    631 NASAIPEGqfIDSKKASEKLLGSIDIdhTQYKFGHTKVFFK 671

MYSc_Myh1_mammals

cd14910

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...

76-719

4.13e-144

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: 457.27 E-value: 4.13e-144

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVS 155
Cdd:cd14910      1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  156 GESGAGKTESTKMLMQYLAFMG------------GKVQSggrSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQF 223
Cdd:cd14910     80 GESGAGKTVNTKRVIQYFATIAvtgekkkeeatsGKMQG---TLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  224 DQSGKISGAAIRTYLLERSRVCQISDPERNYHCFYMLCSAPAEERERYKL--GDPASFHYLNQSNcIKLDGMDDSSEYIA 301
Cdd:cd14910    157 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLitTNPYDYAFVSQGE-ITVPSIDDQEELMA 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  302 TRRAMDIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSKfhlRTASELFMCDEEALEESLCKRVIATRG 381
Cdd:cd14910    236 TDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA---DKAAYLQNLNSADLLKALCYPRVKVGN 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  382 ESIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQH 461
Cdd:cd14910    313 EYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQF 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  462 FNQHVFKMEQEEYTKEEIDWSYIQF-VDNQEILDLIEkKPGGIIALLDETCMLRNSTHETFAEKLYQQFKG-NQHFSRPK 539
Cdd:cd14910    393 FNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHLGkSNNFQKPK 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  540 FSR----SDFTIHHYAGHVTYQTDLFLDKNIDyAVNEHQV-LLHASRCSFVSSLFPPSEES------------TKSTKFT 602
Cdd:cd14910    472 PAKgkveAHFSLIHYAGTVDYNIAGWLDKNKD-PLNETVVgLYQKSSMKTLALLFSGAAAAeaeegggkkggkKKGSSFQ 550

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  603 SIGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVL 682
Cdd:cd14910    551 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 630

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 1002244077  683 LPEVLDES--YDEVTATEMLLEKVNL--TGYQIGKTKVFLR 719
Cdd:cd14910    631 NASAIPEGqfIDSKKASEKLLGSIDIdhTQYKFGHTKVFFK 671

MYSc_Myh19

cd15896

class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...

78-719

3.32e-143

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: 454.91 E-value: 3.32e-143

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVSGE 157
Cdd:cd15896      3 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  158 SGAGKTESTKMLMQYLAFMGGK----------VQSGGRsVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSG 227
Cdd:cd15896     82 SGAGKTENTKKVIQYLAHVASShktkkdqnslALSHGE-LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  228 KISGAAIRTYLLERSRVCQISDPERNYHCF-YMLCSAPAEERERYKLGDPASFHYLNQSNcIKLDGMDDSSEYIATRRAM 306
Cdd:cd15896    161 YIVGANIETYLLEKSRAIRQAKEERTFHIFyYLLTGAGDKLRSELLLENYNNYRFLSNGN-VTIPGQQDKDLFTETMEAF 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  307 DIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSKfhlRTASELFMCDEEALEESLCKRVIATRGESIVK 386
Cdd:cd15896    240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAA---QKVCHLMGMNVTDFTRAILSPRIKVGRDYVQK 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  387 NLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDP-SSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQH 465
Cdd:cd15896    317 AQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  466 VFKMEQEEYTKEEIDWSYIQF-VDNQEILDLIEK--KPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPKFSR 542
Cdd:cd15896    397 MFILEQEEYQREGIEWSFIDFgLDLQPCIDLIEKpaSPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLK 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  543 --SDFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFP-----------------PSEESTKSTKFTS 603
Cdd:cd15896    477 deADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKdvdrivgldkvsgmsemPGAFKTRKGMFRT 556

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  604 IGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLL 683
Cdd:cd15896    557 VGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 636

                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1002244077  684 PEVLDESY-DEVTATEMLLEKVNLTG--YQIGKTKVFLR 719
Cdd:cd15896    637 PNAIPKGFmDGKQACVLMIKSLELDPnlYRIGQSKVFFR 675

MYSc_Myh8

cd14918

class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...

76-719

1.22e-142

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: 453.42 E-value: 1.22e-142

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVS 155
Cdd:cd14918      1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  156 GESGAGKTESTKMLMQYLAFMG----------GKVQSggrSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQ 225
Cdd:cd14918     80 GESGAGKTVNTKRVIQYFATIAvtgekkkeesGKMQG---TLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  226 SGKISGAAIRTYLLERSRVCQISDPERNYHCFYMLCSAPAEERERYKL--GDPASFHYLNQSNcIKLDGMDDSSEYIATR 303
Cdd:cd14918    157 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLitTNPYDYAFVSQGE-ITVPSIDDQEELMATD 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  304 RAMDIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSKfhlRTASELFMCDEEALEESLCKRVIATRGES 383
Cdd:cd14918    236 SAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA---DKAAYLQSLNSADLLKALCYPRVKVGNEY 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  384 IVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFN 463
Cdd:cd14918    313 VTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  464 QHVFKMEQEEYTKEEIDWSYIQF-VDNQEILDLIEkKPGGIIALLDETCMLRNSTHETFAEKLYQQFKG-NQHFSRPKF- 540
Cdd:cd14918    393 HHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQHLGkSANFQKPKVv 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  541 ---SRSDFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFP--PSEESTKSTK---------FTSIGS 606
Cdd:cd14918    472 kgkAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFStyASAEADSGAKkgakkkgssFQTVSA 551

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  607 SFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEV 686
Cdd:cd14918    552 LFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASA 631

                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1002244077  687 LDES--YDEVTATEMLLEKVNL--TGYQIGKTKVFLR 719
Cdd:cd14918    632 IPEGqfIDSKKASEKLLASIDIdhTQYKFGHTKVFFK 668

MYSc_Myh11

cd14921

class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...

78-719

1.37e-142

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: 453.32 E-value: 1.37e-142

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVSGE 157
Cdd:cd14921      3 VLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  158 SGAGKTESTKMLMQYLAFM-----GGKVQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGA 232
Cdd:cd14921     82 SGAGKTENTKKVIQYLAVVasshkGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  233 AIRTYLLERSRVCQISDPERNYHCFYMLCSAPAEE-RERYKLGDPASFHYLNQSNcIKLDGMDDSSEYIATRRAMDIVGI 311
Cdd:cd14921    162 NIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKmRSDLLLEGFNNYTFLSNGF-VPIPAAQDDEMFQETLEAMSIMGF 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  312 SSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDkskfhlrTASELfMCDEEALEESLCKRVIATR----GESIVKN 387
Cdd:cd14921    241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDN-------TAAQK-VCHLMGINVTDFTRSILTPrikvGRDVVQK 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  388 LDARAAA-LSRDALARIVYSRLFDWLVNKINTSIGQDP-SSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQH 465
Cdd:cd14921    313 AQTKEQAdFAIEALAKATYERLFRWILTRVNKALDKTHrQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  466 VFKMEQEEYTKEEIDWSYIQF-VDNQEILDLIEK--KPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPK--F 540
Cdd:cd14921    393 MFILEQEEYQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKqlK 472

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  541 SRSDFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFP-------------------PSEESTKSTKF 601
Cdd:cd14921    473 DKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKdvdrivgldqmakmtesslPSASKTKKGMF 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  602 TSIGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGV 681
Cdd:cd14921    553 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 1002244077  682 LLPEVLDESYDEVTATEMLLEK---VNLTGYQIGKTKVFLR 719
Cdd:cd14921    633 LAANAIPKGFMDGKQACILMIKaleLDPNLYRIGQSKIFFR 673

MYSc_Myh6

cd14916

class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...

76-719

1.03e-141

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: 450.66 E-value: 1.03e-141

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVS 155
Cdd:cd14916      1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  156 GESGAGKTESTKMLMQYLAFMGGKVQSGGR--------SVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSG 227
Cdd:cd14916     80 GESGAGKTVNTKRVIQYFASIAAIGDRSKKenpnankgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  228 KISGAAIRTYLLERSRVCQISDPERNYHCFYMLCSAPAEERERYKL--GDPASFHYLNQSNcIKLDGMDDSSEYIATRRA 305
Cdd:cd14916    160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLvtNNPYDYAFVSQGE-VSVASIDDSEELLATDSA 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  306 MDIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKD----DKSKFhlrtaseLFMCDEEALEESLCKRVIATRG 381
Cdd:cd14916    239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGtedaDKSAY-------LMGLNSADLLKGLCHPRVKVGN 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  382 ESIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQH 461
Cdd:cd14916    312 EYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  462 FNQHVFKMEQEEYTKEEIDWSYIQF-VDNQEILDLIEkKPGGIIALLDETCMLRNSTHETFAEKLYQQFKG-NQHFSRPK 539
Cdd:cd14916    392 FNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKLYDNHLGkSNNFQKPR 470

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  540 F----SRSDFTIHHYAGHVTYQTDLFLDKNIDyAVNEHQV-LLHASRCSFVSSLFPP-----SEESTKSTKFTSIGSSF- 608
Cdd:cd14916    471 NvkgkQEAHFSLVHYAGTVDYNILGWLEKNKD-PLNETVVgLYQKSSLKLMATLFSTyasadTGDSGKGKGGKKKGSSFq 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  609 ------KQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVL 682
Cdd:cd14916    550 tvsalhRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 629

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 1002244077  683 LPEVLDES--YDEVTATEMLLEKVNL--TGYQIGKTKVFLR 719
Cdd:cd14916    630 NPAAIPEGqfIDSRKGAEKLLGSLDIdhNQYKFGHTKVFFK 670

MYSc_Myh2_mammals

cd14912

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...

76-719

5.43e-141

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: 448.80 E-value: 5.43e-141

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVS 155
Cdd:cd14912      1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  156 GESGAGKTESTKMLMQYLAFMG------------GKVQSggrSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQF 223
Cdd:cd14912     80 GESGAGKTVNTKRVIQYFATIAvtgekkkeeitsGKMQG---TLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  224 DQSGKISGAAIRTYLLERSRVCQISDPERNYHCFYMLCSAPAEERERYKL--GDPASFHYLNQSNcIKLDGMDDSSEYIA 301
Cdd:cd14912    157 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLitTNPYDYPFVSQGE-ISVASIDDQEELMA 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  302 TRRAMDIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSKfhlRTASELFMCDEEALEESLCKRVIATRG 381
Cdd:cd14912    236 TDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVA---DKAAYLQSLNSADLLKALCYPRVKVGN 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  382 ESIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQH 461
Cdd:cd14912    313 EYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQF 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  462 FNQHVFKMEQEEYTKEEIDWSYIQF-VDNQEILDLIEkKPGGIIALLDETCMLRNSTHETFAEKLYQQFKG-NQHFSRPK 539
Cdd:cd14912    393 FNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHLGkSANFQKPK 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  540 F----SRSDFTIHHYAGHVTYQTDLFLDKNIDyAVNEHQV-LLHASRCSFVSSLFPPSEES--------------TKSTK 600
Cdd:cd14912    472 VvkgkAEAHFSLIHYAGVVDYNITGWLDKNKD-PLNETVVgLYQKSAMKTLAYLFSGAQTAegasagggakkggkKKGSS 550

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  601 FTSIGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFG 680
Cdd:cd14912    551 FQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 630

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|...
gi 1002244077  681 VLLPEVLDES--YDEVTATEMLLEKVNL--TGYQIGKTKVFLR 719
Cdd:cd14912    631 VLNASAIPEGqfIDSKKASEKLLASIDIdhTQYKFGHTKVFFK 673

MYSc_Myh13

cd14923

class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...

76-719

1.86e-140

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: 447.59 E-value: 1.86e-140

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVS 155
Cdd:cd14923      1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  156 GESGAGKTESTKMLMQYLAFMG-----------GKVQSggrSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFD 224
Cdd:cd14923     80 GESGAGKTVNTKRVIQYFATIAvtgdkkkeqqpGKMQG---TLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  225 QSGKISGAAIRTYLLERSRVCQISDPERNYHCFYMLCSAPAEERERYKL--GDPASFHYLNQSNcIKLDGMDDSSEYIAT 302
Cdd:cd14923    157 ATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLisTNPFDFPFVSQGE-VTVASIDDSEELLAT 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  303 RRAMDIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSKfhlRTASELFMCDEEALEESLCKRVIATRGE 382
Cdd:cd14923    236 DNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA---DKAGYLMGLNSAEMLKGLCCPRVKVGNE 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  383 SIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHF 462
Cdd:cd14923    313 YVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  463 NQHVFKMEQEEYTKEEIDWSYIQF-VDNQEILDLIEkKPGGIIALLDETCMLRNSTHETFAEKLYQQFKG-NQHFSRPKF 540
Cdd:cd14923    393 NHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLGkSNNFQKPKP 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  541 SR----SDFTIHHYAGHVTYQTDLFLDKNIDyAVNEHQVLLHASRC----SFVSSLFPPSEE----------STKSTKFT 602
Cdd:cd14923    472 AKgkaeAHFSLVHYAGTVDYNIAGWLDKNKD-PLNETVVGLYQKSSlkllSFLFSNYAGAEAgdsggskkggKKKGSSFQ 550

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  603 SIGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVL 682
Cdd:cd14923    551 TVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRIL 630

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 1002244077  683 LPEVLDES--YDEVTATEMLLEKVNL--TGYQIGKTKVFLR 719
Cdd:cd14923    631 NASAIPEGqfIDSKNASEKLLNSIDVdrEQYRFGHTKVFFK 671

MYSc_Myo25

cd14886

class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...

78-719

3.96e-140

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: 445.87 E-value: 3.96e-140

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPHLYNNHMMEIYKGA----GF-GELSPHPFAIADRAYRYMMNYGVSQAI 152
Cdd:cd14886      3 VIDILRDRFAKDKIYTYAGKLLVALNPFKQIRNLYGTEVIGRYRQAdtsrGFpSDLPPHSYAVAQSALNGLISDGISQSC 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  153 LVSGESGAGKTESTKMLMQYLAFmggKVQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGA 232
Cdd:cd14886     83 IVSGESGAGKTETAKQLMNFFAY---GHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  233 AIRTYLLERSRVCQISDPERNYHCFY-MLCSAPAEERERYKLGDPASFHYLNQSNCIKLDGMDDSSEYIATRRAMDIVgI 311
Cdd:cd14886    160 KITSYMLELSRIEFQSTNERNYHIFYqCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKL-F 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  312 SSDEQDAIFRVVAAILHLGNVEFVEGSE--ADSSVPKDDKSKFhlRTASELFMCDEEALEESLCKRVIATRGESIVKNLD 389
Cdd:cd14886    239 SKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDF--GKMCELLGIESSKAAQAIITKVVVINNETIISPVT 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  390 ARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKM 469
Cdd:cd14886    317 QAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKS 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  470 EQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFKgNQHFSRPKFSRSDFTIHH 549
Cdd:cd14886    397 EIQEYEIEGIDHSMITFTDNSNVLAVFDKPNLSIFSFLEEQCLIQTGSSEKFTSSCKSKIK-NNSFIPGKGSQCNFTIVH 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  550 YAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFP--PSEESTKSTKFtsIGSSFKQQLQALLETLSSVEPHYI 627
Cdd:cd14886    476 TAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSdiPNEDGNMKGKF--LGSTFQLSIDQLMKTLSATKSHFI 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  628 RCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLL---PEVLDESYDEVTATEMLLEKV 704
Cdd:cd14886    554 RCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILIshnSSSQNAGEDLVEAVKSILENL 633

                          650
                   ....*....|....*..
gi 1002244077  705 NL--TGYQIGKTKVFLR 719
Cdd:cd14886    634 GIpcSDYRIGKTKVFLR 650

MYSc_Myh14_mammals

cd14930

class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...

78-719

5.82e-137

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: 437.99 E-value: 5.82e-137

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVSGE 157
Cdd:cd14930      3 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  158 SGAGKTESTKMLMQYLAFMG----GKVQSG-GRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGA 232
Cdd:cd14930     82 SGAGKTENTKKVIQYLAHVAsspkGRKEPGvPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  233 AIRTYLLERSRVCQISDPERNYHCFYMLCSAPAEERERYKLGDPASfHYLNQSNCIKLDGMDDSSEYIATRRAMDIVGIS 312
Cdd:cd14930    162 NIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCS-HYRFLTNGPSSSPGQERELFQETLESLRVLGFS 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  313 SDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSKFHLRTASELFMCDeeaLEESLCKRVIATRGESIVKNLDARA 392
Cdd:cd14930    241 HEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTD---FSRALLTPRIKVGRDYVQKAQTKEQ 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  393 AALSRDALARIVYSRLFDWLVNKINTSIGQDP-SSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQ 471
Cdd:cd14930    318 ADFALEALAKATYERLFRWLVLRLNRALDRSPrQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQ 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  472 EEYTKEEIDWSYIQF-VDNQEILDLIEK--KPGGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPKFSR--SDFT 546
Cdd:cd14930    398 EEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRdqADFS 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  547 IHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLF------------------PPSEESTKSTkFTSIGSSF 608
Cdd:cd14930    478 VLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvegivgleqvsslgdgPPGGRPRRGM-FRTVGQLY 556

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  609 KQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVLD 688
Cdd:cd14930    557 KESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIP 636

                          650       660       670
                   ....*....|....*....|....*....|....
gi 1002244077  689 ESY-DEVTATEMLLEKVNLTG--YQIGKTKVFLR 719
Cdd:cd14930    637 KGFmDGKQACEKMIQALELDPnlYRVGQSKIFFR 670

MYSc_Myo38

cd14899

class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...

78-719

2.25e-135

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: 435.29 E-value: 2.25e-135

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPHLYNNHMMEIYK---GAGFGE-------LSPHPFAIADRAYRYMMNYG 147
Cdd:cd14899      3 ILNALRLRYERHAIYTHIGDILISINPFQDLPQLYGDEILRGYAydhNSQFGDrvtstdpREPHLFAVARAAYIDIVQNG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  148 VSQAILVSGESGAGKTESTKMLMQYLAFMGGKVQSGGR--------------SVQQQVLESNPVLEAFGNAKTVRNNNSS 213
Cdd:cd14899     83 RSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTnsesisppaspsrtTIEEQVLQSNPILEAFGNARTVRNDNSS 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  214 RFGKFVEIQF-DQSGKISGAAIRTYLLERSRVCQISDPERNYHCFYMLCSAPA-----EERERYKL-GDPASFHYLNQSN 286
Cdd:cd14899    163 RFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADNncvskEQKQVLALsGGPQSFRLLNQSL 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  287 CIKL-DGMDDSSEYIATRRAMDIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSKF---------HLRT 356
Cdd:cd14899    243 CSKRrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKGDDTVFADEARVmssttgafdHFTK 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  357 ASELFMCDEEALEESLCKRVIATRGESIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPS----------- 425
Cdd:cd14899    323 AAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASapwgadesdvd 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  426 ----SKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPG 501
Cdd:cd14899    403 deedATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHRPI 482

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  502 GIIALLDETCMLRNSTHETFAEKLYQQF---KGNQHF-SRPKFSR-SDFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVL 576
Cdd:cd14899    483 GIFSLTDQECVFPQGTDRALVAKYYLEFekkNSHPHFrSAPLIQRtTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAAQL 562

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  577 LHASRCSFVSSLFPPSEE-------------------STKSTKFTSIGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLK 637
Cdd:cd14899    563 LAGSSNPLIQALAAGSNDedangdseldgfggrtrrrAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIKPNDSHV 642

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  638 PAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVldesydeVTATEMLLEKVNLTGYQIGKTKVF 717
Cdd:cd14899    643 GSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYRRVLLSL-------YKWGDNDFERQMRCGVSLGKTRVF 715


                   ..
gi 1002244077  718 LR 719
Cdd:cd14899    716 FR 717

MYSc_Myo13

cd14875

class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...

78-719

1.28e-133

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: 428.84 E-value: 1.28e-133

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRY-GMNEIYTYTGNILIAVNPFQRLPHLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGV-SQAILVS 155
Cdd:cd14875      3 LLHCIKERFeKLHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLLPPHIWQVAHKAFNAIFVQGLgNQSVVIS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  156 GESGAGKTESTKMLMQYLAFMGgKVQSGG---RSVQQQVLE----SNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQ-SG 227
Cdd:cd14875     83 GESGSGKTENAKMLIAYLGQLS-YMHSSNtsqRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPtSG 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  228 KISGAAIRTYLLERSRVCQISDPERNYHCFY-MLCSAPAEEREryKLGD---PASFHYLNQSNCI---KLDG--MDDSSE 298
Cdd:cd14875    162 VMVGGQTVTYLLEKSRIIMQSPGERNYHIFYeMLAGLSPEEKK--ELGGlktAQDYKCLNGGNTFvrrGVDGktLDDAHE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  299 YIATRRAMDIVGISSDEQDAIFRVVAAILHLGNVEFvEGSEADSSVPKDDKSkfhLRTASELFMCDEEALEESLckrVIA 378
Cdd:cd14875    240 FQNVRHALSMIGVELETQNSIFRVLASILHLMEVEF-ESDQNDKAQIADETP---FLTACRLLQLDPAKLRECF---LVK 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  379 TRgESIVKNLDARAAALS-RDALARIVYSRLFDWLVNKINTSIG--QDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTN 455
Cdd:cd14875    313 SK-TSLVTILANKTEAEGfRNAFCKAIYVGLFDRLVEFVNASITpqGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYAN 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  456 EKLQQHFNQHVFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFKG-NQH 534
Cdd:cd14875    392 ESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANkSPY 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  535 FSRPKFS-RSDFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFP--PSEESTKSTkftsIGSSFKQQ 611
Cdd:cd14875    472 FVLPKSTiPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSteKGLARRKQT----VAIRFQRQ 547

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  612 LQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVLDESY 691
Cdd:cd14875    548 LTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTASLF 627

                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1002244077  692 D----EVTATEML-----LEKVNLTGYQIGKTKVFLR 719
Cdd:cd14875    628 KqekySEAAKDFLayyqrLYGWAKPNYAVGKTKVFLR 664

MYSc_Myo17

cd14879

class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...

78-718

1.45e-127

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: 411.56 E-value: 1.45e-127

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTG-NILIAVNPFQRLPHLYNNHMME---IYKGAGFGE---LSPHPFAIADRAYRYMMNYGVSQ 150
Cdd:cd14879      6 ITSHLASRFRSDLPYTRLGsSALVAVNPYKYLSSNSDASLGEygsEYYDTTSGSkepLPPHAYDLAARAYLRMRRRSEDQ 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  151 AILVSGESGAGKTESTKMLMQYLAFMGGKVQSGGRsVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKIS 230
Cdd:cd14879     86 AVVFLGETGSGKSESRRLLLRQLLRLSSHSKKGTK-LSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGRLI 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  231 GAAIRTYLLERSRVCQISDPERNYHCFYMLCS-APAEERERYKLGDPASFHYLNQSNCIKLD---GMDDSSEYIATRRAM 306
Cdd:cd14879    165 GAKVLDYRLERSRVASVPTGERNFHVFYYLLAgASPEERQHLGLDDPSDYALLASYGCHPLPlgpGSDDAEGFQELKTAL 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  307 DIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEA--DSSVPkddKSKFHLRTASELFMCDEEALEESLCKRVIATRGESI 384
Cdd:cd14879    245 KTLGFKRKHVAQICQLLAAILHLGNLEFTYDHEGgeESAVV---KNTDVLDIVAAFLGVSPEDLETSLTYKTKLVRKELC 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  385 VKNLDARAAALSRDALARIVYSRLFDWLVNKINTSI-GQDPSSKLLIGVLDIYGFESFKT---NSFEQFCINLTNEKLQQ 460
Cdd:cd14879    322 TVFLDPEGAAAQRDELARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRSStggNSLDQFCVNFANERLHN 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  461 HFNQHVFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETC-MLRNSTHETFAEKLYQQFKGNQHF-SRP 538
Cdd:cd14879    402 YVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGGLLGILDDQTrRMPKKTDEQMLEALRKRFGNHSSFiAVG 481

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  539 KFSRSD----FTIHHYAGHVTYQTDLFLDKNIDyAVNehqvllhasrCSFVSSLfppseestKSTkftsigSSFKQQLQA 614
Cdd:cd14879    482 NFATRSgsasFTVNHYAGEVTYSVEGFLERNGD-VLS----------PDFVNLL--------RGA------TQLNAALSE 536

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  615 LLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVLDESYDEV 694
Cdd:cd14879    537 LLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLRGSAAERIRQC 616

                          650       660
                   ....*....|....*....|....
gi 1002244077  695 TATEMLLEkvnLTGYQIGKTKVFL 718
Cdd:cd14879    617 ARANGWWE---GRDYVLGNTKVFL 637

MYSc_Myo16

cd14878

class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...

78-719

3.25e-111

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: 367.22 E-value: 3.25e-111

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIY---KGAGFGELSPHPFAIADRAYRYMMNYGVSQAILV 154
Cdd:cd14878      3 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  155 SGESGAGKTESTKMLMQYLAFMGGkvqSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGK-ISGAA 233
Cdd:cd14878     82 SGERGSGKTEASKQIMKHLTCRAS---SSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERKKhLTGAR 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  234 IRTYLLERSRVCQISDPERNYHCFYMLCSA-PAEERERYKLGDPASFHYLNQS---NCIKLDGMDDSSEYIATRRAMDIV 309
Cdd:cd14878    159 IYTYMLEKSRLVSQPPGQSNFLIFYLLMDGlSAEEKYGLHLNNLCAHRYLNQTmreDVSTAERSLNREKLAVLKQALNVV 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  310 GISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDDKSkfhLRTASELFMCDEEALEESLCKRVIATRGESIVKNLD 389
Cdd:cd14878    239 GFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQL---LEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  390 ARAAALSRDALARIVYSRLFDWLVNKINTSI-GQDPSSK---LLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQH 465
Cdd:cd14878    316 IQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqSQDEQKSmqtLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  466 VFKMEQEEYTKEEIDWSYIQFVDNQE-ILDLIEKKPGGIIALLDETCMLRNSTHETFAEKLYQQFK-------------G 531
Cdd:cd14878    396 LFLQEQTECVQEGVTMETAYSPGNQTgVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLEssntnavyspmkdG 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  532 NQHFSrPKFSRSDFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFppseestkSTKFTSIGSSFKQQ 611
Cdd:cd14878    476 NGNVA-LKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLF--------QSKLVTIASQLRKS 546

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  612 LQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLpEVLDESY 691
Cdd:cd14878    547 LADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA-DTLLGEK 625

                          650       660       670
                   ....*....|....*....|....*....|.
gi 1002244077  692 DEVTATE---MLLEKVNLTGYQIGKTKVFLR 719
Cdd:cd14878    626 KKQSAEErcrLVLQQCKLQGWQMGVRKVFLK 656

MYSc_Myo26

cd14887

class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...

76-719

9.81e-111

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: 367.82 E-value: 9.81e-111

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYG--------MNEIYTYTGNILIAVNPFqRLPHLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYG 147
Cdd:cd14887      1 PNLLENLYQRYNkayinkenRNCIYTYTGTLLIAVNPY-RFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  148 VSQAILVSGESGAGKTESTKMLMQYLAFMGGKvQSGGRS--VQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQ 225
Cdd:cd14887     80 RSQSILISGESGAGKTETSKHVLTYLAAVSDR-RHGADSqgLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTG 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  226 SGKISGAAIRTYLLERSRVCQISDPERNYHCFYMLCSAPAEERERYKL---GDPASFhylnqsncikldgmddSSEYIAt 302
Cdd:cd14887    159 RGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSageGDPEST----------------DLRRIT- 221

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  303 rRAMDIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEAD-------------------------------SSVPKDDKSK 351
Cdd:cd14887    222 -AAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPEtskkrkltsvsvgceetaadrshssevkclsSGLKVTEASR 300

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  352 FHLRTASELF-----MCDEEALEESLC-KRVIATRgesivKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQD-- 423
Cdd:cd14887    301 KHLKTVARLLglppgVEGEEMLRLALVsRSVRETR-----SFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSak 375

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  424 ----------PSSKLL--IGVLDIYGFESFKT---NSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIQFVD 488
Cdd:cd14887    376 psesdsdedtPSTTGTqtIGILDLFGFEDLRNhskNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAF 455

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  489 NQE--ILDLIEKKPGGIIALLDETCMLRNSTHET------------------------------FAEKLYQQFKGNQHFS 536
Cdd:cd14887    456 PFSfpLASTLTSSPSSTSPFSPTPSFRSSSAFATspslpsslsslssslsssppvwegrdnsdlFYEKLNKNIINSAKYK 535

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  537 R--PKFSRS--DFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHAsrCSFVSSLFPPSEESTK---STKFTSIGSSFK 609
Cdd:cd14887    536 NitPALSREnlEFTVSHFACDVTYDARDFCRANREATSDELERLFLA--CSTYTRLVGSKKNSGVraiSSRRSTLSAQFA 613

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  610 QQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVLDE 689
Cdd:cd14887    614 SQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALRE 693

                          730       740       750
                   ....*....|....*....|....*....|..
gi 1002244077  690 SYDEVTATEMLLE--KVNLTGYQIGKTKVFLR 719
Cdd:cd14887    694 ALTPKMFCKIVLMflEINSNSYTFGKTKIFFR 725

MYSc_Myo37

cd14898

class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...

78-688

2.12e-106

class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276863 Cd Length: 578 Bit Score: 351.12 E-value: 2.12e-106

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQrlpHLYNNHMMEIYKgAGFGELSPHPFAIADRAYRYMMNYGvSQAILVSGE 157
Cdd:cd14898      3 TLEILEKRYASGKIYTKSGLVFLALNPYE---TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVHG-NQTIVISGE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  158 SGAGKTESTKMLMQYLAFMggkvQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDqsGKISGAAIRTY 237
Cdd:cd14898     78 SGSGKTENAKLVIKYLVER----TASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETY 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  238 LLERSRVCQISDPERNYHCFYMLCSApaeerERYKLGDP---ASFHYLNQSNCIKLdgmddSSEYIATRRAMDIVGISSD 314
Cdd:cd14898    152 LLEKSRVTHHEKGERNFHIFYQFCAS-----KRLNIKNDfidTSSTAGNKESIVQL-----SEKYKMTCSAMKSLGIANF 221

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  315 EqdAIFRVVAAILHLGNVEFVegseaDSSVPKDDKSKFhLRTASELFMCDEEALEESLCKRVIATRGESIVKNLDARAAA 394
Cdd:cd14898    222 K--SIEDCLLGILYLGSIQFV-----NDGILKLQRNES-FTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQAR 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  395 LSRDALARIVYSRLFDWLVNKINTSIGQdpSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEY 474
Cdd:cd14898    294 TIRNSMARLLYSNVFNYITASINNCLEG--SGERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMY 371

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  475 TKEEIDWSYIQFVDNQEILDLIEKkPGGIIALLDETCMLRNSTHETFAEKLYqqfKGNQHFSRPKFsRSDFTIHHYAGHV 554
Cdd:cd14898    372 KEEGIEWPDVEFFDNNQCIRDFEK-PCGLMDLISEESFNAWGNVKNLLVKIK---KYLNGFINTKA-RDKIKVSHYAGDV 446

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  555 TYQTDLFLDKNIDYAvnehQVLLhasrcsfVSSLFPPSEESTKStkftsIGSSFKQQLQALLETLSSVEPHYIRCIKPNN 634
Cdd:cd14898    447 EYDLRDFLDKNREKG----QLLI-------FKNLLINDEGSKED-----LVKYFKDSMNKLLNSINETQAKYIKCIRPNE 510

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1002244077  635 VLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVLD 688
Cdd:cd14898    511 ECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITLFE 564

MYSc_Myo23

cd14884

class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...

76-679

3.79e-95

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: 323.01 E-value: 3.79e-95

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPHLYNNHMMEIY-------KGAGFGELSPHPFAIADRAYRYMMNYGV 148
Cdd:cd14884      1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKELYDQDVMNVYlhkksnsAASAAPFPKAHIYDIANMAYKNMRGKLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  149 SQAILVSGESGAGKTESTKMLMQYLAFMGGKVQSGGRsvQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQ--- 225
Cdd:cd14884     81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTER--IDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEven 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  226 ------SGKISGAAIRTYLLERSRVCQISDPERNYHCFYML---CSAPAEERER-------YKLGDPASFHYLNQS--NC 287
Cdd:cd14884    159 tqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVlrgLSDEDLARRNlvrncgvYGLLNPDESHQKRSVkgTL 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  288 ---------IKLDGMDDSSEYIATRRAMDIVGISSDEQDAIFRVVAAILHLGNvefvegseadssvpkddkskFHLRTAS 358
Cdd:cd14884    239 rlgsdsldpSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGN--------------------RAYKAAA 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  359 ELFMCDEEALEESLCKRVIATRGESIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPSSK----------- 427
Cdd:cd14884    299 ECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDesdnediysin 378

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  428 -LLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKkpggIIAL 506
Cdd:cd14884    379 eAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAK----IFRR 454

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  507 LDETCMLRNSTHETFAEKLYQQF--------------------KGNQHFSRP-KFSRSDFTIHHYAGHVTYQTDLFLDKN 565
Cdd:cd14884    455 LDDITKLKNQGQKKTDDHFFRYLlnnerqqqlegkvsygfvlnHDADGTAKKqNIKKNIFFIRHYAGLVTYRINNWIDKN 534

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  566 IDYAVNEHQVLLHASRCSFVSSlfppSEESTKSTKFTSIGSSFKQQLQALLETLSSVEPHYIRCIKPNNVLKPAIFENSN 645
Cdd:cd14884    535 SDKIETSIETLISCSSNRFLRE----ANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLL 610

                          650       660       670
                   ....*....|....*....|....*....|....
gi 1002244077  646 VLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRF 679
Cdd:cd14884    611 VYRQLKQCGSNEMIKILNRGLSHKIPKKETAAAL 644

MYSc_Myo20

cd14881

class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...

78-718

2.57e-94

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: 318.98 E-value: 2.57e-94

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLP---HLYNNHMMEiykgagfgeLSPHPFAIADRAYRYMMNYGVSQAILV 154
Cdd:cd14881      3 VMKCLQARFYAKEFFTNVGPILLSVNPYRDVGnplTLTSTRSSP---------LAPQLLKVVQEAVRQQSETGYPQAIIL 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  155 SGESGAGKT-ESTKMLMQYLAFMGGKVQSggrSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQsGKISGAA 233
Cdd:cd14881     74 SGTSGSGKTyASMLLLRQLFDVAGGGPET---DAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-GALYRTK 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  234 IRTYLLERSRVCQISDPERNYHCFY-MLCSAPAEERERYKLG--DPASFHYLNQSNcIKLDGMDDSSEYIATRRAMDIVG 310
Cdd:cd14881    150 IHCYFLDQTRVIRPLPGEKNYHIFYqMLAGLSQEERVKLHLDgySPANLRYLSHGD-TRQNEAEDAARFQAWKACLGILG 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  311 IS-SDeqdaIFRVVAAILHLGNVEFVEGSEADSSVpkddKSKFHLRTASELFMCDEEALEESLCKRVIATRGEsIVKNL- 388
Cdd:cd14881    229 IPfLD----VVRVLAAVLLLGNVQFIDGGGLEVDV----KGETELKSVAALLGVSGAALFRGLTTRTHNARGQ-LVKSVc 299

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  389 DARAAALSRDALARIVYSRLFDWLVNKINT-----SIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFN 463
Cdd:cd14881    300 DANMSNMTRDALAKALYCRTVATIVRRANSlkrlgSTLGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYN 379

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  464 QHVFKMEQEEYTKEEIDWSY-IQFVDNQEILDLIEKKPGGIIALLDETCMLRnSTHETFAEKLYQQFKGNQHFSRPK-FS 541
Cdd:cd14881    380 THIFKSSIESCRDEGIQCEVeVDYVDNVPCIDLISSLRTGLLSMLDVECSPR-GTAESYVAKIKVQHRQNPRLFEAKpQD 458

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  542 RSDFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFvsslfppseestkstKFTSIGSSFKQQLQALLETLSS 621
Cdd:cd14881    459 DRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF---------------GFATHTQDFHTRLDNLLRTLVH 523

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  622 VEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLP----EVLDESYDEVTAT 697
Cdd:cd14881    524 ARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPfrllRRVEEKALEDCAL 603

                          650       660
                   ....*....|....*....|....*....
gi 1002244077  698 ----EMLLEKVNL----TGYQIGKTKVFL 718
Cdd:cd14881    604 ilqfLEAQPPSKLssvsTSWALGKRHIFL 632

MYSc_Myo18

cd01386

class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...

77-719

7.86e-94

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: 319.26 E-value: 7.86e-94

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   77 GVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVSG 156
Cdd:cd01386      2 SVLHTLRQRYGANLIHTYAGPSLIVINPRHPLA-VYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  157 ESGAGKTESTKMLMQYLAFMGGkvQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGAAIRT 236
Cdd:cd01386     81 RSGSGKTTNCRHILEYLVTAAG--SVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  237 YLLERSRVCQISDPERNYHCFY-MLCSAPAEERERYKLGDPASFHYLNQSNCIKL-DGMDDSSEYIATRRAMDIVGISSD 314
Cdd:cd01386    159 LLLERSRVARRPEGESNFNVFYyLLAGADAALRTELHLNQLAESNSFGIVPLQKPeDKQKAAAAFSKLQAAMKTLGISEE 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  315 EQDAIFRVVAAILHLGnvefVEGSEADSSVPKDDKSKF-HLRTASELFMCDEEAL---------------------EESL 372
Cdd:cd01386    239 EQRAIWSILAAIYHLG----AAGATKAASAGRKQFARPeWAQRAAYLLGCTLEELssaifkhhlsggpqqsttssgQESP 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  373 CKRVIATRGESIVKNLDARAAALsrdalarivYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFE------SFKTNSF 446
Cdd:cd01386    315 ARSSSGGPKLTGVEALEGFAAGL---------YSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQnpahsgSQRGATF 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  447 EQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIQFVDN-QEILDLIEKKP--------------GGIIALLDETC 511
Cdd:cd01386    386 EDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSpGALVALIDQAPqqalvrsdlrdedrRGLLWLLDEEA 465

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  512 MLRNSTHETFAEKLYQQF-----KGNQHFSRPKFSRSDFTIHHYAGH--VTYQTDLFLDKNIDYAV--NEHQVLLHASRc 582
Cdd:cd01386    466 LYPGSSDDTFLERLFSHYgdkegGKGHSLLRRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKENPSaqNATQLLQESQK- 544

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  583 sfvsslfppseeSTKSTKFTSIGSSFKQQLQALLETLSSVEPHYIRCIKPN-----NVLKPAIFENSNVL-------QQL 650
Cdd:cd01386    545 ------------ETAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkDERSTSSPAAGDELldvpllrSQL 612

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002244077  651 RCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVL------DESYDEVTATEMLLEKVNL--TGYQIGKTKVFLR 719
Cdd:cd01386    613 RGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTkklglnSEVADERKAVEELLEELDLekSSYRIGLSQVFFR 689

MYSc_Myo24A

cd14937

class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...

78-719

1.75e-93

class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276897 Cd Length: 637 Bit Score: 316.57 E-value: 1.75e-93

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQrlphLYNNHMMEiYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVSGE 157
Cdd:cd14937      3 VLNMLALRYKKNYIYTIAEPMLISINPYQ----VIDVDINE-YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  158 SGAGKTESTKMLMQYlaFMGGKVQSGgrSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGAAIRTY 237
Cdd:cd14937     78 SGSGKTEASKLVIKY--YLSGVKEDN--EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIF 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  238 LLERSRVCQISDPERNYHCFYMLCSAPAEE-RERYKLGDPASFHYLNQSNcIKLDGMDDSSEYIATRRAMDIVGIsSDEQ 316
Cdd:cd14937    154 LLENIRVVSQEEEERGYHIFYQIFNGMSQElKNKYKIRSENEYKYIVNKN-VVIPEIDDAKDFGNLMISFDKMNM-HDMK 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  317 DAIFRVVAAILHLGNVEFVE---GSEADSSvPKDDKSKFHLRTASELFMCDEEALEESLC--KRVIATRGESIVKNLDAR 391
Cdd:cd14937    232 DDLFLTLSGLLLLGNVEYQEiekGGKTNCS-ELDKNNLELVNEISNLLGINYENLKDCLVftEKTIANQKIEIPLSVEES 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  392 AA---ALSRDalariVYSRLFDWLVNKINTSIGQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFK 468
Cdd:cd14937    311 VSickSISKD-----LYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYE 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  469 MEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPgGIIALLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPKFS-RSDFTI 547
Cdd:cd14937    386 KETELYKAEDILIESVKYTTNESIIDLLRGKT-SIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDiNKNFVI 464

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  548 HHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFPPSEESTKSTKFTSIGSSFKQQLQALLETLSSVEPHYI 627
Cdd:cd14937    465 KHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRKNLITFKYLKNLNNIISYLKSTNIYFI 544

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  628 RCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLgYPTRRTFDEFVDRFGVL-LPEVLDESYDEVTATEMLLEK-VN 705
Cdd:cd14937    545 KCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNISFF-FQYKYTFDVFLSYFEYLdYSTSKDSSLTDKEKVSMILQNtVD 623

                          650
                   ....*....|....
gi 1002244077  706 LTGYQIGKTKVFLR 719
Cdd:cd14937    624 PDLYKVGKTMVFLK 637

MYSc_Myo21

cd14882

class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...

78-719

8.25e-89

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: 303.59 E-value: 8.25e-89

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   78 VLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVSGE 157
Cdd:cd14882      3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQ-EYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  158 SGAGKTESTKMLMQYLAFMGgkvqSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGAAIRTY 237
Cdd:cd14882     82 SYSGKTTNARLLIKHLCYLG----DGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMY 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  238 LLERSRVCQISDPERNYHCFYMLCSA-PAEERER-YKLGDPASFHYLNQSNCIKLDGM----DDSS-------EYIATRR 304
Cdd:cd14882    158 QLEKLRVSTTDGNQSNFHIFYYFYDFiEAQNRLKeYNLKAGRNYRYLRIPPEVPPSKLkyrrDDPEgnverykEFEEILK 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  305 AMDIvgiSSDEQDAIFRVVAAILHLGNVEFVEGsEADSSVPKDDKSKfhlRTAsELFMCDEEALEESLCKRVIATRGESI 384
Cdd:cd14882    238 DLDF---NEEQLETVRKVLAAILNLGEIRFRQN-GGYAELENTEIAS---RVA-ELLRLDEKKFMWALTNYCLIKGGSAE 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  385 VKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIGQDPS---SKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQH 461
Cdd:cd14882    310 RRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPRAvfgDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQMQYH 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  462 FNQHVFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDE---TCMLRNSTHETFAEKLYQQFKgnqhfsrp 538
Cdd:cd14882    390 YNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDasrSCQDQNYIMDRIKEKHSQFVK-------- 461

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  539 KFSRSDFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFPPSEestkSTKFTSIGSSFKQQLQALLET 618
Cdd:cd14882    462 KHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQ----VRNMRTLAATFRATSLELLKM 537

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  619 LS----SVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVL---LPEVLDESY 691
Cdd:cd14882    538 LSiganSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLafdFDETVEMTK 617

                          650       660
                   ....*....|....*....|....*...
gi 1002244077  692 DEVtatEMLLEKVNLTGYQIGKTKVFLR 719
Cdd:cd14882    618 DNC---RLLLIRLKMEGWAIGKTKVFLK 642

MYSc_Myo44

cd14905

class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...

82-719

1.79e-88

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: 303.55 E-value: 1.79e-88

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   82 LKSRYGMNEIYTYTGNILIAVNPFQRLPHLYNNHMMEIYKGAGfgELSPHPFAIADRAYRYMMNYGVSQAILVSGESGAG 161
Cdd:cd14905      7 IQARYKKEIIYTYIGPILVSVNPLRYLPFLHSQELVRNYNQRR--GLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  162 KTESTKMLMQYLAFMGgkvQSGGRSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSGKISGAAIRTYLLER 241
Cdd:cd14905     85 KSENTKIIIQYLLTTD---LSRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDE 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  242 SRVCQISDPERNYHCFY-MLCSAPAEERERYKLGDPASFHYLNQSNCIKLDGMDDSSEYIATRRAMDIVGISSDEQDAIF 320
Cdd:cd14905    162 NRVTYQNKGERNFHIFYqFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIF 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  321 RVVAAILHLGNVEFVEgseadssvpKDDKSKFHLRTaselfmcdeeaLEESLCKRVI--ATRGESIV---KNLDARAAAL 395
Cdd:cd14905    242 KTLSFIIILGNVTFFQ---------KNGKTEVKDRT-----------LIESLSHNITfdSTKLENILisdRSMPVNEAVE 301

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  396 SRDALARIVYSRLFDWLVNKINTSIGQDPSSKLLiGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYT 475
Cdd:cd14905    302 NRDSLARSLYSALFHWIIDFLNSKLKPTQYSHTL-GILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQ 380

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  476 KEEIDW-SYIQFVDNQEILDLIEKkpggIIALLDETCMLRNSTHETFAEKLyQQFKGNQHFSRPKFSRsdFTIHHYAGHV 554
Cdd:cd14905    381 TERIPWmTPISFKDNEESVEMMEK----IINLLDQESKNINSSDQIFLEKL-QNFLSRHHLFGKKPNK--FGIEHYFGQF 453

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  555 TYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSS----------------LFPPSEESTKS-----TKFTSIGSSFKQQLQ 613
Cdd:cd14905    454 YYDVRGFIIKNRDEILQRTNVLHKNSITKYLFSrdgvfninatvaelnqMFDAKNTAKKSplsivKVLLSCGSNNPNNVN 533

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  614 -----------------------ALLETLSSVEP---------HYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRI 661
Cdd:cd14905    534 npnnnsgggggggnsgggsgsggSTYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRI 613

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  662 SCLGYPTRRTFDEFVDRFGVLLPEV--LDESYDEVTATEMLLEKVNLTGYQIGKTKVFLR 719
Cdd:cd14905    614 QRFGYTIHYNNKIFFDRFSFFFQNQrnFQNLFEKLKENDINIDSILPPPIQVGNTKIFLR 673

MYSc_Myo12

cd14874

class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...

77-719

1.27e-79

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: 276.37 E-value: 1.27e-79

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   77 GVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLPhLYNNHMMEIYKGAGFGElsphpfAIADRAYRYMMNygvSQAILVSG 156
Cdd:cd14874      2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLS-IQDQLVIKKCHISGVAE------NALDRIKSMSSN---AESIVFGG 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  157 ESGAGKTEStkmLMQYLAFMGGKVQSGGRSVQQQVLESnpVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSgKISGAAIR- 235
Cdd:cd14874     72 ESGSGKSYN---AFQVFKYLTSQPKSKVTTKHSSAIES--VFKSFGCAKTLKNDEATRFGCSIDLLYKRN-VLTGLNLKy 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  236 TYLLERSRVCQISDPERNYHCFYMLCSAPAEE-RERYKLGDPASFHYLNQSNCIKlDGMDDSSEYIATRRAMDIVGISSD 314
Cdd:cd14874    146 TVPLEVPRVISQKPGERNFNVFYEVYHGLNDEmKAKFGIKGLQKFFYINQGNSTE-NIQSDVNHFKHLEDALHVLGFSDD 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  315 EQDAIFRVVAAILHLGNVEF----VEGSEADSSVPKDDKskfHLRTASELFMCDEEALEESL-CKRVIATrgesivkNLD 389
Cdd:cd14874    225 HCISIYKIISTILHIGNIYFrtkrNPNVEQDVVEIGNMS---EVKWVAFLLEVDFDQLVNFLlPKSEDGT-------TID 294

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  390 ARAAALSRDALARIVYSRLFDWLVNKINTSIgQDPSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKM 469
Cdd:cd14874    295 LNAALDNRDSFAMLIYEELFKWVLNRIGLHL-KCPLHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHD 373

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  470 EQEEYTKEEI--DWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLRNSTHETFAEK--LYQQFKGNQHFSRPKfSRSDF 545
Cdd:cd14874    374 QLVDYAKDGIsvDYKVPNSIENGKTVELLFKKPYGLLPLLTDECKFPKGSHESYLEHcnLNHTDRSSYGKARNK-ERLEF 452

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  546 TIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFpPSEESTKSTKFTSIGSSFKQQLQALLETLSSVEPH 625
Cdd:cd14874    453 GVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLF-ESYSSNTSDMIVSQAQFILRGAQEIADKINGSHAH 531

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  626 YIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFGVLLPEVLDESYDEVTATEMLLEKVN 705
Cdd:cd14874    532 FVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPGDIAMCQNEKEIIQDILQGQG 611

                          650
                   ....*....|....*..
gi 1002244077  706 L---TGYQIGKTKVFLR 719
Cdd:cd14874    612 VkyeNDFKIGTEYVFLR 628

MYSc_Myo32

cd14893

class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...

79-718

1.25e-73

class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.

Pssm-ID: 276858 Cd Length: 741 Bit Score: 261.83 E-value: 1.25e-73

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   79 LHNLKSRYGMNEIYTYTGNILIAVNPFQRLPHLYNNHMMEI---------YKGAGFGELSPHPFAIADRAYRYMMNYGVS 149
Cdd:cd14893      4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYnksreqtplYEKDTVNDAPPHVFALAQNALRCMQDAGED 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  150 QAILVSGESGAGKTESTKMLMQYLAFMGGKVQ--------SGG-RSVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVE 220
Cdd:cd14893     84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEprpdsegaSGVlHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  221 IQFDQSGKISGAAIRTYLLERSRVCQISDPERNYHCFYMLCSAPAEE---RERYKLGDPAS-FHYLNQSNCIKLDGMDDS 296
Cdd:cd14893    164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDptlRDSLEMNKCVNeFVMLKQADPLATNFALDA 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  297 SEYIATRRAMDIVGISSDEQDAIFRVVAAILHLGNVEFV---EGSEADSSVPKDD---------KSKFHLRTASELFMCD 364
Cdd:cd14893    244 RDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVpdpEGGKSVGGANSTTvsdaqscalKDPAQILLAAKLLEVE 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  365 EEALEESLCKRVIATRGE----SIVKNLDARAAALSRDALARIVYSRLFDWLVNKINTSIG----QDPSSKLLIG----- 431
Cdd:cd14893    324 PVVLDNYFRTRQFFSKDGnktvSSLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGgifdRYEKSNIVINsqgvh 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  432 VLDIYGFESFKT--NSFEQFCINLTNEKLQQHFNQHVFKM-------EQEEYTKEEIDWSYIQFVDNQE-ILDLIEKKPG 501
Cdd:cd14893    404 VLDMVGFENLTPsqNSFDQLCFNYWSEKVHHFYVQNTLAInfsfledESQQVENRLTVNSNVDITSEQEkCLQLFEDKPF 483

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  502 GIIALLDETCMLRNSTHETFAEKLY---QQFKG-----------NQHFSRPKFSRSDFTIHHYAGHVTYQTDLFLDKNID 567
Cdd:cd14893    484 GIFDLLTENCKVRLPNDEDFVNKLFsgnEAVGGlsrpnmgadttNEYLAPSKDWRLLFIVQHHCGKVTYNGKGLSSKNML 563

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  568 YAVNEHQVLLHASRCSFVSSLFPP--------------SEESTKSTKFTSIGSSFKQ--------------QLQALLETL 619
Cdd:cd14893    564 SISSTCAAIMQSSKNAVLHAVGAAqmaaassekaakqtEERGSTSSKFRKSASSAREsknitdsaatdvynQADALLHAL 643

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  620 SSVEPHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRF-------GVLlpEVLDESYD 692
Cdd:cd14893    644 NHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYknvcghrGTL--ESLLRSLS 721

                          730       740
                   ....*....|....*....|....*.
gi 1002244077  693 EVTatemLLEKVNltgYQIGKTKVFL 718
Cdd:cd14893    722 AIG----VLEEEK---FVVGKTKVYL 740

MYSc_Myo24B

cd14938

class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...

76-718

5.98e-51

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: 193.51 E-value: 5.98e-51

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   76 PGVLHNLKSRYGMNEIYTYTGNILIAVNPFQRLpHLYNNHMMEIYKGA-GFGELSPHPFAIADRAYRYMMNYGVSQAILV 154
Cdd:cd14938      1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINN-NINNEETIEKYKCIdCIEDLSLNEYHVVHNALKNLNELKRNQSIII 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  155 SGESGAGKTESTKMLMQYLAF--MGGKVQSGGRSVQQQVLES------------------NPVLEAFGNAKTVRNNNSSR 214
Cdd:cd14938     80 SGESGSGKSEIAKNIINFIAYqvKGSRRLPTNLNDQEEDNIHneentdyqfnmsemlkhvNVVMEAFGNAKTVKNNNSSR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  215 FGKFVEIQFDQSgKISGAAIRTYLLERSRVCQISDPERNYHCFYMLCSAPAEE-RERYKLGDPASFHYLNQSNCIKLDGm 293
Cdd:cd14938    160 FSKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKfKKMYFLKNIENYSMLNNEKGFEKFS- 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  294 DDSSEYIATRRAMDIVGISSDEQDAIFRVVAAILHLGNVEFVEGSEADSSVPKDD------KSKFHLR--TASELFMCDE 365
Cdd:cd14938    238 DYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKAFRKKSLLMGKNqcgqniNYETILSelENSEDIGLDE 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  366 EALEESLCKRVIATRGESIVK----NLDARAAALSR-----------DALARIVYSRLFDWLVNKINTSIGQDPSSKL-- 428
Cdd:cd14938    318 NVKNLLLACKLLSFDIETFVKyfttNYIFNDSILIKvhnetkiqkklENFIKTCYEELFNWIIYKINEKCTQLQNINInt 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  429 -LIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSY-IQFVDNQEILD-LIEKKPGGIIA 505
Cdd:cd14938    398 nYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNlLVGPTEGSLFS 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  506 LLDETCMLRNSTHETFAEKLYQQFKGNQHFSRPK---FSRSDFTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASR- 581
Cdd:cd14938    478 LLENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDditGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEn 557

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  582 ------CSFVSslFPPSEESTKSTKFTSIGSSFK---------QQL------QALLETLSSVEP---HYIRCIKPN-NVL 636
Cdd:cd14938    558 eymrqfCMFYN--YDNSGNIVEEKRRYSIQSALKlfkrrydtkNQMavsllrNNLTELEKLQETtfcHFIVCMKPNeSKR 635

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  637 KPAIFENSNVLQQLRCGGVLEAIRISCLGYPTRRTFDEFVDRFgvllpEVLDESYDEVTATEMLLEKVNLTGYQIGKTKV 716
Cdd:cd14938    636 ELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIF-----DIKNEDLKEKVEALIKSYQISNYEWMIGNNMI 710


                   ..
gi 1002244077  717 FL 718
Cdd:cd14938    711 FL 712

Myo5-like_CBD

cd14945

Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied ...

1105-1455

7.03e-51

Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5 a,b,c) in vertebrates and two (myo2 and myo4) in fungi and related to plant class XI myosins. Their C-terminal cargo binding domains is important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. MyoV-CBDs interact with several adaptor proteins that in turn interact with the cargo.

Pssm-ID: 271253 [Multi-domain] Cd Length: 288 Bit Score: 181.83 E-value: 7.03e-51

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1105 ESVDALINCVTENIGFSEG--KPIAAITIYKCLVHW-KIFETEK-TSVFDRLIQIFGSAMQKH-DSNEDLAYWLSTSSTL 1179
Cdd:cd14945      1 SEEDSLLRGIVTDFEPSSGdhKLTPAYILYLCIRHAaSNGLTGQsTSLLNKVLKTIQQVVQQHnDDMQLLAFWLSNASEL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1180 LIMLQKSLKAAGSSGGTPRKKPqtqssflgrmvfrssnitvdmdlvRQIEAKYPAFLFKQQLTAFVEGLYGMIRDNVKKE 1259
Cdd:cd14945     81 LYFLKQDSKLYGAAGEAPQKEE------------------------EQKLTVSDLNELKQDLEAVSIKIYQQALKYLNKN 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1260 LSSllshaiqvprimkasmvrgrsfgtsslprgrsfsnqgsYWQAIVDNLDELLKILQENCVPAIFMRKIFTQIFSFINA 1339
Cdd:cd14945    137 LQP--------------------------------------KIRDIVKFLNSFLDLLKSFHVHPEIRSQVFTQLFSFINA 178

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1340 QLFNSLLVRHECCSFSNGEYVKQGLAQMEVWCGEVKPEyvGSALDELKHIRQAVGFLVIfKKFRISYDEIVNDLCPVLSV 1419
Cdd:cd14945    179 RLFNQLITKKDALSWSRGMQIRANISRLEEWCEGRGLE--HLAVDFLSKLIQAVQLLQL-KKYTQEDIEILCELCPSLNP 255

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1002244077 1420 QQLYKICTQYWDDKYNTESVSEEVldeMRTLITKES 1455
Cdd:cd14945    256 AQLQAILTQYQPANYGESPVPKEI---LRTLAAEVS 288

Motor_domain

cd01363

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...

98-227

8.26e-36

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: 134.01 E-value: 8.26e-36

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   98 ILIAVNPFQRLPHLYNNHMMEIYKGAGFGELSPHPFAIADRAYRYMMNYGVSQAILVSGESGAGKTESTKMLMQYLAFMG 177
Cdd:cd01363      1 VLVRVNPFKELPIYRDSKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002244077  178 GKVQSGGR------------SVQQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDQSG 227
Cdd:cd01363     81 FNGINKGEtegwvylteitvTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAG 142

MYSc_Myo33

cd14894

class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...

82-689

1.77e-34

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: 143.73 E-value: 1.77e-34

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   82 LKSRYGMNEIYTYTGNILIAV-NPFQ-----RLPHLYNNHMMEIYKGAGFGE--LSPHPFAIADRAYRYM---------- 143
Cdd:cd14894      7 LTSRFDDDRIYTYINHHTMAVmNPYRllqtaRFTSIYDEQVVLTYADTANAEtvLAPHPFAIAKQSLVRLffdnehtmpl 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  144 ---------MNYGVSQAILVSGESGAGKTESTKMLMQYLAFMGGKVQSGGR------------------------SVQQQ 190
Cdd:cd14894     87 pstissnrsMTEGRGQSLFLCGESGSGKTELAKDLLKYLVLVAQPALSKGSeetckvsgstrqpkiklftsstksTIQMR 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077      --------------------------------------------------------------------------------
Cdd:cd14894    167 teeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeklehledeeqlrmyfknphaakkl 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  191 --VLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQF-----DQSGKISGAAIRTYLLERSRVCQI------SDPERNYHCF 257
Cdd:cd14894    247 siVLDSNIVLEAFGHATTSMNLNSSRFGKMTTLQVafglhPWEFQICGCHISPFLLEKSRVTSErgresgDQNELNFHIL 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  258 YMLCSAPAE-------ERERYKLG-DPASFHYLNQSNCiKLDGM--------DDSSEYIATRRAMDIVGISSDEQDAIFR 321
Cdd:cd14894    327 YAMVAGVNAfpfmrllAKELHLDGiDCSALTYLGRSDH-KLAGFvskedtwkKDVERWQQVIDGLDELNVSPDEQKTIFK 405

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  322 VVAAILHLGNVEF----VEGSEADSSVPKDDKSKfhlRTASELFMCDEEALEESLCKRVIA--TRGESIVKNLDARAAAL 395
Cdd:cd14894    406 VLSAVLWLGNIELdyreVSGKLVMSSTGALNAPQ---KVVELLELGSVEKLERMLMTKSVSlqSTSETFEVTLEKGQVNH 482

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  396 SRDALARIVYSRLFDWLVNKIN-----TSIGQD------------PSSKLLIGVLDIYGFESFKTNSFEQFCINLTNEKL 458
Cdd:cd14894    483 VRDTLARLLYQLAFNYVVFVMNeatkmSALSTDgnkhqmdsnasaPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL 562

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  459 qqhfnqhvFKMEQEEYTKEEIDWSYIQFVDNQEILDLIEKKPGGIIALLDETCMLrnstHETFAEKLYQQFKGNQHFSRP 538
Cdd:cd14894    563 --------YAREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTIL----HQSENMNAQQEEKRNKLFVRN 630

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  539 KFSRSD-------------------------FTIHHYAGHVTYQTDLFLDKNIDYAVNEHQVLLHASRCSFVSSLFPPSE 593
Cdd:cd14894    631 IYDRNSsrlpepprvlsnakrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESS 710

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  594 ES--TKSTKFTSIGS---------SFKQQLQALLETLSSVE----PHYIRCIKPNNVLKPAIFENSNVLQQLRCGGVLEA 658
Cdd:cd14894    711 QLgwSPNTNRSMLGSaesrlsgtkSFVGQFRSHVNVLTSQDdknmPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQ 790

                          810       820       830
                   ....*....|....*....|....*....|....*..
gi 1002244077  659 IRISCLGYPTRRTFD----EFVDRFGVLL--PEVLDE 689
Cdd:cd14894    791 MEICRNSSSSYSAIDisksTLLTRYGSLLrePYILDD 827

DIL

pfam01843

DIL domain; The DIL domain has no known function.

1328-1432

4.62e-32

DIL domain; The DIL domain has no known function.

Pssm-ID: 460359 [Multi-domain] Cd Length: 103 Bit Score: 120.77 E-value: 4.62e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1328 KIFTQIFSFINAQLFNSLLVRHECCSFSNGEYVKQGLAQMEVWCGEVKPEYvgSALDELKHIRQAVGFLVIFKKFRISYD 1407
Cdd:pfam01843    1 QLFSQLFYFINAELFNRLLLRKKYCSWSKGMQIRYNLSRLEEWARSNGLES--EARDHLAPLIQAAQLLQLRKSTLEDLD 78

                           90       100
                   ....*....|....*....|....*
gi 1002244077 1408 EIVnDLCPVLSVQQLYKICTQYWDD 1432
Cdd:pfam01843   79 SIL-QVCPALNPLQLHRLLTLYQPD 102

Myo5_CBD

cd15470

Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, ...

1302-1429

3.97e-12

Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. The MyoV-CBDs directly interact with several adaptor proteins, in case of Myo5a, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin, and in case of Myo5b, Rab11-family interacting protein 2.

Pssm-ID: 271254 [Multi-domain] Cd Length: 332 Bit Score: 69.16 E-value: 3.97e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1302 WQAIVDNLDELLKILQENCVPAIFMRKIFTQIFSFINAQLFNSLLVRHECCSFSNGEYVKQGLAQMEVWCGEVK--PEYV 1379
Cdd:cd15470    143 LDSLLQQLNSFHTTLTQHGLDPELIKQVFRQLFYLICASTLNNLLLRKDLCSWSKGMQIRYNVSQLEEWLRDKGlqDSGA 222

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1380 GSALDELKhirQAVGFLVIFKKFRISYDEIVnDLCPVLSVQQLYKICTQY 1429
Cdd:cd15470    223 RETLEPLI---QAAQLLQVKKTTEEDAQSIC-EMCTKLTTAQIVKILNLY 268

Myo5b_CBD

cd15477

Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, ...

1163-1429

1.81e-10

Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. They interact with several adaptor proteins, in case of Myo5b-CBD, Rab11-family interacting protein 2.

Pssm-ID: 271261 Cd Length: 372 Bit Score: 64.50 E-value: 1.81e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1163 HDSNEDLAYWLSTSSTLLIML-QKSLKAAGSSGGTPRKKPQTQSSFlgrmvfrssnitvDMDLVRQIEAKYPAFLFkQQL 1241
Cdd:cd15477     67 NDDFEMTSFWLANTCRLLHCLkQYSGDEGFMTQNTAKQNEHCLKNF-------------DLTEYRQVLSDLSIQIY-QQL 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1242 TAFVEG-LYGMIrdnvkkeLSSLL-SHAIQVPRIMKAsmvRGRSFGTSSLPRGrsfsnQGSY-WQAIVDNLDELLKILQE 1318
Cdd:cd15477    133 IKIAEGiLQPMI-------VSAMLeNESIQGLSGVKP---MGYRKRSSSMADG-----DNSYtLEALIRQLNTFHSIMCD 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1319 NCVPAIFMRKIFTQIFSFINAQLFNSLLVRHECCSFSNGEYVKQGLAQMEVWCgEVKPEYVGSALDELKHIRQAVGFLVI 1398
Cdd:cd15477    198 QGLDPEIIQQVFKQLFYMINAVTLNNLLLRKDVCSWSTGMQLRYNISQLEEWL-RGRNLHQSGAAQTMEPLIQAAQLLQL 276

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1002244077 1399 FKKfrISYD-EIVNDLCPVLSVQQLYKICTQY 1429
Cdd:cd15477    277 KKK--TSEDaEAICSLCTALSTQQIVKILNLY 306

Myo5p-like_CBD_fungal

cd15474

cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin ...

1138-1454

4.60e-09

cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin cables, actin filaments that are bundled by fimbrin, in the presence of tropomyosin. This is in contrast to the other vertebrate class V myosins. Like other class V myosins, fungal myosin 2 and 4 contain a C-terminal cargo binding domain. In case of Myo4 it has been shown to bind to the adapter protein She3p (Swi5p-dependent HO expression 3), which in turn anchors myosin 4 to its cargos, zip-coded mRNP (messenger ribonucleoprotein particles) and tER (tubular endoplasmic reticulum). Myo 2 binds to Vac17, vacuole-specific cargo adaptor, and Mmr1, mitochondria-specific cargo adaptor. Both adaptors bind competitivly at the same site.

Pssm-ID: 271258 Cd Length: 352 Bit Score: 60.12 E-value: 4.60e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1138 WKIFETEKTSVFDRLIQIFGSAMQKHDSN------EDLAYWLSTSSTL--LIMLQKSLKAAGSSGGTPRKkpqtqssflg 1209
Cdd:cd15474     46 WKSLLELLTQSERFLSHVLSYIASIVDSLpkketiPDGAFWLANLHELrsFVVYLLSLIEHSSSDEFSKE---------- 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1210 rmvfrssnitvDMDLVRQIEAKYPAFLFKqqltafvegLYGMIRDNVKKELSsllshaiqvPRIMKASMVRGRS--FGTS 1287
Cdd:cd15474    116 -----------SEEYWNTLFDKTLKHLSN---------IYSTWIDKLNKHLS---------PKIEGAVLVLLTSldLSEL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1288 SLPRGRSFSNQGSYWQAIVDNLDELLKILQENCVPAIFMRKIFTQIFSFINAQLFNSLLVRHECCSFSNGEYVKQGLAQM 1367
Cdd:cd15474    167 IDLNKEFFNKPKKKMADLITFLNEVYDLLQSFSVQPELLNAIVSSTLQYINVEAFNSLITKRSALSWKRGSQISYNVSRL 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1368 EVWCgevKPEYVGSALDELKHIRQAVGFLVIFKKFRISYDEIVNdLCPVLSVQQLYKICTQYwdDKYNTES-VSEEVLDE 1446
Cdd:cd15474    247 KEWC---HQHGLSDANLQLEPLIQASKLLQLRKDDENDFKIILS-VCYALNPAQIQKLLDKY--QPANYEApVPKEFLNA 320


                   ....*...
gi 1002244077 1447 MRTLITKE 1454
Cdd:cd15474    321 LEKLIKKE 328

Myosin_N

pfam02736

Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ...

8-52

7.08e-09

Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.

Pssm-ID: 460670 Cd Length: 45 Bit Score: 52.82 E-value: 7.08e-09

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1002244077    8 TVGSNVWVEDADVAWIDGLVEQVTGDELIIRCTSGKKVTANVSSV 52
Cdd:pfam02736    1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

820-1042

1.58e-08

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 1.58e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  820 AARKELQYRQQTKAAVIIQSYCRSYLAHSQYMGLKKA-AITTQCAWRGRLARRELRKLK--------MAAKETGALQAAK 890
Cdd:TIGR02168  702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLeAEVEQLEERIAQLSKELTELEaeieeleeRLEEAEEELAEAE 781

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  891 ---NKLEKQVEELTWRLQLEKRMRVDMEEAKSQENKKLQQKLQELELQSNETKDLLKR----EQETAKAAWEKAALVPEV 963
Cdd:TIGR02168  782 aeiEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRledlEEQIEELSEDIESLAAEI 861

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  964 QVDTTLVNELTAENEKLKTLVASLE--------------TKIDETEQRFDEVKKAREELLKKATDAESKINGLTNTMLSL 1029
Cdd:TIGR02168  862 EELEELIEELESELEALLNERASLEealallrseleelsEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941

                          250
                   ....*....|....*.
gi 1002244077 1030 QEKLTN---MELENQV 1042
Cdd:TIGR02168  942 QERLSEeysLTLEEAE 957

Smc

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...

849-1047

4.95e-08

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 4.95e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  849 QYMGLKKAAITTQCAWRGRLARRELRKLKMAAKETGALQAAKNKLEKQVEELTWRLQLEK----RMRVDMEEAKSQENkK 924
Cdd:COG1196    214 RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRleleELELELEEAQAEEY-E 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  925 LQQKLQELELQSNETKDLLKREQET-AKAAWEKAALVPEVQVDTTLVNELTAENEKLKTLVASLETKIDETEQRFDEVKK 1003
Cdd:COG1196    293 LLAELARLEQDIARLEERRRELEERlEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1002244077 1004 AREELLKKATDAESKINGLTNTMLSLQEKLTNMELENQVLRQQA 1047
Cdd:COG1196    373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416

fMyo2p_CBD

cd15480

cargo binding domain of fungal myosin 2; Yeast myosin V travels along actin cables, actin ...

1326-1468

4.97e-08

cargo binding domain of fungal myosin 2; Yeast myosin V travels along actin cables, actin filaments that are bundled by fimbrin, in the presence of tropomyosin. This is in contrast to the other vertebrate class V myosins. Like other class V myosins, fungal myosin 2 and 4 contain a C-terminal cargo binding domain. Myo 2 binds to Vac17, vacuole-specific cargo adaptor, and Mmr1, mitochondria-specific cargo adaptor. Both adaptors bind competitivly at the same site.

Pssm-ID: 271264 Cd Length: 363 Bit Score: 56.82 E-value: 4.97e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1326 MRKIFTQIFSFINAQLFNSLLVRHECCSFSNGEYVKQGLAQMEVWCgevKPEYVGSALDELKHIRQAVGFLViFKKFRIS 1405
Cdd:cd15480    192 IRQVVTELLKLIGVTAFNDLLMRRNFLSWKRGLQINYNITRLEEWC---KSHDIPEGTLQLEHLMQATKLLQ-LKKATLE 267

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002244077 1406 YDEIVNDLCPVLSVQQLYKICTQYWDDKYntES-VSEEVLDEMRTLITKESGQDSSENTFLLDD 1468
Cdd:cd15480    268 DIEIIYDVCWILTPAQIQKLISQYYVADY--ENpISPEILKAVAARVKPEDKSDHLLLIPLVEE 329

EnvC

COG4942

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

874-1046

5.88e-08

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: 56.70 E-value: 5.88e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  874 RKLKMAAKETGALQAAKNKLEKQVEELTWRLQ-LEKRMRvdmeeAKSQENKKLQQKLQELELQSNETKDLLKRE----QE 948
Cdd:COG4942     41 KELAALKKEEKALLKQLAALERRIAALARRIRaLEQELA-----ALEAELAELEKEIAELRAELEAQKEELAELlralYR 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  949 TAKAAWEKAALVPE---------------VQVDTTLVNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKAT 1013
Cdd:COG4942    116 LGRQPPLALLLSPEdfldavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA 195

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1002244077 1014 DAESKINGLTNTMLSLQEKLTNMELENQVLRQQ 1046
Cdd:COG4942    196 ERQKLLARLEKELAELAAELAELQQEAEELEAL 228

CwlO1

COG3883

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

875-1071

8.00e-08

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 8.00e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  875 KLKMAAKETGALQAAKNKLEKQVEELtwRLQLEKRMRvDMEEAKsQENKKLQQKLQELELQSNETKDLLKREQET----A 950
Cdd:COG3883     17 QIQAKQKELSELQAELEAAQAELDAL--QAELEELNE-EYNELQ-AELEALQAEIDKLQAEIAEAEAEIEERREElgerA 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  951 KAAWEKAALVPEVQV-----------------------DTTLVNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREE 1007
Cdd:COG3883     93 RALYRSGGSVSYLDVllgsesfsdfldrlsalskiadaDADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002244077 1008 LLKKATDAESKINGLTNTMLSLQEKLtnMELENQVLRQQALFRSPVRTIPENTSPKANSTNSSP 1071
Cdd:COG3883    173 LEAQQAEQEALLAQLSAEEAAAEAQL--AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234

Smc

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...

867-1048

1.46e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 1.46e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  867 RLARRELRKLKMAAKETGALQAAKNKLEKQVEELTWRLQLEKRMRVDMEEAKSQENKKLQQKLQELELQSNETKDLLKRE 946
Cdd:COG1196    309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  947 QETAKAAWEKAAlvpEVQVDTTLVNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKATDAESKINGLTNTM 1026
Cdd:COG1196    389 LEALRAAAELAA---QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465

                          170       180
                   ....*....|....*....|..
gi 1002244077 1027 LSLQEKLTNMELENQVLRQQAL 1048
Cdd:COG1196    466 AELLEEAALLEAALAELLEELA 487

Myosin_tail_1

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

798-1046

1.71e-07

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 56.34 E-value: 1.71e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  798 ARKNYRDLC----SASTTVQSGLRGMAARKELQYRQQTKAAVI---IQSYCRSYLAHSQYMGLKKAAittqcawrgrlAR 870
Cdd:pfam01576  290 AEKQRRDLGeeleALKTELEDTLDTTAAQQELRSKREQEVTELkkaLEEETRSHEAQLQEMRQKHTQ-----------AL 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  871 REL-RKLKMAAKETGALQAAKNKLEKQVEELTWRLQLEKRMRVDMEEAKsqenKKLQQKLQELELQSNETkdllkrEQET 949
Cdd:pfam01576  359 EELtEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKR----KKLEGQLQELQARLSES------ERQR 428

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  950 AKAAWEKAALVPEVQVDTTLVNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKATDAESKINGLTNTMLSL 1029
Cdd:pfam01576  429 AELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEE 508

                          250
                   ....*....|....*..
gi 1002244077 1030 QEKLTNMELENQVLRQQ 1046
Cdd:pfam01576  509 EEAKRNVERQLSTLQAQ 525

CCDC158

pfam15921

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

758-1046

2.01e-07

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: 55.89 E-value: 2.01e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  758 RLSA--TQLQAVCRGQIARHYY------EDLRrKAATLTIQTYYRMHFARKNYRDLCSASTTVQSGLRGM----AARKEL 825
Cdd:pfam15921  430 RLEAllKAMKSECQGQMERQMAaiqgknESLE-KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVsdltASLQEK 508

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  826 QYRQQTKAAVIIQSYCRSYLAHSQYMGLKKAA-----ITTQC-AWRGRLARRE-----LRK--------LKMAAKETGAL 886
Cdd:pfam15921  509 ERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlrnVQTECeALKLQMAEKDkvieiLRQqienmtqlVGQHGRTAGAM 588

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  887 QAAKNKLEKQVEELTWRLQlEKRMRVDMEEAKSQEnkkLQQKLQELELqsnETKDLLKREQETAKAA----WEKAALVPE 962
Cdd:pfam15921  589 QVEKAQLEKEINDRRLELQ-EFKILKDKKDAKIRE---LEARVSDLEL---EKVKLVNAGSERLRAVkdikQERDQLLNE 661

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  963 VQVDTTLVNELTAENE------------------KLKTLVASLETKIDETEQRFDEVKKAREELLKKA-------TDAES 1017
Cdd:pfam15921  662 VKTSRNELNSLSEDYEvlkrnfrnkseemetttnKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAmgmqkqiTAKRG 741

                          330       340
                   ....*....|....*....|....*....
gi 1002244077 1018 KINGLTNTMLSLQEKLTNMELENQVLRQQ 1046
Cdd:pfam15921  742 QIDALQSKIQFLEEAMTNANKEKHFLKEE 770

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

869-1019

2.45e-07

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];

Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.39 E-value: 2.45e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  869 ARRELRKLKMAAKEtgaLQAAKNKLEKQVEELTwrlQLEKRMRVDMEEAKSqeNKKLQQKLQELELqsnetkdlLKREQE 948
Cdd:COG1579     43 LEARLEAAKTELED---LEKEIKRLELEIEEVE---ARIKKYEEQLGNVRN--NKEYEALQKEIES--------LKRRIS 106

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002244077  949 TAkaawEKAALVPEVQVDTtLVNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKATDAESKI 1019
Cdd:COG1579    107 DL----EDEILELMERIEE-LEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172

COG1340

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];

870-1047

3.66e-07

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 53.76 E-value: 3.66e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  870 RRELRKLKMAAKETGALQAAKNKLEKQVEELTWRLQLEKrMRVDMEeaksqenKKLQQKLQELELQSNETKDLLKREQET 949
Cdd:COG1340     91 REELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEV-LSPEEE-------KELVEKIKELEKELEKAKKALEKNEKL 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  950 AKAAWEKAALVPEVQVDTTLVNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKATDAESKINGLTNTMLSL 1029
Cdd:COG1340    163 KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELREL 242

                          170
                   ....*....|....*...
gi 1002244077 1030 QEKLTNMELENQVLRQQA 1047
Cdd:COG1340    243 RKELKKLRKKQRALKREK 260

SMC_prok_A

TIGR02169

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

869-1047

5.55e-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: 5.55e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  869 ARRELRKLkmaAKETGALQAAKNKLEKQVEELtwrlqlEKRMRVDMEEAKSQENKKLQQKLQELELQSNETkdllkrEQE 948
Cdd:TIGR02169  756 VKSELKEL---EARIEELEEDLHKLEEALNDL------EARLSHSRIPEIQAELSKLEEEVSRIEARLREI------EQK 820

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  949 TAKAAWEKAALVPEVQVDTTLVNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKATDAESKINGLTNTMLS 1028
Cdd:TIGR02169  821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900

                          170
                   ....*....|....*....
gi 1002244077 1029 LQEKLTNMELENQVLRQQA 1047
Cdd:TIGR02169  901 LERKIEELEAQIEKKRKRL 919

Myo5a_CBD

cd15478

Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, ...

1126-1476

6.43e-07

Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. They interact with several adaptor proteins, in case of Myo5a-CBD, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin. Mutations in human Myo5a (many of which map to the cargo binding domain) lead to Griscelli syndrome, a severe neurological disease.

Pssm-ID: 271262 Cd Length: 375 Bit Score: 53.49 E-value: 6.43e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1126 IAAITIYKCLVHWKIFETEK------TSVFDRLIQIFgsaMQKHDSNEDLAYWLSTSSTLLIML-QKSLKAAGSSGGTPR 1198
Cdd:cd15478     28 LPAYILFMCVRHADYLNDDQkvrsllTSTINSIKKVL---KKRGDDFETVSFWLSNTCRFLHCLkQYSGEEGFMKHNTSR 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1199 KKPQTQSSFlgrmvfrssnitvDMDLVRQIEAKYPAFLFKQQLTAFVEGLYGMIrdnvkkeLSSLLSH-AIQVPRIMKAS 1277
Cdd:cd15478    105 QNEHCLTNF-------------DLAEYRQVLSDLAIQIYQQLVRVLENILQPMI-------VSGMLEHeTIQGVSGVKPT 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1278 MVRGRSfgtsslprgRSFSNQGSY-WQAIVDNLDELLKILQENCVPAIFMRKIFTQIFSFINAQLFNSLLVRHECCSFSN 1356
Cdd:cd15478    165 GLRKRT---------SSIADEGTYtLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSK 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1357 GEYVKQGLAQMEVWCGEvKPEYVGSALDELKHIRQAVGFLVIFKKFRISYDEIVNdLCPVLSVQQLYKICTQYWDDKYNT 1436
Cdd:cd15478    236 GMQIRYNVSQLEEWLRD-KNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICS-MCNALTTAQIVKVLNLYTPVNEFE 313

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1002244077 1437 ESVSEEVLD--EMRTLITKESGQdssentFLLDDEISMPISL 1476
Cdd:cd15478    314 ERVSVSFIRtiQMRLRDRKDSPQ------LLMDAKHIFPVTF 349

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

871-1046

3.10e-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: 51.94 E-value: 3.10e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  871 RELRKLKMAAK-ETGALQAAKNKLEKQVEELTW-RLQLEKRMRVdmEEAKSQENKKLQQKLQELELQSNETKDLLKREQE 948
Cdd:TIGR04523  162 NDLKKQKEELEnELNLLEKEKLNIQKNIDKIKNkLLKLELLLSN--LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  949 takaawEKAALVPEVQVDTTLVNELTAENEKLKTL-------VASLETKIDETEQRFDEVK------------------- 1002
Cdd:TIGR04523  240 ------EINEKTTEISNTQTQLNQLKDEQNKIKKQlsekqkeLEQNNKKIKELEKQLNQLKseisdlnnqkeqdwnkelk 313

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1002244077 1003 -------KAREELLKKATDAESKINGLTNTMLSLQEKLTNMELENQVLRQQ 1046
Cdd:TIGR04523  314 selknqeKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE 364

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

720-1026

5.77e-06

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 5.77e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  720 AGQMAELDARRTEvLSSSASKIQRKVRSYLAHKHFIQLRLSATQLQAVCRGQIARHYYEDLRRKAATLTIQTYYRMhfar 799
Cdd:TIGR02168  690 EEKIAELEKALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE---- 764

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  800 KNYRDLCSASTTVQSGLRGMAARKELQYRQQTKAAVIIQSYCRsylAHSQYMGLKKAAITTQC----------AWRGRLA 869
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE---LRAELTLLNEEAANLRErleslerriaATERRLE 841

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  870 RRELRKLKM------AAKETGALQAAKNKLEKQVEELT-WRLQLEKRMRV--DMEEAKSQENKKLQQKLQELELQSNETK 940
Cdd:TIGR02168  842 DLEEQIEELsediesLAAEIEELEELIEELESELEALLnERASLEEALALlrSELEELSEELRELESKRSELRRELEELR 921

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  941 DLLK-----------REQETAKAAWEKAALVPEVQVdtTLVNELTAENEKLKTLVASLETKIDE-------TEQRFDEVK 1002
Cdd:TIGR02168  922 EKLAqlelrleglevRIDNLQERLSEEYSLTLEEAE--ALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELK 999

                          330       340
                   ....*....|....*....|....
gi 1002244077 1003 KAREELLKKATDAESKINGLTNTM 1026
Cdd:TIGR02168 1000 ERYDFLTAQKEDLTEAKETLEEAI 1023

HMMR_N

pfam15905

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...

886-1045

7.12e-06

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.

Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 49.81 E-value: 7.12e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  886 LQAAKNKLE-KQVEELTWRLQLEKRMRV---DMEEAKSqENKKLQQKLQELELQSNETK-DLLKREQETAK--AAWEKaa 958
Cdd:pfam15905  161 LMKLRNKLEaKMKEVMAKQEGMEGKLQVtqkNLEHSKG-KVAQLEEKLVSTEKEKIEEKsETEKLLEYITElsCVSEQ-- 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  959 lVPEVQVDTTLVNELTAE-NEKLKTLVASLETKIDE----TEQRFDEVKKAREELLKKATDAESKINGLTNTMLSLQEKL 1033
Cdd:pfam15905  238 -VEKYKLDIAQLEELLKEkNDEIESLKQSLEEKEQElskqIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKL 316

                          170
                   ....*....|..
gi 1002244077 1034 TNMELENQVLRQ 1045
Cdd:pfam15905  317 TLEEQEHQKLQQ 328

rad50

TIGR00606

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

870-1019

1.01e-05

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).

Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.43 E-value: 1.01e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  870 RRELRKLKMAAKETGALQAAKNKLEKQVEELTWRLQLEKRMRVDMEEAKSQENKKLQQKLQELELQSNETKDLLKREQET 949
Cdd:TIGR00606  401 ERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQEL 480

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002244077  950 AKAAWEKAALVPEVQVDTTLVNELTAENEKLKtLVASLETKIDETEQ--RFDEVKKAREELLKKATDAESKI 1019
Cdd:TIGR00606  481 RKAERELSKAEKNSLTETLKKEVKSLQNEKAD-LDRKLRKLDQEMEQlnHHTTTRTQMEMLTKDKMDKDEQI 551

Myosin_tail_1

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

867-1037

1.02e-05

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.56 E-value: 1.02e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  867 RLARRELRKLKMAAKETGA----LQAAKNKLEKQVEELtwRLQLEK-------------RMRVDMEEAKSQ--------- 920
Cdd:pfam01576  660 KQLRAEMEDLVSSKDDVGKnvheLERSKRALEQQVEEM--KTQLEEledelqatedaklRLEVNMQALKAQferdlqard 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  921 ---ENKK--LQQKLQELELQSNEtkdllKREQETAKAAWEKAALVP----EVQVDTTlvNEltAENEKLKTLvASLETKI 991
Cdd:pfam01576  738 eqgEEKRrqLVKQVRELEAELED-----ERKQRAQAVAAKKKLELDlkelEAQIDAA--NK--GREEAVKQL-KKLQAQM 807

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1002244077  992 DETEQRFDEVKKAREELLKKATDAESKINGLTNTMLSLQEKLTNME 1037
Cdd:pfam01576  808 KDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASE 853

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

866-1042

1.08e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 1.08e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  866 GRLARRELRKLKMAAKETGALQAAKNKLEKQVEELTWRLQlekRMRVDMEEAKSqENKKLQQKLQELELQ-SNETKDLLK 944
Cdd:COG4372     23 GILIAALSEQLRKALFELDKLQEELEQLREELEQAREELE---QLEEELEQARS-ELEQLEEELEELNEQlQAAQAELAQ 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  945 REQETAKAAWEKAALVPEVQvdttlvnELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKATDAESKINGLTN 1024
Cdd:COG4372     99 AQEELESLQEEAEELQEELE-------ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171

                          170
                   ....*....|....*...
gi 1002244077 1025 TMLSLQEKLTNMELENQV 1042
Cdd:COG4372    172 ELQALSEAEAEQALDELL 189

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

874-1043

2.24e-05

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 2.24e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  874 RKLKMAAKETGALQAAKNKLEKQVEELTWRLQLEKRMRVDMEEAKSQENKKLQQKLQEL-ELQSNETKDLLKRE-----Q 947
Cdd:TIGR04523  489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnKDDFELKKENLEKEideknK 568

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  948 ETAKAAWEKAALVPEVQVDTTLVNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKATDAESKINGLT---- 1023
Cdd:TIGR04523  569 EIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKqevk 648

                          170       180
                   ....*....|....*....|...
gi 1002244077 1024 ---NTMLSLQEKLTNMELENQVL 1043
Cdd:TIGR04523  649 qikETIKEIRNKWPEIIKKIKES 671

PTZ00121

MAEBL; Provisional

872-1018

2.45e-05

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 2.45e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  872 ELRKLKMAAKETGALQAAKNKLE--KQVEELTwrlQLEKRMRVDmEEAKSQENKKLQQ---------KLQELELQSNETK 940
Cdd:PTZ00121  1253 EIRKFEEARMAHFARRQAAIKAEeaRKADELK---KAEEKKKAD-EAKKAEEKKKADEakkkaeeakKADEAKKKAEEAK 1328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  941 ---DLLKREQETAKAAWEKAALVPEVQVDTTLVNELTAENEKLKTlvASLETKIDETEQRFDEVKKArEELLKKATDAES 1017
Cdd:PTZ00121  1329 kkaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK--EEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKK 1405


                   .
gi 1002244077 1018 K 1018
Cdd:PTZ00121  1406 K 1406

YhaN

COG4717

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

867-1050

2.47e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.47e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  867 RLARRELRKLKMAAKETGALQAAKNKLEKQVEELTWRLQLEKRMRVDMEEAKS-----QENKKLQQKLQELELQSNEtkd 941
Cdd:COG4717     74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPERLEE--- 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  942 LLKREQETAKAAWEKAALvpevqvDTTLVNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKATDAESKING 1021
Cdd:COG4717    151 LEERLEELRELEEELEEL------EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224

                          170       180
                   ....*....|....*....|....*....
gi 1002244077 1022 LTNTMLSLQEKLTNMELENQVLRQQALFR 1050
Cdd:COG4717    225 LEEELEQLENELEAAALEERLKEARLLLL 253

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

886-1046

2.94e-05

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 2.94e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  886 LQAAKNKLEKQVEELTWRLQLEKRMRVDMEEAKSQEN---KKLQQKLQELELQSnetkDLLKREQETAKAAWEKaaLVPE 962
Cdd:TIGR04523  417 LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEliiKNLDNTRESLETQL----KVLSRSINKIKQNLEQ--KQKE 490

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  963 VQVDTTLVNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKATDAESKINgltntmlSLQEKLTNMELENQV 1042
Cdd:TIGR04523  491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN-------KDDFELKKENLEKEI 563


                   ....
gi 1002244077 1043 LRQQ 1046
Cdd:TIGR04523  564 DEKN 567

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

885-1036

3.12e-05

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 3.12e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  885 ALQAAKNKLEKQVEELTwrlqlEKRMRVDMEEAKSQENKKLQQKLQELElQSNETKDLLKREQETA-----KAAWEKAAL 959
Cdd:TIGR04523  528 KLESEKKEKESKISDLE-----DELNKDDFELKKENLEKEIDEKNKEIE-ELKQTQKSLKKKQEEKqelidQKEKEKKDL 601

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  960 VPEVQVDTTLVNELT-------AENEKLKTLVASLETKIDETEQRF----DEVKKARE---ELLKKATDAESKINGLTNT 1025
Cdd:TIGR04523  602 IKEIEEKEKKISSLEkelekakKENEKLSSIIKNIKSKKNKLKQEVkqikETIKEIRNkwpEIIKKIKESKTKIDDIIEL 681

                          170
                   ....*....|....*....
gi 1002244077 1026 M--------LSLQEKLTNM 1036
Cdd:TIGR04523  682 MkdwlkelsLHYKKYITRM 700

PspA

COG1842

Phage shock protein A [Transcription, Signal transduction mechanisms];

910-1047

3.59e-05

Phage shock protein A [Transcription, Signal transduction mechanisms];

Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 46.74 E-value: 3.59e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  910 MRVDMEEAKSQ------ENKKLQQKLQELELQSNE----TKDLLKREQETA--KAAWEKAALVPEVQVDTTLVNELTAEN 977
Cdd:COG1842     35 MEEDLVEARQAlaqviaNQKRLERQLEELEAEAEKweekARLALEKGREDLarEALERKAELEAQAEALEAQLAQLEEQV 114

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002244077  978 EKLKTLVASLETKIDETEQRFDEVkKARE---ELLKKATDAESKINGlTNTMLSLQekltnmELENQVLRQQA 1047
Cdd:COG1842    115 EKLKEALRQLESKLEELKAKKDTL-KARAkaaKAQEKVNEALSGIDS-DDATSALE------RMEEKIEEMEA 179

Smc

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...

869-1048

3.74e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 3.74e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  869 ARRE--LRKLKmAAKE--------TGALQAAKNKLEKQVE------ELTWRLQ-LEKRMRVDMEEAKSQENKKLQQKLQE 931
Cdd:COG1196    172 ERKEeaERKLE-ATEEnlerlediLGELERQLEPLERQAEkaeryrELKEELKeLEAELLLLKLRELEAELEELEAELEE 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  932 LELQSNEtkdlLKREQETAKAAWEKAALvpEVQVDTTLVNELTAENEKLKTLVASLETKID-------ETEQRFDEVKKA 1004
Cdd:COG1196    251 LEAELEE----LEAELAELEAELEELRL--ELEELELELEEAQAEEYELLAELARLEQDIArleerrrELEERLEELEEE 324

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1002244077 1005 REELLKKATDAESKINGLTNTMLSLQEKLTNMELENQVLRQQAL 1048
Cdd:COG1196    325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

PspA_IM30

pfam04012

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...

867-1041

3.81e-05

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.

Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 46.60 E-value: 3.81e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  867 RLARRELRKLKMAAKETGALQAaknKLEKQVEELTwrlqlekrmrvdmeeaksQENKKLQQKLQELelqsnetkdLLKRE 946
Cdd:pfam04012   32 RDMQSELVKARQALAQTIARQK---QLERRLEQQT------------------EQAKKLEEKAQAA---------LTKGN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  947 QETAKAAWEKAALVPEVQVD-TTLVNELTAENEKLKTLVASLETKIDETEQRFDEVK------KAREELlkKATDAESKI 1019
Cdd:pfam04012   82 EELAREALAEKKSLEKQAEAlETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKarlkaaKAQEAV--QTSLGSLST 159

                          170       180
                   ....*....|....*....|..
gi 1002244077 1020 NGLTNTMLSLQEKLTNMELENQ 1041
Cdd:pfam04012  160 SSATDSFERIEEKIEEREARAD 181

GAS

pfam13851

Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...

891-1046

3.99e-05

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.

Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 46.44 E-value: 3.99e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  891 NKLEKQVEELTWRlqlEKRMRVDMEEAkSQENKKLQQKLQELELQSNEtkdlLKREQETAKAawEKAALvpevqvdttlv 970
Cdd:pfam13851   29 KSLKEEIAELKKK---EERNEKLMSEI-QQENKRLTEPLQKAQEEVEE----LRKQLENYEK--DKQSL----------- 87

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002244077  971 NELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKatdaeskingLTNTMLSLQEKltnMELENQVLRQQ 1046
Cdd:pfam13851   88 KNLKARLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDK----------FEAAIQDVQQK---TGLKNLLLEKK 150

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

867-1048

4.48e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 4.48e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  867 RLARRELRKLKMAAKETGALQAAKNKLEKQVEELtwrlqlekrmrvdmeEAKSQENKKLQQKLQELELQSNETKDLLKRE 946
Cdd:COG4372      7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFEL---------------DKLQEELEQLREELEQAREELEQLEEELEQA 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  947 QETAKAAWEK---------AALVPEVQVDTTLvNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKATDAES 1017
Cdd:COG4372     72 RSELEQLEEEleelneqlqAAQAELAQAQEEL-ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREE 150

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1002244077 1018 KINGLTNTMLSLQEKLTNMELENQVLRQQAL 1048
Cdd:COG4372    151 ELKELEEQLESLQEELAALEQELQALSEAEA 181

PRK03918

DNA double-strand break repair ATPase Rad50;

870-1039

4.63e-05

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 4.63e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  870 RRELRKLKMAAKETGALQAAKNKLEKQVEEltwrlqLEKRMRvdMEEAKSQEnkkLQQKLQELELQSNETKDLLKREQET 949
Cdd:PRK03918   220 REELEKLEKEVKELEELKEEIEELEKELES------LEGSKR--KLEEKIRE---LEERIEELKKEIEELEEKVKELKEL 288

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  950 AKAAWEKAALVPEVQVDTTLVNELTAENEKLKTLVASLETKIDETEQ---RFDEVKKAREELLKKATDAE------SKIN 1020
Cdd:PRK03918   289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELEerhelyEEAK 368

                          170
                   ....*....|....*....
gi 1002244077 1021 GLTNTMLSLQEKLTNMELE 1039
Cdd:PRK03918   369 AKKEELERLKKRLTGLTPE 387

Myosin_tail_1

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

880-1046

5.38e-05

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.86 E-value: 5.38e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  880 AKETGA-LQAAKNKLEKQVEELtwrlqlekRMRVDMEEAKSQ----ENKKLQQKLQELELQSNETK-------------- 940
Cdd:pfam01576   59 AEEMRArLAARKQELEEILHEL--------ESRLEEEEERSQqlqnEKKKMQQHIQDLEEQLDEEEaarqklqlekvtte 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  941 --------DLLKREQETAKAAWEKAALVPEVQVDTTlvnELTAENEKLKTLvASLETK----IDETEQRFDEVKKAREEL 1008
Cdd:pfam01576  131 akikkleeDILLLEDQNSKLSKERKLLEERISEFTS---NLAEEEEKAKSL-SKLKNKheamISDLEERLKKEEKGRQEL 206

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1002244077 1009 --LKKATDAESKingltntmlSLQEKLTNMELENQVLRQQ 1046
Cdd:pfam01576  207 ekAKRKLEGEST---------DLQEQIAELQAQIAELRAQ 237

YhaN

COG4717

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

865-1046

5.94e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 5.94e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  865 RGRLARRELRKLKMAAKETGALQAAKNKLEKQVEELtwrLQLEKRMrvdmeEAKSQENKKLQQKLQELELQSNETKDLLK 944
Cdd:COG4717     62 QGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL---EELEEEL-----EELEAELEELREELEKLEKLLQLLPLYQE 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  945 REQETAKAAWEKA---ALVPEVQVDTTLVNELTAENEKLKTLVASLETKID----ETEQRFDEVKKAREELLKKATDAES 1017
Cdd:COG4717    134 LEALEAELAELPErleELEERLEELRELEEELEELEAELAELQEELEELLEqlslATEEELQDLAEELEELQQRLAELEE 213

                          170       180
                   ....*....|....*....|....*....
gi 1002244077 1018 KINGLTNTMLSLQEKLTNMELENQVLRQQ 1046
Cdd:COG4717    214 ELEEAQEELEELEEELEQLENELEAAALE 242

PRK03918

DNA double-strand break repair ATPase Rad50;

906-1047

6.90e-05

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 6.90e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  906 LEKRMRVDMEEAKSQEN--KKLQQKLQELELQSNETKDLLKREQETAKAAWEKAALVPEVQVDTTLVNELTAENEKLKTL 983
Cdd:PRK03918   174 IKRRIERLEKFIKRTENieELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002244077  984 VASLETKIDETEQRFDEVKKAREELLKKATDAEsKINGLTNTMLSLQE-------KLTNMELENQVLRQQA 1047
Cdd:PRK03918   254 KRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEfyeeyldELREIEKRLSRLEEEI 323

Myosin_tail_1

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

865-1054

7.68e-05

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.48 E-value: 7.68e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  865 RGRLARRE------LRKLKMAAKETGALQAAKNKLEKQVEELTWRLQLEKRMRVDMEEAKSQENKKLQQKLQELE--LQS 936
Cdd:pfam01576  235 RAQLAKKEeelqaaLARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdtLDT 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  937 NETKDLL--KREQETA--KAAWEKAALVPEVQVD------TTLVNELT---------------------AENEKLKTLVA 985
Cdd:pfam01576  315 TAAQQELrsKREQEVTelKKALEEETRSHEAQLQemrqkhTQALEELTeqleqakrnkanlekakqaleSENAELQAELR 394

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  986 SLETKIDETEQ--------------RFDEVKKAREELLKKATDAESKINGLTNTMLSLQEKLTNM-----ELENQVLRQQ 1046
Cdd:pfam01576  395 TLQQAKQDSEHkrkklegqlqelqaRLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLskdvsSLESQLQDTQ 474


                   ....*...
gi 1002244077 1047 ALFRSPVR 1054
Cdd:pfam01576  475 ELLQEETR 482

SCP-1

pfam05483

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...

885-1047

8.77e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.41 E-value: 8.77e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  885 ALQAAKNKLEKQVEELTWRLQLEKRMRVDME---EAKSQENKKLQQKLQELELQ-SNETKDLL--KREQETAKAAWEKAA 958
Cdd:pfam05483  461 AIKTSEEHYLKEVEDLKTELEKEKLKNIELTahcDKLLLENKELTQEASDMTLElKKHQEDIIncKKQEERMLKQIENLE 540

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  959 lvpevQVDTTLVNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKATDAESKINGLTNTMLSLQEKLTNMEL 1038
Cdd:pfam05483  541 -----EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615


                   ....*....
gi 1002244077 1039 ENQVLRQQA 1047
Cdd:pfam05483  616 ENKALKKKG 624

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

884-1060

1.26e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 1.26e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  884 GALQAAKNKLEKQVEeltwRLQLEKRMRvDMEEAKSQENKKLQQKLQELELQSNETKDLLKREQETAK----AAWEKAAL 959
Cdd:TIGR02168  664 GSAKTNSSILERRRE----IEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisaLRKDLARL 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  960 VPEVQVDTTLVNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKATDAESKINGLTNTMLSLQEKL--TNME 1037
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtlLNEE 818

                          170       180
                   ....*....|....*....|...
gi 1002244077 1038 LENQVLRQQALFRSPVRTIPENT 1060
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLE 841

SMC_prok_A

TIGR02169

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

854-1047

1.38e-04

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 1.38e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  854 KKAAITTQCAWRGRLA--RRELRKLKMA----AKETGALQAAKNKLEKQVEELT--WRLQLEKRMR---------VDMEE 916
Cdd:TIGR02169  232 KEALERQKEAIERQLAslEEELEKLTEEiselEKRLEEIEQLLEELNKKIKDLGeeEQLRVKEKIGeleaeiaslERSIA 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  917 AKSQENKKLQQKLQELELQSNETK---DLLKREQETAKAawEKAALvpevqvdttlvnelTAENEKLKTLVASLETKIDE 993
Cdd:TIGR02169  312 EKERELEDAEERLAKLEAEIDKLLaeiEELEREIEEERK--RRDKL--------------TEEYAELKEELEDLRAELEE 375

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1002244077  994 TEQRFDEVKKAREELLKKATDAESKINGLTNTMLSLQEKLTNMELENQVLRQQA 1047
Cdd:TIGR02169  376 VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI 429

PTZ00121

MAEBL; Provisional

851-1018

1.85e-04

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.85e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  851 MGLKKAAITTQcAWRGRLarRELRKLKMAAKETGALQAAKNKLEKQVEELTWRLQLEKRMRVDMEEAKSQENKKLQQKLQ 930
Cdd:PTZ00121  1578 MALRKAEEAKK-AEEARI--EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  931 ELELQSNETKDLLKREQETAKAAWEkaalVPEVQVDTTLVNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLK 1010
Cdd:PTZ00121  1655 AEEENKIKAAEEAKKAEEDKKKAEE----AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKI 1730


                   ....*...
gi 1002244077 1011 KATDAESK 1018
Cdd:PTZ00121  1731 KAEEAKKE 1738

COG4913

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

874-1016

1.97e-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: 1.97e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  874 RKLKMAAKETGALQAAKNKLEKQVEEL-TWRLQLEKR------------MRVDMEEAKSQENkKLQQKLQELElQSNETK 940
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEALeAELDALQERrealqrlaeyswDEIDVASAEREIA-ELEAELERLD-ASSDDL 687

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002244077  941 DLLKREQETAKAAWEkaalvpevqvdttlvnELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKATDAE 1016
Cdd:COG4913    688 AALEEQLEELEAELE----------------ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

870-1046

2.01e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 2.01e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  870 RRELRKLKM---AAKETGALQAAKNKLEKQVEELTWRLQLEKRMRVDMEEAKSQ-ENKKLQQKLQELELQSNETKDllkr 945
Cdd:TIGR02168  199 ERQLKSLERqaeKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEeELEELTAELQELEEKLEELRL---- 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  946 eqetakaawekaalvpEVQVDTTLVNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKATDAESKINgltnt 1025
Cdd:TIGR02168  275 ----------------EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD----- 333

                          170       180
                   ....*....|....*....|.
gi 1002244077 1026 mlSLQEKLTNMELENQVLRQQ 1046
Cdd:TIGR02168  334 --ELAEELAELEEKLEELKEE 352

Smc

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...

865-1018

2.08e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 2.08e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  865 RGRLARRELRKLKMAAKETGALQAAKNKLEKQVEELtwrlQLEKRMRVDMEEAKSQENKKLQQKLQELELQSNETKDLLK 944
Cdd:COG1196    659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELE----LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  945 REQETAKAAWEKAALVPEVQVDTTLVNEltaenEKLKTLVASLETKI--------------DETEQRFDE-------VKK 1003
Cdd:COG1196    735 EELLEELLEEEELLEEEALEELPEPPDL-----EELERELERLEREIealgpvnllaieeyEELEERYDFlseqredLEE 809

                          170
                   ....*....|....*..
gi 1002244077 1004 AREELLK--KATDAESK 1018
Cdd:COG1196    810 ARETLEEaiEEIDRETR 826

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

922-1046

2.12e-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: 44.53 E-value: 2.12e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  922 NKKLQQ--KLQELELQSNETKDLLKR-EQETAKAAWEKAALVPEVQVDTTLVNELTAENEKLKTLVASLETKIDETEQRF 998
Cdd:COG1579      3 PEDLRAllDLQELDSELDRLEHRLKElPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1002244077  999 DEVKKARE--ELLKKATDAESKINGLTNTMLSLQEKLTNMELENQVLRQQ 1046
Cdd:COG1579     83 GNVRNNKEyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE 132

PRK03918

DNA double-strand break repair ATPase Rad50;

867-1046

2.26e-04

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 2.26e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  867 RLARRELRKLKMAAKETGALQAAKNKLEKQVEELTWRLQ----LEKRMRVDMEEAKSQENKK--LQQKLQELELQSNEtk 940
Cdd:PRK03918   511 KLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEkleeLKKKLAELEKKLDELEEELaeLLKELEELGFESVE-- 588

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  941 DLLKREQETAKAAWEKAALVPEVQvdttlvnELTAENEKLKtlvaSLETKIDETEQRFDEVKKAREELLKKATDAESKIN 1020
Cdd:PRK03918   589 ELEERLKELEPFYNEYLELKDAEK-------ELEREEKELK----KLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1002244077 1021 -----GLTNTMLSLQEKLTNMELENQVLRQQ 1046
Cdd:PRK03918   658 eeeyeELREEYLELSRELAGLRAELEELEKR 688

Myosin_tail_1

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

886-1018

2.28e-04

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.94 E-value: 2.28e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  886 LQAAKNKLEKQVEELTWRLQLEKRMRVDMEEAKSQ---ENKKLQQKLQELELQSNETKDLLKR------------EQETA 950
Cdd:pfam01576  178 LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKlegESTDLQEQIAELQAQIAELRAQLAKkeeelqaalarlEEETA 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  951 ------KAAWEKAALVPEVQVDttLVNELTAEN----------EKLKTLVASLETKIDETEQRfDEVKKARE---ELLKK 1011
Cdd:pfam01576  258 qknnalKKIRELEAQISELQED--LESERAARNkaekqrrdlgEELEALKTELEDTLDTTAAQ-QELRSKREqevTELKK 334


                   ....*..
gi 1002244077 1012 ATDAESK 1018
Cdd:pfam01576  335 ALEEETR 341

PRK03918

DNA double-strand break repair ATPase Rad50;

892-1039

2.30e-04

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 2.30e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  892 KLEKQVEELTWRLQLEKRMRVDMEEAKsQENKKLQQKLQELELQSNETKDLLKREQETAKAAWEKAALVPEVQVDTTLVN 971
Cdd:PRK03918   218 ELREELEKLEKEVKELEELKEEIEELE-KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI 296

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002244077  972 ELTAENEKLKtlvaSLETKIDETEQRFDEVKKAREELLKKATDAESKINGLTNTMLSLQEKLtnMELE 1039
Cdd:PRK03918   297 KLSEFYEEYL----DELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL--EELE 358

Motor_domain

cd01363

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...

593-632

2.51e-04

Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 43.49 E-value: 2.51e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1002244077  593 EESTKSTKFTSI-----GS-SFKQQLQALLETLSSVEPHYIRCIKP 632
Cdd:cd01363    125 ENSSRFGKFIEIlldiaGFeIINESLNTLMNVLRATRPHFVRCISP 170

PTZ00121

MAEBL; Provisional

817-1016

3.28e-04

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 3.28e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  817 RGMAARKELQYRQQTKAAVIIQSYCRSYLAHSQYMGLKKAAittqcawRGRLARRELRKLKMAAKETGALQAAKNKLEKQ 896
Cdd:PTZ00121  1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE-------EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  897 VEELTwRLQLEKRMRVDMEEAKSQENKKLQQKLQELELQSNETKDLLKREQETAKAawekaalvpevqvdttlVNELTAE 976
Cdd:PTZ00121  1649 AEELK-KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK-----------------AEELKKK 1710

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1002244077  977 NEKLKTLVASLETKIDETEQRFDEVKKAREELLKKATDAE 1016
Cdd:PTZ00121  1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750

PTZ00121

MAEBL; Provisional

869-1018

3.50e-04

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 3.50e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  869 ARRELRKLKMAAKETGALQAAKnklEKQVEELTWRLQLEKRMRVdmEEAKSQENKKLQ-QKLQELELQSNETKDLLKREQ 947
Cdd:PTZ00121  1569 AKKAEEDKNMALRKAEEAKKAE---EARIEEVMKLYEEEKKMKA--EEAKKAEEAKIKaEELKKAEEEKKKVEQLKKKEA 1643

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002244077  948 ETAKAAwekaalvpevqvdttlvNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELlKKATDAESK 1018
Cdd:PTZ00121  1644 EEKKKA-----------------EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE-KKAAEALKK 1696

SMC_prok_A

TIGR02169

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

892-1039

4.07e-04

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 4.07e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  892 KLEKQVEELtwrlqleKRMRVDMEEAKSQENKKLQQ--KLQELELQSNETKDLLKREQETakAAWEKAAlvpevqvdttL 969
Cdd:TIGR02169  171 KKEKALEEL-------EEVEENIERLDLIIDEKRQQleRLRREREKAERYQALLKEKREY--EGYELLK----------E 231

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002244077  970 VNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKATDAESKINGLT-NTMLSLQEKLTNMELE 1039
Cdd:TIGR02169  232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGeEEQLRVKEKIGELEAE 302

PRK12704

phosphodiesterase; Provisional

864-1012

5.16e-04

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 5.16e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  864 WRGRLARRELRKLKMAAKETgaLQAAKNK---------LEKQVEELTWRLQLEKRMRVDMEEAKSQEnKKLQQKLQELEl 934
Cdd:PRK12704    24 VRKKIAEAKIKEAEEEAKRI--LEEAKKEaeaikkealLEAKEEIHKLRNEFEKELRERRNELQKLE-KRLLQKEENLD- 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  935 qsNETKDLLKREQETAKaawekaalvpevqvdttLVNELTAENEKLKTLVASLETKIDETEQRFDEV-----KKAREELL 1009
Cdd:PRK12704   100 --RKLELLEKREEELEK-----------------KEKELEQKQQELEKKEEELEELIEEQLQELERIsgltaEEAKEILL 160


                   ...
gi 1002244077 1010 KKA 1012
Cdd:PRK12704   161 EKV 163

GumC

COG3206

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];

832-1056

5.23e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 5.23e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  832 KAAVIIQSYCRSYLAhsQYMGLKKAAITTQCAW--------RGRL--ARRELRKLK-------------MAAKETGALQA 888
Cdd:COG3206    149 LAAAVANALAEAYLE--QNLELRREEARKALEFleeqlpelRKELeeAEAALEEFRqknglvdlseeakLLLQQLSELES 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  889 AKNKLEKQVEELTWRL-QLEKRMRVDMEEA----KSQENKKLQQKLQELELQ-SNETKDL---------LKREQETAKAA 953
Cdd:COG3206    227 QLAEARAELAEAEARLaALRAQLGSGPDALpellQSPVIQQLRAQLAELEAElAELSARYtpnhpdviaLRAQIAALRAQ 306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  954 WEKAAlvpevqvdTTLVNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKATDAESKinglTNTMLSLQEKL 1033
Cdd:COG3206    307 LQQEA--------QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVA----RELYESLLQRL 374

                          250       260
                   ....*....|....*....|...
gi 1002244077 1034 TNMELenqvlrQQALFRSPVRTI 1056
Cdd:COG3206    375 EEARL------AEALTVGNVRVI 391

PRK02224

DNA double-strand break repair Rad50 ATPase;

879-1047

5.68e-04

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 5.68e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  879 AAKETGALQAAKNKLEKQVEELTWRLQLEKRMRVDMEEAKSQENKKL---QQKLQELELQSNETKDLlkreQET-AKAAW 954
Cdd:PRK02224   197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLeehEERREELETLEAEIEDL----RETiAETER 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  955 EKAALVPEVQVDTTLVNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKATDAESKINGLTNTMLSLQEKLT 1034
Cdd:PRK02224   273 EREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDAD 352

                          170
                   ....*....|...
gi 1002244077 1035 NMELENQVLRQQA 1047
Cdd:PRK02224   353 DLEERAEELREEA 365

CALCOCO1

pfam07888

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...

859-1046

7.24e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.

Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 7.24e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  859 TTQCAWRGRlaRRELR----KLKMAAKETGALQAAKNKLEKQVEELTWRLQLEKRMRVDMEEAKSQENKKLQQKLQELEL 934
Cdd:pfam07888   66 RDREQWERQ--RRELEsrvaELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQ 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  935 QSNETKDLLKREQETAKAAwekaalvpevqvdttlVNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKATD 1014
Cdd:pfam07888  144 RVLERETELERMKERAKKA----------------GAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQ 207

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1002244077 1015 A---ESKINGLTNTMLSLQEKltnmELENQVLRQQ 1046
Cdd:pfam07888  208 VlqlQDTITTLTQKLTTAHRK----EAENEALLEE 238

PTZ00121

MAEBL; Provisional

853-1014

7.60e-04

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 7.60e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  853 LKKAAITTQCAWRGRLARRELRK---LKMAAKETGALQAAKNKLE--KQVEELtwRLQLEKRMRVDMEEAKSQENKKLQQ 927
Cdd:PTZ00121  1410 LKKAAAAKKKADEAKKKAEEKKKadeAKKKAEEAKKADEAKKKAEeaKKAEEA--KKKAEEAKKADEAKKKAEEAKKADE 1487

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  928 KLQELELQSNETKDLLKREQETAKAAWEKAAlvpevqVDTTLVNELTAENEKLKtlvaSLETKIDETEQRFDEVKKAREe 1007
Cdd:PTZ00121  1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKKA------EEAKKADEAKKAEEAKK----ADEAKKAEEKKKADELKKAEE- 1556


                   ....*..
gi 1002244077 1008 lLKKATD 1014
Cdd:PTZ00121  1557 -LKKAEE 1562

PRK03918

DNA double-strand break repair ATPase Rad50;

865-1034

8.19e-04

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 8.19e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  865 RGRLARRELRKLKMAAKETGALQAAKNKLEKQVEELTWRLQLEKRMRVDMEEAKsqENKKLQQKLQELELQ--SNETKDL 942
Cdd:PRK03918   450 RKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE--QLKELEEKLKKYNLEelEKKAEEY 527

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  943 LKREQETAKAAWEKAALVPEVQVDTTLVNELTAENEKLKTL---VASLETKI--------DETEQRFDEVKKAREELLkK 1011
Cdd:PRK03918   528 EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELeeeLAELLKELeelgfesvEELEERLKELEPFYNEYL-E 606

                          170       180
                   ....*....|....*....|...
gi 1002244077 1012 ATDAESKINGLTNTMLSLQEKLT 1034
Cdd:PRK03918   607 LKDAEKELEREEKELKKLEEELD 629

EnvC

COG4942

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

917-1012

8.41e-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: 43.60 E-value: 8.41e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  917 AKSQENKKLQQKLQELELQSNETKDLLKREQETAKAAWEKAALVpEVQVDTT--LVNELTAENEKLKTLVASLETKIDET 994
Cdd:COG4942     17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-ERRIAALarRIRALEQELAALEAELAELEKEIAEL 95

                           90
                   ....*....|....*...
gi 1002244077  995 EQRFDEVKKAREELLKKA 1012
Cdd:COG4942     96 RAELEAQKEELAELLRAL 113

tolA_full

TIGR02794

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...

885-1018

1.11e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]

Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.91 E-value: 1.11e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  885 ALQAAKNKLEKQVEELTWRLQLEKRMRvDMEEAKSQEnkklQQKLQELELQSNETKDLLKREQEtAKAAWEKAAlvpEVQ 964
Cdd:TIGR02794   73 LEQQAEEAEKQRAAEQARQKELEQRAA-AEKAAKQAE----QAAKQAEEKQKQAEEAKAKQAAE-AKAKAEAEA---ERK 143

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1002244077  965 VDTTLVNEltAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKATDAESK 1018
Cdd:TIGR02794  144 AKEEAAKQ--AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195

PTZ00121

MAEBL; Provisional

872-1016

1.12e-03

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 1.12e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  872 ELRKLKMAAKETGALQAAkNKLEKQVEELTWRLQLEKRmrvDMEEAKSQ-ENKKLQQKLQELELQSNETK---DLLKREQ 947
Cdd:PTZ00121  1300 EKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADAAKK---KAEEAKKAaEAAKAEAEAAADEAEAAEEKaeaAEKKKEE 1375

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002244077  948 ETAKA--AWEKAALVPEVQVDTTLVNELTAENEKLKTLVASlETKIDETEQRFDEVKKArEELLKKATDAE 1016
Cdd:PTZ00121  1376 AKKKAdaAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA-KKKADEAKKKAEEKKKA-DEAKKKAEEAK 1444

Myo5p-like_CBD_afadin

cd15471

cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and ...

1146-1396

1.16e-03

cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and Rap1 small G protein-binding protein, found in cadherin-based adherens junctions in epithelial cells, endothelial cells, and fibroblasts. It interacts with cell adhesion molecules and signaling molecules and plays a role in the formation of cell junctions, cell polarization, migration, survival, proliferation, and differentiation. Afadin is a multi domain protein, that contains beside a myosin5-like CBD, two Ras-associated domains, a forkhead-associated domain, a PDZ domain, three proline-rich domains, and an F-actin-binding domain.

Pssm-ID: 271255 Cd Length: 322 Bit Score: 42.68 E-value: 1.16e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1146 TSVFDRLIQIFGSAMQKHDSN-EDLAYWLSTSSTLLIMLQkslkaagssggtprkkpqtQSSFLGRmvFRSSNITVDMDL 1224
Cdd:cd15471     55 TAFLNKIASLIQQVIQEQRNIaGALAFWMANASELLNFLK-------------------QDRDLSA--FSVQAQDVLAEA 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1225 VRqieakypaflfkqqlTAFveglygmirdnvkkelsSLLSHAIQVPriMKASMVrgrSFGTSSLPrgrsfSNQGSYWQA 1304
Cdd:cd15471    114 VQ---------------SAF-----------------SYLVRCLQEE--LERSLP---AFLDSLVS-----LDDEPAIGD 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077 1305 IVDNLDELLKILQENCVPAIFMRKIFTQIFSFINAQLFNSLLV--RHECCSFSNGEYVKQGLAQMEVWCgevKPEYVGSA 1382
Cdd:cd15471    152 VLHTLSSAMRLLRRCRVNAALTIQLFSQLFHFINAWLFNSLVSnpDSGLCTRYWGKRLRQRLAHVEAWA---ERQGLELA 228

                          250
                   ....*....|....*
gi 1002244077 1383 LD-ELKHIRQAVGFL 1396
Cdd:cd15471    229 ADcHLDRIVQAANLL 243

PTZ00121

MAEBL; Provisional

869-1018

1.18e-03

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 1.18e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  869 ARRELRKLKMAAKETGALQAAKNKLEKQVEELtwRLQLEKRMRVDMEEAKSQENKKLQQKLQELELQSNETKDLLKREQE 948
Cdd:PTZ00121  1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKADAA--KKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE 1429

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002244077  949 TAKAawEKAALVPEVQVDTTLVNELTAENEKLKTLVASLE--------TKIDETEQRFDEVKKAREELLKKATDAESK 1018
Cdd:PTZ00121  1430 KKKA--DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEeakkadeaKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505

PDCD7

pfam16021

Programmed cell death protein 7;

853-948

1.28e-03

Programmed cell death protein 7;

Pssm-ID: 464979 [Multi-domain] Cd Length: 305 Bit Score: 42.79 E-value: 1.28e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  853 LKKAAITTQCAWRGRLAR-----------RELRKLKMAAK-------ETGALQAAKNKLEKQVEELTWRLQL----EKRM 910
Cdd:pfam16021  126 LKLAADAVLSEVRKKQADakrmldilrslEKLRKLRKEAArrkgikpESECDEAFESHLEKLRSVWKKRTEEysaeEKAL 205

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1002244077  911 RVDMEEAKSQENKKLQQKLQElelqsNETKDLLKREQE 948
Cdd:pfam16021  206 KVMLEGEQEEERKRRREKRQK-----KEREEFLQKKWE 238

PRK02224

DNA double-strand break repair Rad50 ATPase;

869-1049

1.43e-03

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.43e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  869 ARRELRKLKMAAKEtgALQAAKnKLEKQVEELTWRLQ-LEK-RMRVDMEEAKSQENKKLQQKLQELELQSNETKDLLKRE 946
Cdd:PRK02224   556 KREAAAEAEEEAEE--AREEVA-ELNSKLAELKERIEsLERiRTLLAAIADAEDEIERLREKREALAELNDERRERLAEK 632

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  947 QEtakaawEKAALvpEVQVDTTLVNELTAENEKLKTLVASLETKIDETEQRfdevkkaREELLKKATDAESKINGLTntm 1026
Cdd:PRK02224   633 RE------RKREL--EAEFDEARIEEAREDKERAEEYLEQVEEKLDELREE-------RDDLQAEIGAVENELEELE--- 694

                          170       180
                   ....*....|....*....|...
gi 1002244077 1027 lSLQEKLTnmELENQVLRQQALF 1049
Cdd:PRK02224   695 -ELRERRE--ALENRVEALEALY 714

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

886-1051

1.51e-03

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 1.51e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  886 LQAAKNKLEKQVEELTWRLQLE----KRMRVDMEEAKS----------QENKKLQQKLQELELQSNETKDLLKR----EQ 947
Cdd:TIGR02168  335 LAEELAELEEKLEELKEELESLeaelEELEAELEELESrleeleeqleTLRSKVAQLELQIASLNNEIERLEARlerlED 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  948 ETAKAAWEKAALVPEVQvdTTLVNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKATDAESKINGLTNTML 1027
Cdd:TIGR02168  415 RRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492

                          170       180
                   ....*....|....*....|....
gi 1002244077 1028 SLQEKLTNMELENQVLRQQALFRS 1051
Cdd:TIGR02168  493 SLERLQENLEGFSEGVKALLKNQS 516

Myosin_tail_1

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

917-1043

1.66e-03

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 1.66e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  917 AKSQENKKLQQKLQELElqsNETKDLLKREQETAKaawEKAALVPEVQVDTTLVNE-------LTAENEKLKTLVASLET 989
Cdd:pfam01576    9 AKEEELQKVKERQQKAE---SELKELEKKHQQLCE---EKNALQEQLQAETELCAEaeemrarLAARKQELEEILHELES 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002244077  990 KIDETEQR---------------------FDEVKKAREEL-LKKATdAESKINGLTNTMLSLQEKLTNMELENQVL 1043
Cdd:pfam01576   83 RLEEEEERsqqlqnekkkmqqhiqdleeqLDEEEAARQKLqLEKVT-TEAKIKKLEEDILLLEDQNSKLSKERKLL 157

COG4913

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

828-1046

1.74e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.74e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  828 RQQTKAAVIIQSYCRSYLAHSQYMGLKKAAITTQCAWRGRLARRELRK-LKMAAKETGALQAAKNKLEKQVEELTWRLQl 906
Cdd:COG4913    248 REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAeLEELRAELARLEAELERLEARLDALREELD- 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  907 ekRMRVDMEEAKSQENKKLQQKLQELELQSNETKDLLKREQETAKAAWEKAALVPEvqvdttlvnELTAENEKLKTLVAS 986
Cdd:COG4913    327 --ELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE---------EFAALRAEAAALLEA 395

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  987 LETKIDETEQrfdevkkAREELLKKATDAESKINGLTNTMLSLQEKLTNMELENQVLRQQ 1046
Cdd:COG4913    396 LEEELEALEE-------ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448

CAGE1

pfam15066

Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ...

891-1046

1.75e-03

Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.

Pssm-ID: 464481 Cd Length: 528 Bit Score: 42.90 E-value: 1.75e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  891 NKLEKQVEELtwrlqLEKRMRVDMEeaKSQENKKLQQkLQELelqSNETKdllKREQETAKaawEKAAL---VPEVQVDT 967
Cdd:pfam15066  366 NKLKENVEEL-----IEDKYNVILE--KNDINKTLQN-LQEI---LANTQ---KHLQESRK---EKETLqleLKKIKVNY 428

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  968 TLVNE--LTAENEKLKTLVASLET-----KIDETEQRFDEVKKARE-------ELLKKATDAESKingltnTMLSLQEKL 1033
Cdd:pfam15066  429 VHLQEryITEMQQKNKSVSQCLEMdktlsKKEEEVERLQQLKGELEkattsalDLLKREKETREQ------EFLSLQEEF 502

                          170
                   ....*....|...
gi 1002244077 1034 TNMELENQVLRQQ 1046
Cdd:pfam15066  503 QKHEKENLEERQK 515

mukB

PRK04863

chromosome partition protein MukB;

912-1050

1.80e-03

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.80e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  912 VDMEEAKSQENKKLQQKLQELELQSNETKDLLKR-EQETAKAAWEKAALVPEVQVDTTLVNELTAENEKLK-TLVASLET 989
Cdd:PRK04863   977 AEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQaQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGvPADSGAEE 1056

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002244077  990 KI----DETEQRFDEVKKAREELLKKATDAESKINGLTNTMLSLQEKLTNM--ELENQVLRQQALFR 1050
Cdd:PRK04863  1057 RArarrDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMreQVVNAKAGWCAVLR 1123

ERM_helical

pfam20492

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...

890-1008

2.63e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.

Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.13 E-value: 2.63e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  890 KNKLEKQVEELTWRL-QLEKRMRVDMEEAKSQENK--KLQQKLQELElqsnETKDLLKREQETAKAAWEKAALVPEVQVD 966
Cdd:pfam20492    1 REEAEREKQELEERLkQYEEETKKAQEELEESEETaeELEEERRQAE----EEAERLEQKRQEAEEEKERLEESAEMEAE 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1002244077  967 T--TLVNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREEL 1008
Cdd:pfam20492   77 EkeQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120

PRK03918

DNA double-strand break repair ATPase Rad50;

871-1012

2.75e-03

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 2.75e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  871 RELRKLKMAAKETGALQAAKNKLEKQVEELTWRL---------QLEKRMRvDME-------EAKSQEnKKLQQKLQELEL 934
Cdd:PRK03918   546 KELEKLEELKKKLAELEKKLDELEEELAELLKELeelgfesveELEERLK-ELEpfyneylELKDAE-KELEREEKELKK 623

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  935 QSNETKDLLKREQETAKAAWEKAALVPEVQVD-------------TTLVNE---LTAENEKLKTLVASLETKIDETEQRF 998
Cdd:PRK03918   624 LEEELDKAFEELAETEKRLEELRKELEELEKKyseeeyeelreeyLELSRElagLRAELEELEKRREEIKKTLEKLKEEL 703

                          170
                   ....*....|....*.
gi 1002244077  999 DEVKKAREEL--LKKA 1012
Cdd:PRK03918   704 EEREKAKKELekLEKA 719

PRK03918

DNA double-strand break repair ATPase Rad50;

870-1050

2.99e-03

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 2.99e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  870 RRELRKLKMAAKETGALQAAKNKLEKQVEELTWRLQLEKRMRVDMEEAKSQENKKlqqklqelelqSNETKDLLKREQET 949
Cdd:PRK03918   327 EERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRL-----------TGLTPEKLEKELEE 395

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  950 AKAAWEkaalvpevqvdttlvnELTAENEKLKTLVASLETKIDETEQRFDEVKKA---------------REELLKKATd 1014
Cdd:PRK03918   396 LEKAKE----------------EIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrelteehRKELLEEYT- 458

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1002244077 1015 aeSKINGLTNTMLSLQEKLTNM-----ELENQVLRQQALFR 1050
Cdd:PRK03918   459 --AELKRIEKELKEIEEKERKLrkelrELEKVLKKESELIK 497

COG4913

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

887-1019

3.52e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 3.52e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  887 QAAKNKLEKQVEELTWRL-QLEKRMrvdmeeaksQENKKLQQKLQELELQSNETKDLLKREQETAKAAWEKAALvpEVQV 965
Cdd:COG4913    609 RAKLAALEAELAELEEELaEAEERL---------EALEAELDALQERREALQRLAEYSWDEIDVASAEREIAEL--EAEL 677

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002244077  966 DttlvnELTAENEKLKTL---VASLETKIDETEQRFDEVKKAREELLKKATDAESKI 1019
Cdd:COG4913    678 E-----RLDASSDDLAALeeqLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729

Spc7

smart00787

Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...

902-1059

3.64e-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: 41.16 E-value: 3.64e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077   902 WRLQLEKRMRVDMEEaksqENKKLQQKLQELELQSNETKDLLKREQEtakaawEKAALVPEVQVDTTLVNELtaeNEKLK 981
Cdd:smart00787  137 WRMKLLEGLKEGLDE----NLEGLKEDYKLLMKELELLNSIKPKLRD------RKDALEEELRQLKQLEDEL---EDCDP 203

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002244077   982 TLVASLETKIDETEQRFDEVKKAREELLKKATDAESKINGLTNTMLSLQEKLtnMELENQVLRQQALFRSPVRTIPEN 1059
Cdd:smart00787  204 TELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEI--AEAEKKLEQCRGFTFKEIEKLKEQ 279

DUF4355

pfam14265

Domain of unknown function (DUF4355); This family of proteins is found in bacteria and viruses. ...

877-1010

3.80e-03

Domain of unknown function (DUF4355); This family of proteins is found in bacteria and viruses. Proteins in this family are typically between 180 and 214 amino acids in length.

Pssm-ID: 405026 [Multi-domain] Cd Length: 119 Bit Score: 38.83 E-value: 3.80e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  877 KMAAKetgALQAAKNKLEKQVEEltwrLQLEKRMRVDM--EEAKSQENKKLQQKLQELElQSNETKDLLKreqETAKAAW 954
Cdd:pfam14265    6 KIVAK---ALATKKNNLEKEIED----EIKEAKKLAKMnaEEKAKYELEKLQKELEEEK-AELARKELKA---EARKMLS 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002244077  955 EKaalvpevQVDTTLVNELTAENEklKTLVASLETKIDETEqrfDEVKKAREELLK 1010
Cdd:pfam14265   75 EK-------GIPTELLDFVVGADA--ETTKKNLETFEDLFN---KAVEKAVEEKLK 118

smart00015

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...

853-874

4.00e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.

Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 36.15 E-value: 4.00e-03

                            10        20
                    ....*....|....*....|..
gi 1002244077   853 LKKAAITTQCAWRGRLARRELR 874
Cdd:smart00015    2 LTRAAIIIQAAWRGYLARKRYK 23

ZapB

COG3074

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...

924-1001

4.15e-03

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 442308 [Multi-domain] Cd Length: 79 Bit Score: 37.64 E-value: 4.15e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002244077  924 KLQQKLQELElqsnETKDLLKREQETAKAawEKAALVPEVQVDTTLVNELTAENEKLKTLVASLETKIDETEQRFDEV 1001
Cdd:COG3074      8 ELEAKVQQAV----DTIELLQMEVEELKE--KNEELEQENEELQSENEELQSENEQLKTENAEWQERIRSLLGKIDEV 79

YhaN

COG4717

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

885-1046

4.72e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 4.72e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  885 ALQAAKNKLEK-QVEELTWRLQLEKRMRVDMEEAKSQ--ENKKLQQKLQELElqsnETKDLLKREQETAKAAWEKAALVP 961
Cdd:COG4717     50 RLEKEADELFKpQGRKPELNLKELKELEEELKEAEEKeeEYAELQEELEELE----EELEELEAELEELREELEKLEKLL 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  962 EVQVDTTLVNELTAENEKLKTLVASLETKIDETEQRFDEVKKAREELLKKATDAESKINGLTNTML----SLQEKLTNME 1037
Cdd:COG4717    126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEeelqDLAEELEELQ 205


                   ....*....
gi 1002244077 1038 LENQVLRQQ 1046
Cdd:COG4717    206 QRLAELEEE 214

sbcc

TIGR00618

exonuclease SbcC; All proteins in this family for which functions are known are part of an ...

825-1050

5.37e-03

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: 41.49 E-value: 5.37e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  825 LQYRQQTKAAVIIQSYCRSYLAHSQ------YMGLKKAAITTQCAWRGRLARRELRKlkMAAKETGALQAAKNKLEKQVE 898
Cdd:TIGR00618  138 LDYKTFTRVVLLPQGEFAQFLKAKSkekkelLMNLFPLDQYTQLALMEFAKKKSLHG--KAELLTLRSQLLTLCTPCMPD 215

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  899 ELTWRLQLEKRMRVDMEEAKSQENKKLQQKLQELELQSNEtkdlLKREQETAKAAWEKAALVPEVQVDTTLVNELTAENE 978
Cdd:TIGR00618  216 TYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQ----LKKQQLLKQLRARIEELRAQEAVLEETQERINRARK 291

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002244077  979 KLKTL-----VASLETKIDETEQRFDEVKKAREELLKKATDAESKINGLTNTMLSLQEKLTNMELENQVLRQQALFR 1050
Cdd:TIGR00618  292 AAPLAahikaVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR 368

WEMBL

pfam05701

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...

867-1046

5.68e-03

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".

Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.17 E-value: 5.68e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  867 RLARRELRKLK-----------MAAKETGALQAAKNKLEKQVEELTWRL-----QL-----------EKRMRVDM--EEA 917
Cdd:pfam05701  141 KSVKEELESLRkeyaslvserdIAIKRAEEAVSASKEIEKTVEELTIELiatkeSLesahaahleaeEHRIGAALarEQD 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244077  918 KSQENKKLQQ---KLQELELQSNETKDlLKREQETAKA--AWEKAALVPEVQvdtTLVNELTAENEKLKTLVASLETKID 992
Cdd:pfam05701  221 KLNWEKELKQaeeELQRLNQQLLSAKD-LKSKLETASAllLDLKAELAAYME---SKLKEEADGEGNEKKTSTSIQAALA 296

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1002244077  993 ETEQRFDEVKKAREellkKATDaesKINGLTNTMLSLQEKLTNMELENQVLRQQ 1046
Cdd:pfam05701  297 SAKKELEEVKANIE----KAKD---EVNCLRVAAASLRSELEKEKAELASLRQR 343

Mplasa_alph_rch